|
Name |
Accession |
Description |
Interval |
E-value |
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-256 |
7.40e-173 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 476.81 E-value: 7.40e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQ 241
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|....*
gi 499585766 242 IMREPVAGTPMCIVE 256
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-254 |
1.63e-129 |
|
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: 367.06 E-value: 1.63e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQ 241
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|...
gi 499585766 242 IMREPVAGTPMCI 254
Cdd:COG1120 241 VIEDPVTGRPLVL 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-254 |
2.41e-93 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 275.04 E-value: 2.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGV 92
Cdd:COG4604 11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRSPHNSlwGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:COG4604 91 TVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 173 SHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQImrEPVAGTP 251
Cdd:COG4604 169 KHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV--EEIDGKR 246
|
...
gi 499585766 252 MCI 254
Cdd:COG4604 247 ICV 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-254 |
1.91e-88 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 263.39 E-value: 1.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLP 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQI 242
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
250
....*....|..
gi 499585766 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 |
4.79e-82 |
|
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: 243.88 E-value: 4.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 5 KAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 vlpipegvsvrqlvaygrsphnslwgrlsgadqhsvdqALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-252 |
1.38e-81 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 245.41 E-value: 1.38e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLP 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAYGRSPHnslwGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQ------- 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVF 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*.
gi 499585766 237 DVQVQIMREPVAGTPM 252
Cdd:COG4559 238 GADLRVLAHPEGGCPQ 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
7.62e-80 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 240.76 E-value: 7.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSanelaRKVA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLPIPEG--VSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRmVTCGAPSDVLTAELVCQVFDV 238
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTPENLSRAYGG 237
|
....*..
gi 499585766 239 QVQIMRE 245
Cdd:COG1121 238 PVALLAH 244
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-255 |
1.49e-77 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 235.45 E-value: 1.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQL 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 178 LLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQIMREPVAGTPMCIV 255
Cdd:PRK10575 186 VLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPVSFV 264
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-252 |
2.24e-76 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 232.35 E-value: 2.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGVSVRQLVAYGRSPhnslWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAA-- 159
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 160 ----IVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQ 234
Cdd:PRK13548 157 gpprWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
250
....*....|....*...
gi 499585766 235 VFDVQVQIMREPVAGTPM 252
Cdd:PRK13548 237 VYGADVLVQPHPETGAPL 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-251 |
3.19e-69 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 218.94 E-value: 3.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQV 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDART 240
|
250
....*....|.
gi 499585766 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 |
6.55e-66 |
|
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: 203.92 E-value: 6.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 5 KAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygkLSANELARKVAFLPQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPIPEG--VSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVM 212
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-230 |
5.42e-59 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 186.77 E-value: 5.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQ------VLPipegvSVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1122 81 FQnpddqlFAP-----TVEEDVAFG--PENL---GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-231 |
4.02e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 182.19 E-value: 4.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSAnELARKVAFLPQVLPIPEGV 92
Cdd:COG1131 10 YGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYVPQEPALYPDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:COG1131 89 TVRENLRF--------FARLYGLPRKEarerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499585766 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAEL 231
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-212 |
1.85e-55 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 176.66 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklsanelARKVAFLPQVLPIPEG 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 --VSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQAcRYADHLAVM 212
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-227 |
7.17e-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: 7.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSaNELARKVAFLP 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:COG4555 81 DERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-256 |
9.67e-54 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 174.26 E-value: 9.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARiLTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQLV 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYGRSPHNSlwgrlSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLD 171
Cdd:COG4138 91 ALHQPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQIMRepVAGTP 251
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE--VEGHR 243
|
....*
gi 499585766 252 MCIVE 256
Cdd:COG4138 244 WLIPT 248
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-216 |
2.14e-53 |
|
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: 171.88 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlpiPE--- 90
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN---PDdqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 -GVSVRQLVAYGrsPHNSLwgrLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03225 89 fGPTVEEEVAFG--LENLG---LPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499585766 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-255 |
3.93e-53 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 173.47 E-value: 3.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA--------GSLSLDGTAYGKLSANE 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 LARKVAFLPQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 155 AQ---------DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRMVTCGAPS 224
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|.
gi 499585766 225 DVLTAELVCQVFDVQVQIMREPvAGTPMCIV 255
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAG-DGVPPVIV 270
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-231 |
1.13e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.70 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---R 77
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 78 KVAFLPQVLPIPEGVSVRQLVAYGRSPHNSLW----GRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 154 LAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG3638 161 LVQEPKLILADEPVASLDpkTARQV--MDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238
|
.
gi 499585766 231 L 231
Cdd:COG3638 239 L 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-229 |
3.67e-49 |
|
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: 169.31 E-value: 3.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGY-----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSAN--- 73
Cdd:COG1123 259 PLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 74 ELARKVAFLPQvlpIPEG-----VSVRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMELDT-LAERPLSDLSGGQRQ 146
Cdd:COG1123 339 ELRRRVQMVFQ---DPYSslnprMTVGDIIAEPLRLH----GLLSRAERRErVAELLERVGLPPdLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
....
gi 499585766 226 VLTA 229
Cdd:COG1123 492 VFAN 495
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-232 |
6.89e-46 |
|
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: 153.36 E-value: 6.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-VA-- 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FlpQVLPIPEGVSVRQ---LVAYGRSPHNSLWGRLSGADQHSVDQA---LQRMELDTLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:cd03219 81 F--QIPRLFPELTVLEnvmVAAQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-221 |
7.17e-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: 152.67 E-value: 7.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLP 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAYGrsphnsLWGRLSGADQH--SVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG------LKLRGVPKAEIraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-236 |
7.56e-46 |
|
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: 153.49 E-value: 7.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGA-TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKV 79
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPIPEGVSVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 156 QDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDvLTAELV 232
Cdd:cd03256 161 QQPKLILADEPVASLDpaSSRQV--MDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVL 237
|
....
gi 499585766 233 CQVF 236
Cdd:cd03256 238 DEIY 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-217 |
2.85e-45 |
|
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: 149.86 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlSANELARKVAFLP 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVaygrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03230 80 EEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
1.76e-44 |
|
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: 156.60 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MT-ILKAQQLDIGY--GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA---GSLSLDGTAYGKLSANE 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 LARKVAFLPQVlpiPE----GVSVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAW 149
Cdd:COG1123 81 RGRRIGMVFQD---PMtqlnPVTVGDQIAEA-----LENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 499585766 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 |
2.09e-44 |
|
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: 147.01 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 5 KAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 vlpipegvsvrqlvaygrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 165 EPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-221 |
3.37e-43 |
|
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: 146.50 E-value: 3.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGY----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA-- 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 -RKVAFLPQvlpipegvsvrqlvaygrSPHNSLWGRLSGADQ----------HSVDQALQRMELDTLAERPLSD------ 139
Cdd:cd03257 81 rKEIQMVFQ------------------DPMSSLNPRMTIGEQiaeplrihgkLSKKEARKEAVLLLLVGVGLPEevlnry 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 ---LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:cd03257 143 pheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
....*.
gi 499585766 216 RMVTCG 221
Cdd:cd03257 223 KIVEEG 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
4.36e-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: 145.31 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSAnELARKVAFLP 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAygrsphnsLWGRLSG--ADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:COG4133 82 HADGLKPELTVRENLR--------FWAALYGlrADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-255 |
2.24e-42 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 145.08 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 22 LSFSPPPAQVTALIGPNGCGKSTLLKAFARiLTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQLVAYG 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 102 RSPHNSLwgrlsGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLDISH 174
Cdd:PRK03695 94 QPDKTRT-----EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDVQVQimREPVAGTPMCI 254
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR--RLDVEGHPMLI 246
|
.
gi 499585766 255 V 255
Cdd:PRK03695 247 S 247
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-217 |
4.14e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLP 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGvSVRQLVAYGRSPHNSLWgrlsgaDQHSVDQALQRMELDT-LAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKF------DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-232 |
7.00e-42 |
|
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: 143.64 E-value: 7.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-V 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 A--FlpQVLPIPEGVSVRQ--LVAYGRSPHNSLWGRLSG---------ADQHSVDQALQRMELDTLAERPLSDLSGGQRQ 146
Cdd:COG0411 82 ArtF--QNPRLFPELTVLEnvLVAAHARLGRGLLAALLRlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*..
gi 499585766 226 VLTAELV 232
Cdd:COG0411 240 VRADPRV 246
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-215 |
9.97e-42 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 142.01 E-value: 9.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygKLSANELARKVAFLPQ-VLPIPEG 91
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQdVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVAYGRsphnslwgRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03226 87 DSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-245 |
2.15e-41 |
|
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: 142.53 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAG-SLSLDGTAYGKLSANELARKV 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVL--PIPEGVSVRQLVAYGRspHNS--LWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1119 81 GLVSPALqlRFPRDETVLDVVLSGF--FDSigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQ 234
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
|
250
....*....|.
gi 499585766 235 VFDVQVQIMRE 245
Cdd:COG1119 239 AFGLPVEVERR 249
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-218 |
3.24e-41 |
|
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: 141.86 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGA----TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKV 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVlpiPEGV-----SVRQLVAygrsphNSLWGRLSGADQHSVDQALQRMELD-TLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG1124 82 QMVFQD---PYASlhprhTVDRILA------EPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 154 LAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
7.38e-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: 143.70 E-value: 7.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVA 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQvlpipegvS--------VRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRA 148
Cdd:COG3842 81 MVFQ--------DyalfphltVAENVAFGlrmR--------GVPKAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 149 WLAMILAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPS 224
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
..
gi 499585766 225 DV 226
Cdd:COG3842 222 EI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-226 |
7.69e-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: 140.39 E-value: 7.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARIL-----TPQAGSLSLDGTAYGKLSAN--ELA 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQvLPIPEGVSVRQLVAYGRSPHNSLWGRLSGAdqhSVDQALQRMELDTLAERPLS--DLSGGQRQRAWLAMIL 154
Cdd:cd03260 81 RRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGIKLKEELDE---RVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-226 |
8.01e-41 |
|
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: 140.90 E-value: 8.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYG-ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL---ARK 78
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 VAFLPQVLPIPEGVSVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 155 AQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:TIGR02315 161 AQQPDLILADEPIASLDpkTSKQV--MDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-227 |
2.51e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.21 E-value: 2.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDG-TAYGKLSANElaRKVAFLPQvlpipeg 91
Cdd:COG1118 12 FGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrDLFTNLPPRE--RRVGFVFQhyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 vSVRQLVAYG---RSPhnslwgrlSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:COG1118 90 mTVAENIAFGlrvRPP--------SKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 168 TYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:COG1118 162 GALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-230 |
5.43e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 138.35 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 23 SFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQvlpipEG-----VSVRQL 97
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQ-----ENnlfphLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHnslwGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:COG3840 92 IGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 178 LLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG3840 168 MLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-239 |
9.71e-40 |
|
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: 137.29 E-value: 9.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 24 FSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSanelaRKVAFLPQV------LPIpegvSVRQL 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGW-----RHIGYVPQRhefawdFPI----SVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR03771 72 VMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 178 LLDLMRELSAEGKTVITVLHDINQACRYADHLaVMQGGRMVTCGAPSDVLTAELVCQVFDVQ 239
Cdd:TIGR03771 152 LTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-227 |
1.25e-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: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGvSVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELDTLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQAcRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELL 559
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-228 |
7.11e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.93 E-value: 7.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQA---GSLSLDGT-AYGK-LSANE 74
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEdIYDPdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 LARKVAFLPQvLPIPEGVSVRQLVAYG-RsphnsLWGRLSGAD-QHSVDQALQRMEL-----DTLAERPLSdLSGGQRQR 147
Cdd:COG1117 90 LRRRVGMVFQ-KPNPFPKSIYDNVAYGlR-----LHGIKSKSElDEIVEESLRKAALwdevkDRLKKSALG-LSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLD-IS-HQVEllDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
...
gi 499585766 226 VLT 228
Cdd:COG1117 240 IFT 242
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-230 |
1.50e-38 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 134.72 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQvlpipEG-----VSVRQLVAYgrsP---HnslwGRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWL 150
Cdd:COG1127 85 GMLFQ-----GGalfdsLTVFENVAF---PlreH----TDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 151 AMILAQDAAIVLLDEPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
..
gi 499585766 229 AE 230
Cdd:COG1127 232 SD 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-232 |
9.46e-38 |
|
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: 132.41 E-value: 9.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-V 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQ---VLPipeGVSVR---QLVAYGRSphnslwgrlsgaDQHSVDQALQRMeLDT---LAER---PLSDLSGGQRQR 147
Cdd:COG0410 81 GYVPEgrrIFP---SLTVEenlLLGAYARR------------DRAEVRADLERV-YELfprLKERrrqRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 148 AWLAMILAQDAAIVLLDEPTtyLDISHQV--ELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
....*..
gi 499585766 226 VLTAELV 232
Cdd:COG0410 223 LLADPEV 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
3.23e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.93 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQL----DIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA- 76
Cdd:COG1136 3 PLLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 ---RKVAFLPQ---VLPipeGVSVRQLVAYgrsPHnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWL 150
Cdd:COG1136 83 lrrRHIGFVFQffnLLP---ELTALENVAL---PL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRMV 218
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
3.45e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.63 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-VAFL 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVR---QLVAYGRSPhnslwgrlsGADQHSVDQALQRM-ELDTLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03224 81 PEGRRIFPELTVEenlLLGAYARRR---------AKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-216 |
3.69e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 130.30 E-value: 3.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA----RKVAFLPQ--- 84
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrRHIGFVFQsfn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPipeGVSVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03255 93 LLP---DLTALENVELP-----LLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGR 216
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-228 |
1.04e-36 |
|
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: 130.11 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ---VLP--- 87
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQqigLFPhmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 IPEGVS-VRQLVAYGRSphnslwgrlsgADQHSVDQALQRMELD--TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03295 92 VEENIAlVPKLLKWPKE-----------KIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 165 EPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:cd03295 161 EPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
1.08e-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: 126.99 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQLV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 99 AYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-228 |
1.46e-36 |
|
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: 130.65 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDG---TAYGKLSANELARKVAFLPQvlpIPEgvsvRQL 97
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrdiTAKKKKKLKDLRKKVGLVFQ---FPE----HQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 --------VAYGrsPHNslWGrLSGADQHS-VDQALQRMELD-TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR04521 96 feetvykdIAFG--PKN--LG-LSEEEAEErVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 168 TYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-202 |
4.19e-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: 126.77 E-value: 4.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA--YGKLSANELARKVAFlpqVLPIPE- 90
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldYSRKGLLERRQRVGL---VFQDPDd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 ---GVSVRQLVAYGrsPHNSlwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:TIGR01166 80 qlfAADVDQDVAFG--PLNL---GLSEAEVERrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 499585766 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQA 202
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-221 |
1.20e-35 |
|
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: 126.15 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAqVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlSANELARKVAFLPQVLPIPEGV 92
Cdd:cd03264 10 YGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYgrsphNSLWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03264 88 TVREFLDY-----IAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 172 ISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03264 163 PEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-216 |
1.93e-35 |
|
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: 124.42 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGAT--RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQvlpipegvsvrqlvaygrSPHnsLWGrlsgadqhsvdqalqrmelDTLAErplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03228 81 VPQ------------------DPF--LFS-------------------GTIRE---NILSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQAcRYADHLAVMQGGR 216
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-228 |
1.94e-35 |
|
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: 126.46 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 9 LDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL---ARKVAFLPQV 85
Cdd:cd03261 6 LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLFQS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 86 LPIPEGVSVRQLVAYGRSPHnslwGRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03261 86 GALFDSLTVFENVAFPLREH----TRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 165 EPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:cd03261 162 EPTAGLDpIASGV-IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-218 |
3.72e-35 |
|
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: 125.10 E-value: 3.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAY----GKLSANELARKVAFLPQVLPIPEGVSVRQLVAYGrs 103
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 104 phnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMR 183
Cdd:cd03297 100 ----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 499585766 184 ELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:cd03297 176 QIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-221 |
4.50e-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: 4.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFspPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:cd03298 10 YGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRSPhnSLwgRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03298 86 TVEQNVGLGLSP--GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 173 SHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03298 162 ALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-221 |
5.20e-35 |
|
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: 124.79 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlSANELARKVAFLPQVLPIPEGVSVRQLV 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYgrsphnslWGRLSGADQHSVDQAL----QRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03266 100 EY--------FAGLYGLKGDELTARLeelaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499585766 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-227 |
8.42e-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: 131.04 E-value: 8.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATRIV-QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:COG4987 334 LELEDVSFRYpGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGvSVRQ--LVAYGRSPHNSLWgrlsgadqhsvdQALQRMELDTLAERpLSD------------LSGGQRQR 147
Cdd:COG4987 414 VPQRPHLFDT-TLREnlRLARPDATDEELW------------AALERVGLGDWLAA-LPDgldtwlgeggrrLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
1.08e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 125.03 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQA---GSLSLDGTAYGKLSANEL 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 76 ARKVAFLPQVL-PIPEgVSVRQLVAYGRSphnslWGRLSGAD---QHSVDQALQRMEL-DTLAER---PLSDLSGGQRQR 147
Cdd:PRK14247 81 RRRVQMVFQIPnPIPN-LSIFENVALGLK-----LNRLVKSKkelQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
.
gi 499585766 228 T 228
Cdd:PRK14247 234 T 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-238 |
1.38e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.07 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlSANELARKVAFL 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK13537 86 PQFDNLDPDFTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDV 238
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEI 237
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-226 |
1.96e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 125.61 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlsanELARKVAFL 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 pqvlpiPE--G----VSVR-QLVAYGRsphnsLWGrLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:COG4152 77 ------PEerGlypkMKVGeQLVYLAR-----LKG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 155 AQDAAIVLLDEPTTYLD-IShqVELL-DLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:COG4152 145 LHDPELLILDEPFSGLDpVN--VELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-221 |
1.99e-34 |
|
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: 123.16 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygKLSANELARKVAFLP 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVR-QLVAYGRsphnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03269 77 EERGLYPKMKVIdQLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-226 |
3.62e-34 |
|
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: 123.22 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYG-RSPHNSlwGRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03296 90 TVFDNVAFGlRVKPRS--ERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 171 DISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:cd03296 168 DAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-212 |
3.68e-34 |
|
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: 128.94 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGvSVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELDTL-AERPL----------SDLSGGQRQRAWLA 151
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRyADHLAVM 212
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
12-218 |
7.09e-34 |
|
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: 121.81 E-value: 7.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklSANELARKVAFLPQ---VLPi 88
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDRGYVFQqdaLLP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 peGVSVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03293 87 --WLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 169 YLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRMV 218
Cdd:cd03293 161 ALDaltrEQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-216 |
8.31e-34 |
|
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: 120.37 E-value: 8.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSAN--ELARKVAF 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGVSVRQLVAYGrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-232 |
1.40e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.06 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAF 81
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQ-VLPIPEgVSVRQLVAYGRSPHNslWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQ-----RAwlamiL 154
Cdd:COG1129 84 IHQeLNLVPN-LSVAENIFLGREPRR--GGLIDWRAMRRrARELLARLGLDIDPDTPVGDLSVAQQQlveiaRA-----L 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 155 AQDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:COG1129 156 SRDARVLILDEPTASLT-EREVErLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELV 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-229 |
1.42e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 121.64 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYG--KLSANELARKVA 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQ---------VLpipEGVSVRQLVAYGRSPhnslwgrlsgadqhsvDQALQR-ME-LDT--LAER----PlSDLSGG 143
Cdd:COG1126 81 MVFQqfnlfphltVL---ENVTLAPIKVKKMSK----------------AEAEERaMElLERvgLADKadayP-AQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 144 QRQRAWLAMILAQDAAIVLLDEPTTYLD---IShqvELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTC 220
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEE 217
|
....*....
gi 499585766 221 GAPSDVLTA 229
Cdd:COG1126 218 GPPEEFFEN 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
2.11e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 2.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGY--GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKV 79
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFlpqVLPIPE----GVSVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13635 84 GM---VFQNPDnqfvGATVQDDVAFGLEnigvPREEMVER--------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-244 |
2.73e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.15 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFlpqVLPIPE----G 91
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL---VFQDPDdqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK13647 95 STVWDDVAFG--PVNM---GLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 171 DISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQV---FDVQVQIMR 244
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAglrLPLVAQIFE 246
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-236 |
6.86e-33 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 120.76 E-value: 6.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELarkVAFLPQVLPIPEG--VSVRQ 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQV 176
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 177 ELLDLMRELSAEGKTVITVLHDINQACRYADHlAVMQGGRMVTCGAPSDVLTAELVCQVF 236
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPTETTFTAENLELAF 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-223 |
7.44e-33 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 119.15 E-value: 7.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaYGKLSANELARKVAFLPQVLPIPEG 91
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY-SIRTDRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03263 90 LTVREHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 172 ISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAP 223
Cdd:cd03263 166 PASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-228 |
1.02e-32 |
|
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: 120.44 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELaRKV------------AF 81
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKEL-RELrrkkismvfqsfAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQvlpipegVSVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03294 114 LPH-------RTVLENVAFGL----EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:cd03294 183 LMDEAFSALDplirREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
2.06e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlpiPE----GVS 93
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN---PDnqfiGAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13632 101 VEDDIAFGlenkKVPPKKMKDI--------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 170 LDISHQVELLDLMRELSAEG-KTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
3.20e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.95 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVA 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQ---VLPipeGVSVRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3839 79 MVFQsyaLYP---HMTVYENIAFPlklR--------KVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-226 |
9.55e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.80 E-value: 9.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRS--PHNSlwgRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK10851 90 TVFDNIAFGLTvlPRRE---RPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 170 LDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-230 |
1.01e-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: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvSVRQL 97
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-TIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRsphnslwgrlSGADQHSVDQALQRMEL-DTLAERPL----------SDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG2274 569 ITLGD----------PDATDEEIIEAARLAGLhDFIEALPMgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 167 TTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG2274 639 TSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
2.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 117.10 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA--YGKLSANELARKV 79
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQ----VLPIPegvSVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13639 81 GIVFQnpddQLFAP---TVEEDVAFG--PLNL---GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-218 |
4.56e-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: 117.08 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGY----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA---GSLSLDGTAYGKLSANEL 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 76 ----ARKVAFLPQ--------VLpipegvSVRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMELDTLAERpLSD--- 139
Cdd:COG0444 81 rkirGREIQMIFQdpmtslnpVM------TVGDQIAEPLRIH----GGLSKAEARErAIELLERVGLPDPERR-LDRyph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 -LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:COG0444 150 eLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
.
gi 499585766 218 V 218
Cdd:COG0444 230 V 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-198 |
6.72e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 6.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 6 AQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsanelarKVAFLPQV 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 86 LPIPEGVSVRQLVAYGRSPHNSLWGRL---------SGADQHSVDQALQRME--------------LDTL------AERP 136
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELeeleaklaePDEDLERLAELQEEFEalggweaearaeeiLSGLgfpeedLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 137 LSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD 198
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKNYPGTVLVVSHD 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
3.86e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 113.26 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsANELA 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQ---VLPipegvSVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG1116 80 PDRGVVFQepaLLPw---lTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:COG1116 153 LANDPEVLLMDEPFGALDaltrERLQDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-217 |
4.60e-30 |
|
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: 110.77 E-value: 4.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATR--IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPqvlpipegvsvrqlvaygrsphnslwgrlsgadqhsvdqalQRMEL--DTLAErplSDLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03246 81 LP-----------------------------------------QDDELfsGSIAE---NILSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRM 217
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-226 |
5.70e-30 |
|
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: 112.33 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVFQNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03300 88 TVFENIAFGlrlkKLPKAEIKER--------VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 169 YLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:cd03300 160 ALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-218 |
1.07e-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: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvSVRQLV 98
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYGRSPHNSL----WGRLSGADQHSVDQA--LQRMeldtLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03245 99 TLGAPLADDErilrAAELAGVTDFVNKHPngLDLQ----IGERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 173 SHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRMV 218
Cdd:cd03245 174 NSEERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-221 |
1.51e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.42 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIV-QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipE 90
Cdd:COG1132 348 SYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ-----D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GV----SVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELDTLAERpLSD------------LSGGQRQRAWLAMIL 154
Cdd:COG1132 423 TFlfsgTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFIEA-LPDgydtvvgergvnLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRMVTCG 221
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-218 |
2.19e-29 |
|
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: 108.67 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAFLPQvlpipeg 91
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 vsvrqlvaygrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-238 |
3.03e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.00 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGklSANELAR-KVAFLPQVLPIPEG 91
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARaRIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQ-LVAYGRsphnslWGRLSGADQHSV-DQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13536 129 FTVREnLLVFGR------YFGMSTREIEAViPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQVFDV 238
Cdd:PRK13536 203 LDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEI 271
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-227 |
4.00e-29 |
|
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: 115.23 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATR-IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:COG4618 331 LSVENLTVVPpGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGvSVRQLVAygrsphnslwgRLSGADQHSVDQALQR-------MEL----DTLAERPLSDLSGGQRQRAWL 150
Cdd:COG4618 411 LPQDVELFDG-TIAENIA-----------RFGDADPEKVVAAAKLagvhemiLRLpdgyDTRIGEGGARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
4.49e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 4.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKV 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFlpqVLPIPE----GVSVRQLVAYGrsPHNslWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:PRK13652 81 GL---VFQNPDdqifSPTVEQDIAFG--PIN--LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-226 |
5.52e-29 |
|
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: 109.54 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-VAFL 82
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQlvaygrsphNSLWG--RLSGADQHSVDQALQRME-LDTLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:TIGR03410 81 PQGREIFPRLTVEE---------NLLTGlaALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-228 |
9.88e-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: 111.73 E-value: 9.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYgkLSAnelARKVaFLPqvlpiPE----GV---- 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDS---ARGI-FLP-----PHrrriGYvfqe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 -------SVRQLVAYGRsphnslWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4148 86 arlfphlSVRGNLLYGR------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-199 |
1.08e-28 |
|
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: 114.11 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 26 PPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLS--------LD---GTAYG----KLSANELarKVAFLPQ-VLPIP 89
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevLKrfrGTELQdyfkKLANGEI--KVAHKPQyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EGVS--VRQLvaygrsphnslwgrLSGADQH-SVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG1245 174 KVFKgtVREL--------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 499585766 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-210 |
1.35e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.49 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQA---GSLSLDG-TAYGK-LSANE 74
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGkNLYAPdVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 LARKVAFLPQVlPIPEGVSVRQLVAYGrSPHNSLWGRLSGADQHSVDQALQRMEL-DTLAERPLSdLSGGQRQRAWLAMI 153
Cdd:PRK14243 89 VRRRIGMVFQK-PNPFPKSIYDNIAYG-ARINGYKGDMDELVERSLRQAALWDEVkDKLKQSGLS-LSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 154 LAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLA 210
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTA 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
1.80e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYG----ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANela 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAF-----LPQVlpipegvSVRQLVAYGRsphnslwgRLSGADQHS----VDQALQRMELDTLAERPLSDLSGGQRQR 147
Cdd:COG4525 78 RGVVFqkdalLPWL-------NVLDNVAFGL--------RLRGVPKAErrarAEELLALVGLADFARRRIWQLSGGMRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLDI----SHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRMV 218
Cdd:COG4525 143 VGIARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQR---TGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-229 |
1.89e-28 |
|
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: 113.81 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvSVRQLV 98
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYG-TLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYGRsPHnslwgrlsgADQHSVDQALQRMELDTLA-------ERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR03375 560 ALGA-PY---------ADDEEILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 168 TYLDISHQVELLDLMRELSAeGKTVITVLHDiNQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRWLA-GKTLVLVTHR-TSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-216 |
4.82e-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: 4.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYG--KLSANELARKVAFLPQ------ 84
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGMVFQqfnlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 ---VLpipEGVSVRQLVAYGRSPHNslwgrlsgADQHSVdQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03262 90 hltVL---ENITLAPIKVKGMSKAE--------AEERAL-ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-223 |
5.47e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 106.69 E-value: 5.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlSANELARKVAFLPQVLPIPEGV 92
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03265 89 TGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 172 ISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAP 223
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-218 |
7.65e-28 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 105.76 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSanELARKVAFLp 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 qvlpipegVSVRQLVAYGRSPHN-SLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03268 78 --------IEAPGFYPNLTARENlRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-221 |
1.13e-27 |
|
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: 105.82 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFAriltpqaGSLSLDGTAYGKLSANELARK-------VAFLPQVLPIP 89
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIS-------GRVEGGGTTSGQILFNGQPRKpdqfqkcVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EGVSVRQLVAYgrSPHNSLWGRLSGA--DQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:cd03234 94 PGLTVRETLTY--TAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 168 TYLDISHQVELLDLMRELSAEGKTVITVLH----DInqaCRYADHLAVMQGGRMVTCG 221
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
7-230 |
1.49e-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: 105.78 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 7 QQLDIGYGATR--IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ 84
Cdd:cd03251 4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPIPEGvSVRQLVAYGRsphnslwgrlSGADQHSVDQALQ---------RME--LDT-LAERPlSDLSGGQRQRAWLAM 152
Cdd:cd03251 84 DVFLFND-TVAENIAYGR----------PGATREEVEEAARaanahefimELPegYDTvIGERG-VKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-227 |
1.76e-27 |
|
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: 108.28 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGK------LSANElaRKVAFLPQVLPIPEGVSV 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSphnslwgRLSGADQHSVDQALQRM-ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR02142 93 RGNLRYGMK-------RARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 174 HQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
2.85e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYG-ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA--YGKLSANELARK 78
Cdd:PRK13636 4 YILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 VAFlpqVLPIPE----GVSVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWL 150
Cdd:PRK13636 84 VGM---VFQDPDnqlfSASVYQDVSFGavnlKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-217 |
2.99e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.56 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 30 QVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGVSVRQLVAYGRSPhnSLw 109
Cdd:TIGR01277 25 EIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGLHP--GL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 110 gRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG 189
Cdd:TIGR01277 100 -KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSER 178
|
170 180
....*....|....*....|....*....
gi 499585766 190 K-TVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:TIGR01277 179 QrTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-227 |
4.27e-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: 104.62 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATR-IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipE 90
Cdd:cd03253 9 AYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ-----D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GVSVRQLVAYgrsphNSLWGRLSGADQHSVDQA--------LQRME--LDT-LAERPLSdLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03253 84 TVLFNDTIGY-----NIRYGRPDATDEEVIEAAkaaqihdkIMRFPdgYDTiVGERGLK-LSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 160 IVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVL 227
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-199 |
5.04e-27 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 109.13 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 26 PPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLS--------LD---GTAYG----KLSANELarKVAFLPQ-VLPIP 89
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevLKrfrGTELQnyfkKLYNGEI--KVVHKPQyVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EGV--SVRQLvaygrsphnslwgrLSGADQHSV-DQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13409 174 KVFkgKVREL--------------LKKVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|...
gi 499585766 167 TTYLDISHQVELLDLMRELsAEGKTVITVLHDI 199
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-221 |
5.21e-27 |
|
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: 102.78 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYG--ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSaNELARKVAF 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQvlpipegvsvrqlvaygrSPHnsLWgrlsgadqhsvDQALqrmeLDTLAERplsdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03247 80 LNQ------------------RPY--LF-----------DTTL----RNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
5.56e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.80 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVA---FLPQVLpipegvSV 94
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrnAMKPAL------TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYgrsphnslWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK13539 91 AENLEF--------WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|...
gi 499585766 175 QVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATH 185
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-229 |
7.29e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 108.59 E-value: 7.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvS 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVA-YGRSPHNS---LWGRLSGAdqHSVDQALQrMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR01842 408 VAENIArFGENADPEkiiEAAKLAGV--HELILRLP-DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:TIGR01842 485 LDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-234 |
8.50e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.89 E-value: 8.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 23 SFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGVSVRQLVAYGR 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 103 SPhnSLwgRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLM 182
Cdd:PRK10771 97 NP--GL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 183 RELSAEGK-TVITVLHDINQACRYADHLAVMQGGRMVTCGApsdvlTAELVCQ 234
Cdd:PRK10771 173 SQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP-----TDELLSG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-221 |
1.09e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQ---AGSLSLDG-TAYG-KLSANE 74
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGhNIYSpRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 LARKVAFLPQvLPIPEGVSVRQLVAYGRsphnslwgRLSGA-DQHSVDQALQRM--------EL-DTLAERPLSdLSGGQ 144
Cdd:PRK14239 84 LRKEIGMVFQ-QPNPFPMSIYENVVYGL--------RLKGIkDKQVLDEAVEKSlkgasiwdEVkDRLHDSALG-LSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 145 RQRAWLAMILAQDAAIVLLDEPTTYLD-ISH-QVE--LLDLMRELsaegkTVITVLHDINQACRYADHLAVMQGGRMVTC 220
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDpISAgKIEetLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
.
gi 499585766 221 G 221
Cdd:PRK14239 229 N 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-199 |
1.91e-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: 103.60 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 25 SPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSL----SLD-------GTA----YGKLSANELarKVAFLPQ-VLPI 88
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDeildefrGSElqnyFTKLLEGDV--KVIVKPQyVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEGV--SVRQLvaygrsphnslwgrLSGADQ-HSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:cd03236 100 PKAVkgKVGEL--------------LKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
33-227 |
2.57e-26 |
|
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: 102.80 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 33 ALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGVSVRQLVAYGRSphNSLWGRL 112
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNIAYGLK--KRKVDKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 113 SgaDQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKT 191
Cdd:cd03299 105 E--IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEfGVT 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 499585766 192 VITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:cd03299 183 VLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-198 |
2.88e-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: 107.06 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVlPIPEGVSVRQ--LVAYGRSPHNSLWGRLSGADQHSVDQALQRmELDTLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:TIGR02868 415 AQD-AHLFDTTVREnlRLARPDATDEELWAALERVGLADWLRALPD-GLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 499585766 161 VLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHD 198
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-227 |
7.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE----LARKVAFlpqVLPIPE 90
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGV---VFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GV----SVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMELDTLA----ERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13643 95 SQlfeeTVLKDVAFG--PQN-----FGIPKEKAEKIAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-218 |
8.91e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 8.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAFLPQVLP-IPEgVSV 94
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPE-MTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSPHNSLWGRLSGADQHSVDQaLQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499585766 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK11288 176 IEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-218 |
9.46e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsanelarKVAF 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV-----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVL-PIPEGVSVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMeldtL-----AERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG0488 383 FDQHQeELDPDKTVLDELRDGA----------PGGTEQEVRGYLGRF----LfsgddAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELsaEGkTVITVLHDinqacRY-----ADHLAVMQGGRMV 218
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
1.23e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTIlKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGklsanelarkva 80
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 fLPQVLPIPEGVSVRQLVA-----YGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELDTLAER-PLSdLSGG 143
Cdd:COG4161 68 -FSQKPSEKAIRLLRQKVGmvfqqYNLWPHLTVMENLIEApckvlglsKEQAREKAmklLARLRLTDKADRfPLH-LSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 144 QRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDpeITAQV--VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-227 |
1.30e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARkvAFL 82
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE--AER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVsVRQLVAYGRSPHNSLWG----RLSGA-DQH------SVDQALQRMELDtlAERpLSDL----SGGQRQR 147
Cdd:PRK11701 84 RRLLRTEWGF-VHQHPRDGLRMQVSAGGnigeRLMAVgARHygdiraTAGDWLERVEID--AAR-IDDLpttfSGGMQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
.
gi 499585766 227 L 227
Cdd:PRK11701 240 L 240
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-227 |
1.56e-25 |
|
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: 100.69 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVRQL 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPhnslwgrlsgADQHSVDQALQR-------MEL----DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:cd03249 97 IRYGKPD----------ATDEEVEEAAKKanihdfiMSLpdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 167 TTYLD-ISHQV--ELLDLMRelsaEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:cd03249 167 TSALDaESEKLvqEALDRAM----KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-226 |
1.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 32 TALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE----LARKVAFlpqVLPIPEGV----SVRQLVAYGrs 103
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqIRKKVGL---VFQFPESQlfeeTVLKDVAFG-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 104 PHNSlwgrlsGADQHSVDQ-ALQRMEL----DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVEL 178
Cdd:PRK13649 111 PQNF------GVSQEEAEAlAREKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499585766 179 LDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13649 185 MTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-228 |
1.98e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygkLSANELARKVAFLPQvlpiPEGV 92
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKVDERLIRQ----EAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYgrsPH-----NSLWG--RLSGADQHSVDQalQRMELDT---LAER----PlSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK09493 82 VFQQFYLF---PHltaleNVMFGplRVRGASKEEAEK--QARELLAkvgLAERahhyP-SELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-227 |
2.10e-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: 99.99 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIV-QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPE 90
Cdd:cd03254 11 SYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GvSVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELDTLAERpL------------SDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03254 91 G-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMK-LpngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-228 |
2.83e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSAN----ELARKVAFlpqVLPIPEGV---- 92
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSL---VFQFPEAQlfen 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMEL----DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK13641 102 TVLKDVEFG--PKN-----FGFSEDEAKEKALKWLKKvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-226 |
3.31e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGS---LSLDGTAYGKLSANELARKVAFlpqVLPIPE---- 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKVGI---VFQNPDnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GVSVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13640 99 GATVGDDVAFGlenrAVPRPEM--------IKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 167 TTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-221 |
3.37e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTIlKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYgKLSANELARKVA 80
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLpipeGVSVRQlvaYGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELDTLAER-PLSdLSGGQRQRA 148
Cdd:PRK11124 79 ELRRNV----GMVFQQ---YNLWPHLTVQQNLIEApcrvlglsKDQALARAeklLERLRLKPYADRfPLH-LSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 149 WLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeITAQI--VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-202 |
3.69e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA---GSLSLDGTAYGKLSAneLARKVA 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPA--EQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLPIPEGVSVRQLVAYGrsphnsLWGRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLA-MILAQDA 158
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFA------LPPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLrALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499585766 159 AiVLLDEPTTYLDISHQVELLDLMRE-LSAEGKTVITVLHDINQA 202
Cdd:COG4136 154 A-LLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDA 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-217 |
3.71e-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: 99.47 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSV 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYG--RSPHNSLWGRLSGADQHSVDQALQRmELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03248 105 QDNIAYGlqSCSFECVKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499585766 173 SHQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRM 217
Cdd:cd03248 184 ESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-221 |
3.80e-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: 98.87 E-value: 3.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRsphnslwgRLSGADQHSVDQALQR----MELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03301 88 TVYDNIAFGL--------KLRKVPKDEIDERVREvaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 169 YLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03301 160 NLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-229 |
5.01e-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: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGA----TRIVQDLSFSPPPAQVTALIGPNGCGKS----TLLKAFARILTPQAGSLSLDGTAYGKLSA 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 73 NELAR----KVAFLPQ--------VLPIpegvsVRQlVAYGRSPHnslwGRLSGADQHS-VDQALQRMELDTlAERPLSD 139
Cdd:COG4172 84 RELRRirgnRIAMIFQepmtslnpLHTI-----GKQ-IAEVLRLH----RGLSGAAARArALELLERVGIPD-PERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 ----LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:COG4172 153 yphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*
gi 499585766 215 GRMVTCGAPSDVLTA 229
Cdd:COG4172 233 GEIVEQGPTAELFAA 247
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-226 |
5.04e-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: 101.03 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGVSVRQLVAYGRsphnslwgRLS 113
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGL--------KMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 114 GADQHSVD----QALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS----HQVELLDLMREL 185
Cdd:TIGR01187 71 KVPRAEIKprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499585766 186 saeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:TIGR01187 151 ---GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
5.48e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQA---GSLSLDG-TAYG-KLSANELA 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGrNIYSpDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQVL-PIPEgVSVRQLVAYGRSPHNSLWGRlsGADQHSVDQALQRMEL-----DTLAERPlSDLSGGQRQRAWL 150
Cdd:PRK14267 85 REVGMVFQYPnPFPH-LTIYDNVAIGVKLNGLVKSK--KELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-221 |
9.34e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.88 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVRQL 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYG--RSPHNSLwgrLSGADQHSVDQALQRME--LDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR00958 575 IAYGltDTPDEEI---MAAAKAANAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499585766 174 HQVELLDLMrelSAEGKTVITVLHDInQACRYADHLAVMQGGRMVTCG 221
Cdd:TIGR00958 652 CEQLLQESR---SRASRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-232 |
1.47e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLS---ANELArkVAFLPQVLPIP 89
Cdd:PRK09700 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLG--IGIIYQELSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EGVSVRQLVAYGRSPHNSLWGrLSGAD----QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK09700 93 DELTVLENLYIGRHLTKKVCG-VNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-218 |
1.79e-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: 97.42 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA----RKVAFLPQ---VLP 87
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQfhhLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 ---IPEGVSVRQLVAyGRSPhnslwgrlsgadQHSVDQA---LQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:TIGR02211 97 dftALENVAMPLLIG-KKSV------------KEAKERAyemLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRyADHLAVMQGGRMV 218
Cdd:TIGR02211 164 LADEPTGNLDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKK-LDRVLEMKDGQLF 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-229 |
2.25e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA--YGK----LSANELARKVAFL-PQVLPIPE 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlyFGKdifqIDAIKLRKEVGMVfQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 gVSVRQLVAYGRSPHNSLWGRlsgADQHSVDQALQRM----ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK14246 105 -LSIYDNIAYPLKSHGIKEKR---EIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499585766 167 TTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-230 |
2.29e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGY--GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQvlpipegvsvrqlvaygrSPH---NSLWGRLSGADQHSVD----QALQRMELDTLAE-------------RPlsdLS 141
Cdd:PRK11160 419 VSQ------------------RVHlfsATLRDNLLLAAPNASDealiEVLQQVGLEKLLEddkglnawlgeggRQ---LS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRMVTCG 221
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQG 555
|
....*....
gi 499585766 222 APSDVLTAE 230
Cdd:PRK11160 556 THQELLAQQ 564
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-229 |
2.48e-24 |
|
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: 97.27 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL---ARKVAFLPQVLPI 88
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEGVSVRQLVAYgrsPHNsLWGrLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:cd03258 94 LSSRTVFENVAL---PLE-IAG-VPKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499585766 168 TYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:cd03258 169 SALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-229 |
2.98e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 100.91 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGY-----------GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARiLTPQAGSLSLDGTAYGKL 70
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 71 SANELA---RKVaflpQVlpipegV------------SVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMELD-TLA 133
Cdd:COG4172 353 SRRALRplrRRM----QV------VfqdpfgslsprmTVGQIIAEGLRVHGP---GLSAAERRArVAEALEEVGLDpAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 134 ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDInQACRY-ADHLAV 211
Cdd:COG4172 420 HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDL-AVVRAlAHRVMV 498
|
250
....*....|....*...
gi 499585766 212 MQGGRMVTCGAPSDVLTA 229
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
3.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFlpqVLPIPE----GVSVRQ 96
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI---VFQNPDnqfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGRSPHNslwgrLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:PRK13648 104 DVAFGLENHA-----VPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 176 VELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13648 179 QNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-218 |
3.92e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 3.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATR-IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RK 78
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 VAFLPQ---VLP---------IPegvsvrqLVAYGRSPHnslwgrlsgADQHSVDQALQRMELDTLAERPLSDLSGGQRQ 146
Cdd:COG2884 81 IGVVFQdfrLLPdrtvyenvaLP-------LRVTGKSRK---------EIRRRVREVLDLVGLSDKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-226 |
5.19e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.14 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFL 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGlkqdKLPKAEIASR--------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 159 AIVLLDEPTTYLDIS----HQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-232 |
5.25e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 100.10 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAFLPQVLPIPEG 91
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVAYGRSPHNSLWGRLSGADQHsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:COG3845 95 LTVAENIVLGLEPTKGGRLDRKAARAR-IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:COG3845 174 PQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELA 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-214 |
5.68e-24 |
|
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: 96.71 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 30 QVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklsanelarKVAFLPQVLPIPEGVSVRQLvaygrsphnsLW 109
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDL----------LS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 110 GRLSGADQHS--VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA 187
Cdd:cd03237 84 SITKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*...
gi 499585766 188 EG-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03237 164 NNeKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-199 |
6.04e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.27 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 30 QVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDgtaygklsanelaRKVAFLPQVLPIPEGVSVRQL-----VAYGRSP 104
Cdd:PRK13409 366 EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLlrsitDDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 105 HNSlwgrlsgadqhsvdQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRE 184
Cdd:PRK13409 433 YKS--------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170
....*....|....*.
gi 499585766 185 LSAE-GKTVITVLHDI 199
Cdd:PRK13409 499 IAEErEATALVVDHDI 514
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-256 |
6.09e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 22 LSFSPPPaqVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA--YGKLSANELARKVAflpQVLPIPE--------- 90
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVA---TVFQDPEqqifytdid 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 ---GVSVRQLvaygrsphnslwGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PRK13638 97 sdiAFSLRNL------------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 168 TYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT-AELVCQVFDVQVQIMR-E 245
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQAGLTQPWLVKlH 244
|
250
....*....|.
gi 499585766 246 PVAGTPMCIVE 256
Cdd:PRK13638 245 TQLGLPLCKTE 255
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-221 |
9.39e-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: 94.93 E-value: 9.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFA--RILTPQAGSLSLDGTaygKLSANELARKVAFLPQvlpip 89
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQ----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 egvsvrqlvaygrspHNSLWGRLSgadqhsVDQALQrmeldTLAErpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03213 90 ---------------DDILHPTLT------VRETLM-----FAAK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLH----DINQACryaDHLAVMQGGRMVTCG 221
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELF---DKLLLLSQGRVIYFG 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-227 |
1.13e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.57 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA----RKVAFLPQVLPIPEGVSV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSphnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK10070 124 LDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 175 QVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK10070 200 RTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-215 |
1.39e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.92 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANelaRKVAFL 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLpIPeGVSVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK11248 78 NEGL-LP-WRNVQDNVAFGL----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-197 |
1.42e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 94.35 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLsANELARKVAFLP 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVaygrsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:TIGR01189 80 HLPGLKPELSALENL--------HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-203 |
1.97e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.51 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsanelarKVAFLP 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QvlpipegvsvrqlvaygrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSaegKTVITVLHD---INQAC 203
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYP---GTVILVSHDryfLDQVA 134
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-226 |
3.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGT--AYGKLSANELARKVAFlpqVLPIPEgv 92
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVdiTDKKVKLSDIRKKVGL---VFQYPE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 svRQL--------VAYGrsPHNslwgrLSGADQHSVDQALQRMEL-----DTLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK13637 94 --YQLfeetiekdIAFG--PIN-----LGLSEEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-218 |
3.38e-23 |
|
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: 94.32 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKlsanelaRKVAFLPQVlpipeGVSVRQlv 98
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-------RRKKFLRRI-----GVVFGQ-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 aygrspHNSLWGRLSGADQHSVDQALQRME-------LDTLAE---------RPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03267 103 ------KTQLWWDLPVIDSFYLLAAIYDLPparfkkrLDELSElldleelldTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-217 |
7.29e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 7.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 10 DIGY--GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlP 87
Cdd:PRK10247 12 NVGYlaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT-P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 IPEGVSVRQLVAYgrsPhnslWG-RLSGADQHSVDQALQRMEL-DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK10247 91 TLFGDTVYDNLIF---P----WQiRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 166 PTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQaCRYADHLAVMQ--GGRM 217
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDE-INHADKVITLQphAGEM 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-199 |
7.98e-23 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 97.16 E-value: 7.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 31 VTALIGPNGCGKSTLLKAFARILTPQAGSLSLDgtaygklsanelaRKVAFLPQVLPIPEGVSVRQLV--AYGRSPHNSL 108
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISPDYDGTVEEFLrsANTDDFGSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 109 WgrlsgadQHSVdqaLQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE 188
Cdd:COG1245 435 Y-------KTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170
....*....|..
gi 499585766 189 -GKTVITVLHDI 199
Cdd:COG1245 505 rGKTAMVVDHDI 516
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-236 |
8.23e-23 |
|
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: 93.38 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-VAFL 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIR--------GLSKKEREEkLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 159 AIVLLDEPTTYLD-ISHQvELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQ 234
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQ-DIQKIIKILKDRG---IGVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
..
gi 499585766 235 VF 236
Cdd:cd03218 229 VY 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-230 |
1.21e-22 |
|
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: 92.93 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVaflpqvlpipeGVSVRQL 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV-----------GVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRLSGADQHSVDQALQR-------MEL----DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:cd03252 86 VLFNRSIRDNIALADPGMSMERVIEAAKLagahdfiSELpegyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 167 TTYLDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-229 |
8.72e-22 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 94.01 E-value: 8.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvSVRQLV 98
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYGRsphnslwgrLSGADQHSVDQALQRMELDTLAER-PL----------SDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR02203 427 AYGR---------TEQADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 168 TYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:TIGR02203 498 SALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-216 |
8.87e-22 |
|
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: 89.84 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklsanelarkVAFLPQVLPIPEGvSVRQL 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGrSPHNSLWgrlsgadqhsVDQALQRMELDT-LAERPLSD----------LSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:cd03250 86 ILFG-KPFDEER----------YEKVIKACALEPdLEILPDGDlteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 167 TTYLDiSHQVELL--DLMRELSAEGKTVITVLHDInQACRYADHLAVMQGGR 216
Cdd:cd03250 155 LSAVD-AHVGRHIfeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-226 |
1.25e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.23 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSL------DGTAYGKLSAneLARKVAFlpqVLPI 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP--LRKKVGI---VFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEG----VSVRQLVAYGrsPHNSlwgrlsGAdqhSVDQALQR----MELDTLAERPLS----DLSGGQRQRAWLAMILAQ 156
Cdd:PRK13634 94 PEHqlfeETVEKDICFG--PMNF------GV---SEEDAKQKaremIELVGLPEELLArspfELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
33-226 |
1.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 33 ALIGPNGCGKSTLLKAFARILTPQAGSLSLDG-TAYGKLSANELARKVAFLPQVLPIPEGV----SVRQLVAYGrsPHNS 107
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKRIGMVFQFPESQlfedTVEREIIFG--PKNF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 108 lwgrlsGADQHSV-DQALQR-MEL----DTLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDL 181
Cdd:PRK13646 115 ------KMNLDEVkNYAHRLlMDLgfsrDVMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 182 MRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13646 188 LKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-230 |
1.53e-21 |
|
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: 93.65 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipEGV----S 93
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQ-----ENVlfsrS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYGRS----PHNSLWGRLSGAdqHSVDQALQRMELDTLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR01846 547 IRDNIALCNPgapfEHVIHAAKLAGA--HDFISELPQGYNTEVGEKG-ANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 170 LDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:TIGR01846 624 LDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-229 |
2.01e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLsanELArkVAFLPQvlpipegVSVRQ 96
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALL---ELG--AGFHPE-------LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGrsphnslwGRLSGADQHSVDQALQRM----ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:COG1134 108 NIYLN--------GRLLGLSRKEIDEKFDEIvefaELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 173 SHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:COG1134 180 AFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-251 |
2.26e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.93 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANelARKV- 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 ------AFLPQvlpipegVSVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAW 149
Cdd:PRK09452 90 tvfqsyALFPH-------MTVFENVAFGlrmqKTPAAEITPR--------VMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 150 LAMILAQDAAIVLLDEPTTYLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499585766 226 V-------LTAELVCQ--VFDVQV------QIMREPVAGTP 251
Cdd:PRK09452 232 IyeepknlFVARFIGEinIFDATVierldeQRVRANVEGRE 272
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-227 |
3.63e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.50 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGAtRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEG 91
Cdd:TIGR01193 484 GYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLvaygrsphnsLWGRLSGADQHSVDQALQRMELDTLAER-PL----------SDLSGGQRQRAWLAMILAQDAAI 160
Cdd:TIGR01193 563 SILENL----------LLGAKENVSQDEIWAACEIAEIKDDIENmPLgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 161 VLLDEPTTYLDISHQVELLDLMreLSAEGKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVL 227
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
5.29e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARiLTPQAGSLSLDGTA--YG------KLSANEL 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVefFNqniyerRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 76 ARKVAFL---PQVLPIpegvSVRQLVAYGRSP---HNSLwgRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAW 149
Cdd:PRK14258 87 RRQVSMVhpkPNLFPM----SVYDNVAYGVKIvgwRPKL--EIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 150 LAMILAQDAAIVLLDEPTTYLD------ISHQVELLDLMRELsaegkTVITVLHDINQACRYADHLAVMQG-----GRMV 218
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL-----TMVIVSHNLHQVSRLSDFTAFFKGnenriGQLV 235
|
250
....*....|
gi 499585766 219 TCGAPSDVLT 228
Cdd:PRK14258 236 EFGLTKKIFN 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-236 |
8.46e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.03 E-value: 8.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-V 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQvlpipEGVSVRQLVAYgrsphNSLWGRLS-----GADQHSvDQALQRME---LDTLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK10895 81 GYLPQ-----EASIFRRLSVY-----DNLMAVLQirddlSAEQRE-DRANELMEefhIEHLRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAEL 231
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
....*
gi 499585766 232 VCQVF 236
Cdd:PRK10895 230 VKRVY 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-225 |
9.97e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.78 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKVAFLPQVLPIPEGV 92
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11432 94 SLGENVGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 173 SHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:PRK11432 170 NLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-223 |
1.88e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.32 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklSANElarkvaflpqVLPIPEGV 92
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMND----------VPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 S-VRQlvAYGRSPHNSL-----WG-RLSGAD----QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11000 78 GmVFQ--SYALYPHLSVaenmsFGlKLAGAKkeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAP 223
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
34-228 |
4.51e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLpqVLPIPE----GVSVRQLVAYGrsPHNSLW 109
Cdd:PRK13644 33 IIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI--VFQNPEtqfvGRTVEEDLAFG--PENLCL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 110 GRLSgaDQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG 189
Cdd:PRK13644 109 PPIE--IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 499585766 190 KTVITVLHDINQaCRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:PRK13644 187 KTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
4.70e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSL------DGTAYGKLSANELARKVA-------FLPQ 84
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKKIKnfkelrrRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPIPEgvsvRQL-------------VAYGRSPHNSlwgrlsgadQHSVDQALQRMELD-TLAERPLSDLSGGQRQRAWL 150
Cdd:PRK13631 121 VFQFPE----YQLfkdtiekdimfgpVALGVKKSEA---------KKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-229 |
6.61e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAG-SLSLDGTAYGKLSAN-----ELAR 77
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSGDVLLGGRSIFNyrdvlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 78 KVAFLPQvLPIPEGVSVRQLVAYGRSPHNSLWGR-LSGADQHSVDQ-ALQRMELDTLAERPLSdLSGGQRQRAWLAMILA 155
Cdd:PRK14271 102 RVGMLFQ-RPNPFPMSIMDNVLAGVRAHKLVPRKeFRGVAQARLTEvGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-221 |
7.59e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.89 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANelarkVAFLPQVlpipegvSVRQ 96
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-----GGFNPEL-------TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGrsphnslwGRLSGADQHSVDQALQRM----ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03220 104 NIYLN--------GRLLGLSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 173 SHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-202 |
1.05e-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: 84.08 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSaNELARKVAFLP 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 QVLPIPEGVSVRQLVAYgrsphnslWGRLSGADQhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03231 80 HAPGIKTTLSVLENLRF--------WHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAEGKTVI-TVLHDINQA 202
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVlTTHQDLGLS 189
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-221 |
1.14e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.98 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDI-GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILtPQAGSLSLDGTAYGKLSANELARKVAFL 82
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGvSVRQLVAYGRSphnslwgrlsGADQHSVDQALQRMELDTLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLGNP----------DASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALA 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 152 MILAQDAAIVLLDEPTTYLDiSHQVELldLMRELS--AEGKTVITVLHDINQACRYaDHLAVMQGGRMVTCG 221
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLD-AHSEQL--VMQALNaaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-198 |
1.44e-19 |
|
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: 84.00 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKVAFLPQ---VLP---IPEG 91
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQdfrLLPdrnVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVrQLVAYGRSPHnsLWgrlsgadQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03292 99 VAF-ALEVTGVPPR--EI-------RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180
....*....|....*....|....*..
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03292 169 PDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-218 |
1.82e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY---------GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLS 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 72 AnelARKVAFLPQVLPI----PEGVSVRQLV-AYGRSPHNSLWGrLSGADQ-HSVDQALQRMELD-TLAERPLSDLSGGQ 144
Cdd:PRK10419 81 R---AQRKAFRRDIQMVfqdsISAVNPRKTVrEIIREPLRHLLS-LDKAERlARASEMLRAVDLDdSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 145 RQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-235 |
2.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDL---SFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKV 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFlpqVLPIPE----GVSVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13642 84 GM---VFQNPDnqfvGATVEDDVAFGMEnqgiPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVL-TA 229
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFaTS 231
|
....*.
gi 499585766 230 ELVCQV 235
Cdd:PRK13642 232 EDMVEI 237
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
14-218 |
2.82e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.55 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKVaflpQ-VLPIP 89
Cdd:COG4608 29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRM----QmVFQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EGV-----SVRQLVAYGRSPHnslwGRLSGAD-QHSVDQALQRMELDT-LAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG4608 105 YASlnprmTVGDIIAEPLRIH----GLASKAErRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINqACRY-ADHLAVMQGGRMV 218
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLGKIV 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-229 |
3.12e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.98 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTP----QAGSLSLDGTAYgklSANEL-ARKVAFLPQVlPIPEGV 92
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV---APCALrGRKIATIMQN-PRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRSPHNSLwGRLSGADQhsVDQALQRMELDTlAERPLS----DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK10418 94 PLHTMHTHARETCLAL-GKPADDAT--LTAALEAVGLEN-AARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 169 YLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-197 |
3.67e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARIltPQAGSlsldgtayGKLSANELARkVAFLPQVLPIPEGvSVR 95
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--WPYGS--------GRIARPAGAR-VLFLPQRPYLPLG-TLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAYgrsPHnslwgrlsGADQHS---VDQALQRMELDTLAERpLSD-------LSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4178 444 EALLY---PA--------TAEAFSdaeLREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGkTVITVLH 197
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT-TVISVGH 542
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-226 |
4.38e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.98 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVS--VRQ 96
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVAtiVEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGrsPHNslWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQV 176
Cdd:PRK13633 106 DVAFG--PEN--LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499585766 177 ELLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK13633 182 EVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-232 |
5.12e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.87 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANeLARKVA-- 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLPIPEGVSVRQLVAYGRSPHNslwgrlsgADQHSVDQALQRM----ELDTLAerplSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQ--------ASMQKMKQLLAALgcqlDLDSSA----GSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-218 |
5.19e-19 |
|
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: 83.70 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKL---SANELARKVAFLPQVLP--IPEGV 92
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDSPsaVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVaygRSPHNSLwGRLSGADQHSVDQALQRM-ELDT-LAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:TIGR02769 106 TVRQII---GEPLRHL-TSLDESEQKARIAELLDMvGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 171 DISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
1.16e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.83 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAflpQVLPIP-----EG 91
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIG---RVFQDPmmgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQ--LVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDtLAER---PLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG1101 97 MTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 167 TTYLD--ISHQVelLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:COG1101 176 TAALDpkTAALV--LELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-223 |
1.23e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFlpqVLPIPE----GVS 93
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM---VFQNPDnqfvGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13650 99 VEDDVAFGLEnkgiPHEEMKER--------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 170 LDISHQVELLDLMRELSAE-GKTVITVLHDINQACrYADHLAVMQGGRMVTCGAP 223
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-222 |
1.30e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGS---LSLDGTAYGKlsANELARK 78
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQR--EGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 V-------AFLPQVLPIPEGVSVRQLVAYGRSPHNSLWGR----LSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQR 147
Cdd:PRK09984 81 IrksrantGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAVMQGGRMVTCGA 222
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-235 |
1.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.13 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPppAQVTALIGPNGCGKSTLLKAFARILTPQAGSlsldgTAYG--KLSAN--------ELARKVAFlpqVLPIPE 90
Cdd:PRK13645 31 SLTFKK--NKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-----TIVGdyAIPANlkkikevkRLRKEIGL---VFQFPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 ----GVSVRQLVAYGrsPHNSlwgrlsGADQHSVDQAL-QRMELDTL----AERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK13645 101 yqlfQETIEKDIAFG--PVNL------GENKQEAYKKVpELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLT-AELVCQV 235
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSnQELLTKI 248
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-227 |
1.66e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlpipEGV 92
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQL----RLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYgrsPHNSLWGRLSGADqhSVDQA------LQRMELDTLAERPL--------------SDLSGGQRQRAWLAM 152
Cdd:PRK10619 91 RTRLTMVF---QHFNLWSHMTVLE--NVMEApiqvlgLSKQEARERAVKYLakvgideraqgkypVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-226 |
1.89e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK--V 79
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgvV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPIPEGVSVRQL-VAYGRSPHNSLwgrLSG---------ADQHSVDQA---LQRMELDTLAERPLSDLSGGQRQ 146
Cdd:PRK11300 84 RTFQHVRLFREMTVIENLlVAQHQQLKTGL---FSGllktpafrrAESEALDRAatwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSD 225
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
.
gi 499585766 226 V 226
Cdd:PRK11300 241 I 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-226 |
4.15e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.35 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL--ARK-VAFLPQVLPIPE 90
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKrMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GVSVRQLVAYGRSPHNslwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK11831 98 DMNVFDNVAYPLREHT----QLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 170 LD-ISHQVeLLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK11831 174 QDpITMGV-LVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-228 |
4.30e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLK--AFARILtpQAGSLS-LDGTAYGKLSANELARKVAFLPQVLpip 89
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSliAGARKI--QQGRVEvLGGDMADARHRRAVCPRIAYMPQGL--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 eG------VSVRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:NF033858 86 -GknlyptLSVFENLDF--------FGRLFGQDAAErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 160 IVLLDEPTTYLD-ISHQV--ELLDLMRElSAEGKTVITVLHDINQACRYaDHLAVMQGGRMVTCGAPSDVLT 228
Cdd:NF033858 157 LLILDEPTTGVDpLSRRQfwELIDRIRA-ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-240 |
5.68e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.66 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKVAFLPQ---VLP 87
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQhfnLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 ipegvS--VRQLVAYgrsphnSLwgRLSGAD----QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:COG1135 96 -----SrtVAENVAL------PL--EIAGVPkaeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 162 LLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHD---INQACryaDHLAVMQGGRMVTCGAPSDV-------LT 228
Cdd:COG1135 163 LCDEATSALDpeTTRSI--LDLLKDINRElGLTIVLITHEmdvVRRIC---DRVAVLENGRIVEQGPVLDVfanpqseLT 237
|
250
....*....|..
gi 499585766 229 AELVCQVFDVQV 240
Cdd:COG1135 238 RRFLPTVLNDEL 249
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-216 |
7.79e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLsLDGTAygKLS-ANELARKVAFLPQVLPIPeg 91
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA--PLAeAREDTRLMFQDARLLPWK-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 vSVRQLVAYGrsphnslwgrLSGadqHSVDQALQRMELDTLAER----PLSdLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PRK11247 97 -KVIDNVGLG----------LKG---QWRDAALQALAAVGLADRanewPAA-LSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 168 TYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-200 |
7.92e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 81.29 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSaNELARKVAFlpqV----------LPI 88
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGV---VfgqrsqlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEgvSVRQLVA-YgrsphnslwgRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG4586 114 ID--SFRLLKAiY----------RIPDAEyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 499585766 167 TTYLDISHQVELLDLMRELSAEGKTviTVL---HDIN 200
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYNRERGT--TILltsHDMD 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
8.11e-18 |
|
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: 78.63 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGatriVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVA 80
Cdd:cd03215 3 PVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLP---------QVLPIPEGVSVRQLvaygrsphnslwgrlsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLA 151
Cdd:cd03215 79 YVPedrkreglvLDLSVAENIALSSL------------------------------------------LSGGNQQKVVLA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:cd03215 117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-221 |
9.04e-18 |
|
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: 82.56 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATR-IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipE 90
Cdd:COG5265 366 GYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ-----D 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GV----SVRQLVAYGRSphnslwgrlsGADQHSVDQALQRMEL-----------DTL-AERPLSdLSGGQRQRAWLAMIL 154
Cdd:COG5265 441 TVlfndTIAYNIAYGRP----------DASEEEVEAAARAAQIhdfieslpdgyDTRvGERGLK-LSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHdinqacR-----YADHLAVMQGGRMVTCG 221
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH------RlstivDADEILVLEAGRIVERG 574
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-236 |
9.82e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.69 E-value: 9.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-V 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPIPEGVSVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1137 81 GYLPQEASIFRKLTVEDnilAVLELR--------KLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 156 QDAAIVLLDEPTTYLD-IShqV-ELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG1137 153 TNPKFILLDEPFAGVDpIA--VaDIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
....*.
gi 499585766 231 LVCQVF 236
Cdd:COG1137 228 LVRKVY 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-215 |
1.11e-17 |
|
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: 79.43 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygKLSANELARKVAFlpQVLPIPEGVSVRQLV 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGPDRMVVF--QNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYGRsphNSLWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR01184 76 ALAV---DRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 499585766 178 LLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01184 153 LQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-221 |
1.45e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVaflpqvlpipeGVS 93
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI-----------AVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYGRSPHNSLW-GRLSGADQHSVD-----QALQRME-----LDTLA-ERPLSdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK13657 415 FQDAGLFNRSIEDNIRvGRPDATDEEMRAaaeraQAHDFIErkpdgYDTVVgERGRQ-LSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRMVTCG 221
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-218 |
1.72e-17 |
|
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: 81.53 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 7 QQLDIGYGATR--IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ 84
Cdd:TIGR03796 481 RNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQ 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPIPEGvSVRQLVaygrsphnSLWGRlSGADQHSVDQALQRMELDTLAERPL----------SDLSGGQRQRAWLAMIL 154
Cdd:TIGR03796 561 DIFLFEG-TVRDNL--------TLWDP-TIPDADLVRACKDAAIHDVITSRPGgydaelaeggANLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 155 AQDAAIVLLDEPTTYLDIshQVELLdLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRMV 218
Cdd:TIGR03796 631 VRNPSILILDEATSALDP--ETEKI-IDDNLRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVV 690
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-218 |
2.99e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLdigyGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVA 80
Cdd:COG1129 255 VVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLP---------QVLPIPEGVSVRQLVAYGRsphnslWGRLSGADQHS-VDQALQRMELDTL-AERPLSDLSGGQRQRAW 149
Cdd:COG1129 331 YVPedrkgeglvLDLSIRENITLASLDRLSR------GGLLDRRRERAlAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-226 |
3.34e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.89 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANElaRKV 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPIPEGVSVRQLVAYGRsphnslwgRLSGADQHSVDQ----ALQRMELDTLAERPLSDLSGGQRQRawLAMILA 155
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYGL--------KIRGMPKAEIEErvaeAARILELEPLLDRKPRELSGGQRQR--VAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 156 --QDAAIVLLDEPTTYLD----ISHQVELLDLMRELSAegkTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK11650 149 ivREPAVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-217 |
3.37e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA----RKVAFLPQ---VLP- 87
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQfhhLLPd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 --IPEGVSVRQLVAyGRSPHNSlwgrlsgadQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK11629 102 ftALENVAMPLLIG-KKKPAEI---------NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 166 PTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAvMQGGRM 217
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-229 |
3.83e-17 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 78.30 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGV 92
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADRRQLQRIRTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 S-VRQlvaygrspHNSLWGRLS------GADQH----SVDQALQRME--LDT--LAER----PlSDLSGGQRQRAWLAMI 153
Cdd:COG4598 98 GmVFQ--------SFNLWSHMTvlenviEAPVHvlgrPKAEAIERAEalLAKvgLADKrdayP-AHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 154 LAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
4.48e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY-------GATRIVQDL---SFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDG---TAY 67
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrglfKPERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGqdlLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 68 GKLSANELARKVaflpqvlpipegvsvrQLVAygRSPHNSLWGR----------------LSGADQhsVDQALQRMELDT 131
Cdd:PRK11308 83 DPEAQKLLRQKI----------------QIVF--QNPYGSLNPRkkvgqileepllintsLSAAER--REKALAMMAKVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 132 L----AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYA 206
Cdd:PRK11308 143 LrpehYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIA 222
|
250
....*....|....*
gi 499585766 207 DHLAVMQGGRMVTCG 221
Cdd:PRK11308 223 DEVMVMYLGRCVEKG 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
14-216 |
4.79e-17 |
|
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: 77.47 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRI--VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDgTAYGKL---SANE---LA-RK-----V 79
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVdlaQASPreiLAlRRrtigyV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 A-FLpQVLPipeGVSVRQLVAygrsphNSLwgRLSGAD-QHSVDQA---LQRMELDtlaERpLSDL-----SGGQRQRAW 149
Cdd:COG4778 99 SqFL-RVIP---RVSALDVVA------EPL--LERGVDrEEARARArelLARLNLP---ER-LWDLppatfSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
6.07e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklsanelARKVA 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVL----PIPEGVSvRQLvaygrsphnslwgRLS-GADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:PRK09544 71 YVPQKLyldtTLPLTVN-RFL-------------RLRpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDI 199
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-227 |
6.36e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.85 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLS-------LDGTAYGKLSANELA 76
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQvlpipegvsvrqlvAYGRSPHNSLWGRLSGADQHSVDQALQRM--------------ELDTLAERPLSDLSG 142
Cdd:TIGR03269 365 RYIGILHQ--------------EYDLYPHRTVLDNLTEAIGLELPDELARMkavitlkmvgfdeeKAEEILDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 143 GQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*.
gi 499585766 222 APSDVL 227
Cdd:TIGR03269 511 DPEEIV 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
139-227 |
7.42e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
....*....
gi 499585766 219 TCGAPSDVL 227
Cdd:PRK13651 245 KDGDTYDIL 253
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-224 |
7.47e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI--LTPQAGSLSLDGTAYGKLSANELARK---VAFlPQVLPIPeG 91
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgifLAF-QYPVEIP-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVaygRSPHNSLWG-RLSGADQHS-VDQALQRMELD-TLAERPL-SDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:COG0396 92 VSVSNFL---RTALNARRGeELSAREFLKlLKEKMKELGLDeDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499585766 168 TYLDI-SHQVeLLDLMRELSAEGKT--VIT----VLHDINqacryADHLAVMQGGRMVTCGAPS 224
Cdd:COG0396 169 SGLDIdALRI-VAEGVNKLRSPDRGilIIThyqrILDYIK-----PDFVHVLVDGRIVKSGGKE 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
17-230 |
7.82e-17 |
|
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: 79.62 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLkafaRIL----TPQAGSLSLDGTAYGKLSANELARKVaflpqvlpipeGV 92
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVRRQL-----------GV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQlvayGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAE----RPL----------SDLSGGQRQRAWLAMILAQDA 158
Cdd:TIGR03797 532 VLQN----GRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEdiraMPMgmhtviseggGTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSAegkTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-223 |
8.57e-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: 76.76 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVRQ- 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD-PVLFSGTIRSn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGRSPHNSLWGRL--SGADQHSVDQALQrmeLDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03244 98 LDPFGEYSDEELWQALerVGLKEFVESLPGG---LDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 175 QVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRMVTCGAP 223
Cdd:cd03244 175 DALIQKTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-172 |
1.21e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.21 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGT---AYGKLSANEL-ARK 78
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklAYVDQSRDALdPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 VAFlpQVlpIPEGVSVRQLVAYgRSPHNSLWGR--LSGADQhsvdqalqrmeldtlaERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:TIGR03719 402 TVW--EE--ISGGLDIIKLGKR-EIPSRAYVGRfnFKGSDQ----------------QKKVGQLSGGERNRVHLAKTLKS 460
|
170
....*....|....*.
gi 499585766 157 DAAIVLLDEPTTYLDI 172
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDV 476
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-221 |
1.25e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKVAFLPQVlPIPEgVSVR 95
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQD-PYAS-LDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAYGRSPHNSLWGRLSG-ADQHSVDQALQRMEL-DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGkAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 174 HQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:PRK10261 498 IRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-224 |
4.36e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTP---QAGSLSLDGTaygKLSANELARKVAFLPQV-LPIPEgVSVRQLVAYgrS 103
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDdLFIPT-LTVREHLMF--Q 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 104 PHNSLwGRLSGADQ--HSVDQALQRMEL----DTLAERP--LSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--IS 173
Cdd:TIGR00955 124 AHLRM-PRRVTKKEkrERVDEVLQALGLrkcaNTRIGVPgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfMA 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 174 HQVelLDLMRELSAEGKTVITVLHD-INQACRYADHLAVMQGGRMVTCGAPS 224
Cdd:TIGR00955 203 YSV--VQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-240 |
4.51e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.38 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELA---RKVAFLPQVLPIPEGVSVR 95
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQIGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAygrsphnsLWGRLSGADQHS----VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK11153 101 DNVA--------LPLELAGTPKAEikarVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 172 ISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV-------LTAELVCQVFDVQV 240
Cdd:PRK11153 173 PATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVfshpkhpLTREFIQSTLHLDL 249
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-223 |
5.00e-16 |
|
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: 74.37 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGA--TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAF 81
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHsvdqalqrmeldtlaerplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGG-------------------LNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRMVTCGAP 223
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-176 |
6.68e-16 |
|
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: 77.26 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQaGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVS 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYGRSPHNSLWgrlSGADQHSVDQALQRM--ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:TIGR01271 1309 RKNLDPYEQWSDEEIW---KVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
....*.
gi 499585766 172 -ISHQV 176
Cdd:TIGR01271 1386 pVTLQI 1391
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-230 |
8.47e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSA-----------NELARKVAFLPQVlp 87
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiTESRRDNGFFPNF-- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 ipegvSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLA------ERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK09700 357 -----SIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLAlkchsvNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-224 |
9.59e-16 |
|
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: 74.01 E-value: 9.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQL----DIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELAR 77
Cdd:COG4181 7 PIIELRGLtktvGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 78 ----KVAFLPQ--------------VLPIpEGVSVRQlvAYGRSphnslwgrlsgadqhsvDQALQRMEL-DTLAERPlS 138
Cdd:COG4181 87 lrarHVGFVFQsfqllptltalenvMLPL-ELAGRRD--ARARA-----------------RALLERVGLgHRLDHYP-A 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGG 215
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQI--IDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
....*....
gi 499585766 216 RMVTCGAPS 224
Cdd:COG4181 223 RLVEDTAAT 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-218 |
1.02e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 76.38 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPpaQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygkLSANELARkvaflpqvlpipegvsVRQLVA- 99
Cdd:COG4615 352 DLTIRRG--ELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQP---VTADNREA----------------YRQLFSa 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 100 ----YgrspH--NSLWGRLSGADQHSVDQALQRMELD---TLAERPLS--DLSGGQRQRawLAMILA--QDAAIVLLDE- 165
Cdd:COG4615 411 vfsdF----HlfDRLLGLDGEADPARARELLERLELDhkvSVEDGRFSttDLSQGQRKR--LALLVAllEDRPILVFDEw 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 166 -----PtTYLDISHQvELLDLMRelsAEGKTVITVLHDInqacRY---ADHLAVMQGGRMV 218
Cdd:COG4615 485 aadqdP-EFRRVFYT-ELLPELK---ARGKTVIAISHDD----RYfdlADRVLKMDYGKLV 536
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-223 |
1.40e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 30 QVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYgKLSANELARKVAFLPQVLPIPEGVSVRQlvaygrspHNSLW 109
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAE--------HILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 110 GRLSGADQHSVDQALQRMELDT----LAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMREL 185
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTglhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*...
gi 499585766 186 SAeGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAP 223
Cdd:TIGR01257 1108 RS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-224 |
1.54e-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: 73.83 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFA-----RIltpQAGSLSLDGTAYGKLSANELARKVAFLPQVLP--IP 89
Cdd:TIGR01978 14 EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyEV---TSGTILFKGQDLLELEPDERARAGLFLAFQYPeeIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 eGVSVRQLVaygRSPHNSlwgRLSGADQHSVD---------QALQRMELD-TLAERPLSD-LSGGQRQRAWLAMILAQDA 158
Cdd:TIGR01978 91 -GVSNLEFL---RSALNA---RRSARGEEPLDlldfekllkEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRY--ADHLAVMQGGRMVTCGAPS 224
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYikPDYVHVLLDGRIVKSGDVE 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-218 |
2.21e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY---GATR-IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARIL-TPQAGSLSLDGTAYGK--LSAN 73
Cdd:PRK15134 3 QPLLAIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPVVYPSGDIRFHGEslLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 74 EL------ARKVAFL---PQVLPIPEGVSVRQLvAYGRSPHNSLWGR------LSGADQHSVDQALQRmeldtLAERPlS 138
Cdd:PRK15134 83 EQtlrgvrGNKIAMIfqePMVSLNPLHTLEKQL-YEVLSLHRGMRREaargeiLNCLDRVGIRQAAKR-----LTDYP-H 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
.
gi 499585766 218 V 218
Cdd:PRK15134 236 V 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-176 |
2.55e-15 |
|
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: 73.74 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 14 GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQaGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVS 93
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVAYGRSPHNSLWgrlSGADQHSVDQALQRM--ELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03289 94 RKNLDPYGKWSDEEIW---KVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
....*.
gi 499585766 172 -ISHQV 176
Cdd:cd03289 171 pITYQV 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-198 |
3.16e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLdGTaygKLsanelarKVAFLPQVLPI--PEGvSVR 95
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GT---KL-------EVAYFDQHRAEldPEK-TVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAYGRSPHNslwgrLSGADQHsVDQALQrmelDTL-----AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK11147 402 DNLAEGKQEVM-----VNGRPRH-VLGYLQ----DFLfhpkrAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180
....*....|....*....|....*....
gi 499585766 171 DIshqvELLDLMRELSAEGK-TVITVLHD 198
Cdd:PRK11147 472 DV----ETLELLEELLDSYQgTVLLVSHD 496
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
28-221 |
1.66e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSL-----SLDGT---AYGKLSANELARKVAFLPQ---VLP-------IP 89
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIRQLRQHVGFVFQnfnLFPhrtvlenII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 90 EG-VSVR-----QLVAYGRSphnsLWGR--LSGADqhsvdqalqrmelDTLAERplsdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11264 108 EGpVIVKgepkeEATARARE----LLAKvgLAGKE-------------TSYPRR----LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-218 |
3.54e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTA---YGKLSANE---- 74
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEvtfNGPKSSQEagig 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 75 -LARKVAFLPQvLPIPEGVSVrqlvayGRSPHNSlWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAM 152
Cdd:PRK10762 83 iIHQELNLIPQ-LTIAENIFL------GREFVNR-FGRIDWKKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH---DINQACryaDHLAVMQGGRMV 218
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHrlkEIFEIC---DDVTVFRDGQFI 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-224 |
4.28e-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: 69.09 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA--GSLSLDGTAYGKLSANELARKVAFL-PQVLPIPEGVS 93
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEERARLGIFLaFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 VRQLVaygrsphnslwgrlsgadqhsvdqalqrmeldtlaeRPLSD-LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03217 94 NADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 173 SHQVELLDLMRELSAEGKTVITVLH-----DINQacryADHLAVMQGGRMVTCGAPS 224
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSGDKE 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-229 |
5.39e-14 |
|
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: 71.52 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVR-Q 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD-PVLFSGSLRmN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGRSPHNSLWGRLSGADQHSVDQALQRmELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQv 176
Cdd:TIGR00957 1380 LDPFSQYSDEEVWWALELAHLKTFVSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD- 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 177 ELLDLMRELSAEGKTVITVLHDINQACRYAdHLAVMQGGRMVTCGAPSDVLTA 229
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-218 |
5.93e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILtPQA---GSLSLDGTAYGKLSANELARK-VAFLPQVLPI 88
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAgIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEGVSVRQLVAYGRSPHNSlwGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PRK13549 94 VKELSVLENIFLGNEITPG--GIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499585766 168 TYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-218 |
6.03e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.13 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE---LARK 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 79 VAFLPQVLPIPEGVSVRQLVAYGRsphnsLWGRLSGAD-QHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPL-----IIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-214 |
7.82e-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: 67.60 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 29 AQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklsanelarKVAFLPQVLpipegvsvrqlvaygrsphnsl 108
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQYI---------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 109 wgrlsgadqhsvdqalqrmeldtlaerplsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE 188
Cdd:cd03222 71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
170 180
....*....|....*....|....*..
gi 499585766 189 G-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03222 121 GkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-198 |
1.28e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.14 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELAR----KVAFLPQVLP 87
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 IPEGVSVRQLV----AYGRSPHNSlwgRLSGADQhsvdqALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10535 97 LLSHLTAAQNVevpaVYAGLERKQ---RLLRAQE-----LLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....*
gi 499585766 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
1.36e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKA-FARILTPQAGSLSLDGTAYG-KLSANELARKVAFLPQ---------VLP 87
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEdrkrhgivpILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 88 IPEGVSVRQLVAYgrsphnSLWGRL-SGADQHSVDQALQRMELDTLA-ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:TIGR02633 356 VGKNITLSVLKSF------CFKMRIdAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-215 |
1.94e-13 |
|
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: 70.04 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATR--IVQDLSFSPPPAQVTALIGPNGCGKSTLLKafarILTPQAGSLSLDGTAYGK---LSANELAR 77
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFK----MLTGDTTVTSGDATVAGKsilTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 78 KVAFLPQVLPIPEGVSVRQlvaygrspHNSLWGRLSGADQHSVDQ----ALQRMELDTLAERPLSDLSGGQRQRAWLAMI 153
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGRE--------HLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 154 LAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-214 |
1.94e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 7 QQLDIGYGATRIVQdlsfsppPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLS----ANELARKVAFL 82
Cdd:PRK10584 21 HELSILTGVELVVK-------RGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQ---VLPIPEGVSVRQLVAYGRSPhnslwgrlsgADQHSVDQALQRMELDTLAER----PlSDLSGGQRQRAWLAMILA 155
Cdd:PRK10584 94 FQsfmLIPTLNALENVELPALLRGE----------SSRQSRNGAKALLEQLGLGKRldhlP-AQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-231 |
2.25e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDG--TAYGKLSANELARKVAF------------LPQ 84
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQRIRMIFqdpstslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 VLPIPEGVSVrQLVAYGRsphnslwgrlsgadQHSVDQALQRMEL--DTLAERPLSdLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK15112 109 ILDFPLRLNT-DLEPEQR--------------EKQIIETLRQVGLlpDHASYYPHM-LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAEL 231
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-172 |
2.38e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsanelarKVAF 81
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-----------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQvlpipegvsvrqlvayGRS---PHNSLWGRLS-GADQHSV-------------------DQalqrmeldtlaERPLS 138
Cdd:PRK11819 392 VDQ----------------SRDaldPNKTVWEEISgGLDIIKVgnreipsrayvgrfnfkggDQ-----------QKKVG 444
|
170 180 190
....*....|....*....|....*....|....
gi 499585766 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-197 |
3.33e-13 |
|
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: 65.64 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILtpQAGSlsldgtayGKLSANELARkVAFLPQVLPIPEGvSVR 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW--PWGS--------GRIGMPEGED-LLFLPQRPYLPLG-TLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAYgrsPhnslWGRLsgadqhsvdqalqrmeldtlaerplsdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:cd03223 82 EQLIY---P----WDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|..
gi 499585766 176 VELLDLMRELSAegkTVITVLH 197
Cdd:cd03223 128 DRLYQLLKELGI---TVISVGH 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-198 |
3.54e-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: 65.46 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPpaQVTALIGPNGCGKSTLLKAFARILTPQAgslsldgtaygklsanelarkvaflpQVLPIPEGVSVRQ 96
Cdd:cd03227 11 FVPNDVTFGEG--SLTIITGPNGSGKSTILDAIGLALGGAQ--------------------------SATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYgrsphnslwgrlsgadqhsvdqalQRMELDTLaerpLSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDI 172
Cdd:cd03227 63 IVAA------------------------VSAELIFT----RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180
....*....|....*....|....*.
gi 499585766 173 SHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-229 |
3.91e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGY----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDG----------TAYG 68
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 69 KLSANELAR-KVAFLPQVLPIPEgVSVRQLVAYGRSPHNSLwgRL-SGADQHSVDQALQRM-------ELDTLAERPLSD 139
Cdd:PRK10261 92 EQSAAQMRHvRGADMAMIFQEPM-TSLNPVFTVGEQIAESI--RLhQGASREEAMVEAKRMldqvripEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250
....*....|.
gi 499585766 219 TCGAPSDVLTA 229
Cdd:PRK10261 249 ETGSVEQIFHA 259
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-232 |
5.88e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-V 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPIPEGVSVRQLVAYGrsphnslwGRLsgADQHSVDQALQRME--LDTLAERPLS---DLSGGQRQRAWLAMIL 154
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMG--------GFF--AERDQFQERIKWVYelFPRLHERRIQragTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499585766 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELV 232
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-218 |
6.49e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.93 E-value: 6.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 13 YGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILtPQA---GSLSLDGTAYGKLSANELARK-VAFLPQVLPI 88
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 PEGVSVRQLVAYGRS-PHNSlwGRLSGADQ-HSVDQALQRMELDTL-AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:TIGR02633 90 VPELSVAENIFLGNEiTLPG--GRMAYNAMyLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-226 |
7.85e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQ-VTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYgklsaNELARKVaFLPqvlpiPEgvsvRQLVAY----GR 102
Cdd:PRK11144 22 PAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-----FDAEKGI-CLP-----PE----KRRIGYvfqdAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 103 -SPHNSLWGRL----SGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:PRK11144 87 lFPHYKVRGNLrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 178 LLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:PRK11144 167 LLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-227 |
9.00e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 20 QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipeGV-----SV 94
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ------NVhlfndTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSPHNSLWGRLSGADQ-HSVDqALQRME--LDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK11176 434 ANNIAYARTEQYSREQIEEAARMaYAMD-FINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 172 ISHQVELLDLMRELSAEgKTVITVLHDINqACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK11176 513 TESERAIQAALDELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-230 |
1.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQL 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYgrSPHN--SLWGRLSGAdqhSVDQALQR--MELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:PLN03232 1331 DPF--SEHNdaDLWEALERA---HIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499585766 174 HQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-197 |
2.86e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.82 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANeLARKVAFL 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQlvaygrsphNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13540 80 GHRSGINPYLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 499585766 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-218 |
3.78e-12 |
|
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: 63.42 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTpqAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQ 96
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 lvaygrsphnSLwgRLSGAdqhsvdqalqrmeldtlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQV 176
Cdd:cd03232 99 ----------AL--RFSAL---------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499585766 177 ELLDLMRELSAEGKTVITVLHDINQAC-RYADHLAVMQ-GGRMV 218
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKrGGKTV 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-231 |
3.80e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQaGSLSLDGTAYGKLSanelaRKvaflpQVLPI--------- 88
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLN-----RR-----QLLPVrhriqvvfq 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 -PEG-----VSVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMELD-TLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK15134 370 dPNSslnprLNVLQIIEEGLRVHQP---TLSAAQREQqVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 161 VLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDInQACRYADH-LAVMQGGRMVTCG-------APSDVLTAEL 231
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDL-HVVRALCHqVIVLRQGEVVEQGdcervfaAPQQEYTRQL 525
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-218 |
4.39e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 20 QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK-VAFLPQ------VLPIpegV 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEdrkaegIIPV---H 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVAYGRSPHNSLWGRL--SGADQHSVDQALQRMELDTL-AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLinNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-197 |
4.65e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFA-RIltpQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGVSVRQ---LVAYGRS 103
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAgRI---QGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVREtlvFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 104 PHN-SLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLM 182
Cdd:PLN03211 170 PKSlTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 499585766 183 RELSAEGKTVITVLH 197
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-217 |
9.90e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLS-ANELARKVAFLPQ-------VLPIPEGV 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEdrqssglYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 93 SVRQLVaYGRsphNSLWGRlSGADQHSVDQALQRMELD-TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK15439 361 NVCALT-HNR---RGFWIK-PARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-226 |
1.19e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKST-------LLKAFARIltpqAGSLSLDGTAYGKLSANEL----ARKVAFLPQ--- 84
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATFNGREILNLPEKELnklrAEQISMIFQdpm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 85 ---------------VLPIPEGV--------SVRQLvaygrsphnslwgrlsgaDQHSVDQALQRMELdtlaeRPlSDLS 141
Cdd:PRK09473 108 tslnpymrvgeqlmeVLMLHKGMskaeafeeSVRML------------------DAVKMPEARKRMKM-----YP-HEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRMVTC 220
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEY 243
|
....*.
gi 499585766 221 GAPSDV 226
Cdd:PRK09473 244 GNARDV 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-205 |
1.67e-11 |
|
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: 63.80 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPqagslsLDGTAygKLSANelaRKVAFLPQVLPIPEGVSVRQL 97
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEA--RPQPG---IKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRLS----------------------------GADQHSVDQALQrMELDTL----AERPLSDLSGGQR 145
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNeisakyaepdadfdklaaeqaelqeiidAADAWDLDSQLE-IAMDALrcppWDADVTKLSGGER 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 146 QRAWLAMILAQDAAIVLLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPGTVVAVTHD-----RY 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
34-217 |
1.72e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.84 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTllkaFARILT----PQAGSLSLDGtaygklsanelarkvaflpqvlpipEGVSVRQLVAYgRSPHNS-- 107
Cdd:PRK10522 354 LIGGNGSGKST----LAMLLTglyqPQSGEILLDG-------------------------KPVTAEQPEDY-RKLFSAvf 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 108 ----LWGRLSGADQHSVDQA-----LQRMELD---TLAERPLSD--LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD-- 171
Cdd:PRK10522 404 tdfhLFDQLLGPEGKPANPAlvekwLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDph 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 172 ---ISHQvELLDLMRELsaeGKTVITVLHDiNQACRYADHLAVMQGGRM 217
Cdd:PRK10522 484 frrEFYQ-VLLPLLQEM---GKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
19-208 |
2.04e-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: 61.47 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPpaqVTALIGPNGCGKSTLLKAFARILTPQaGSLSLDGTAYgklsANELARKVAFLPQVLPIPEGVSVRQLV 98
Cdd:cd03240 15 RSEIEFFSP---LTLIVGQNGAGKTTIIEALKYALTGE-LPPNSKGGAH----DPKLIREGEVRAQVKLAFENANGKKYT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 AYgRSPH---NSLWgrlsgadqhsVDQAlqrmELDTLAERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03240 87 IT-RSLAileNVIF----------CHQG----ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499585766 170 LDISH-QVELLDLMRE-LSAEGKTVITVLHDINQAcRYADH 208
Cdd:cd03240 152 LDEENiEESLAEIIEErKSQKNFQLIVITHDEELV-DAADH 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-210 |
2.18e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTLLKAFARILTPQAGSLSLD-GTAYGKLSANELarkvAFlpqvlpipEGVSVRQLVAYGrspHNSLWGRL 112
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQF----AF--------EEFTVLDTVIMG---HTELWEVK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 113 SGADQ-------------HSVDQALQRMELD--TLAER-----------------PLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK15064 97 QERDRiyalpemseedgmKVADLEVKFAEMDgyTAEARagelllgvgipeeqhygLMSEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 161 VLLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD---INQACryaDHLA 210
Cdd:PRK15064 177 LLLDEPTNNLDI-NTIRWLE--DVLNERNSTMIIISHDrhfLNSVC---THMA 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-197 |
2.37e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDgtaygkLSANELARKVAFLPQVLPIPE-GVSV 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASLIDAIGRKGDfKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSphnslwgrlsgadqhsvDQALQRmeldtlaeRPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:COG2401 117 ELLNAVGLS-----------------DAVLWL--------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....
gi 499585766 175 QVELLDLMRELSAE-GKTVITVLH 197
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-233 |
3.35e-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: 63.43 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 22 LSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTaygklsanelarkVAFLPQVLPIpEGVSVRQLVAYG 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWI-QNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 102 RSPHNSLWGRLSGADQHSVD-QALQRMELDTLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 181 --LMRELSAEGKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVLT-----AELVC 233
Cdd:TIGR00957 802 hvIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQrdgafAEFLR 860
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-215 |
4.05e-11 |
|
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: 61.19 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARK----VAFLPQVlPIPEGVSV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK-PWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGrSPHNSLWGRL---SGADQHSVDqALQRMELDTLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03290 96 EENITFG-SPFNKQRYKAvtdACSLQPDID-LLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 172 ISHQVELLD--LMRELSAEGKTVITVLHDInQACRYADHLAVMQGG 215
Cdd:cd03290 173 IHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
140-229 |
4.28e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 62.07 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS-AEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|.
gi 499585766 219 TCGAPSDVLTA 229
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
97-243 |
4.73e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAYGRSphnSLWGRL-SGADQHSVDQALQRMELDTL-AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK13549 364 LAALDRF---TGGSRIdDAAELKTILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499585766 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRmvtcgapsdvLTAELVCQVFDvQVQIM 243
Cdd:PRK13549 441 KYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK----------LKGDLINHNLT-QEQVM 498
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-202 |
5.35e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLkafaRILT----PQAGSLSLDGTAYGKLSAnELARKV 79
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLL----RILAglarPDAGEVLWQGEPIRRQRD-EYHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFLPQVLPI-PEgvsvrqLVAYgrspHNSLW-GRLSG-ADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK13538 77 LYLGHQPGIkTE------LTAL----ENLRFyQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLT 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499585766 157 DAAIVLLDEPTTYLDiSHQVELL-DLMRELSAEGKTVI-TVLHDINQA 202
Cdd:PRK13538 147 RAPLWILDEPFTAID-KQGVARLeALLAQHAEQGGMVIlTTHQDLPVA 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-194 |
8.69e-11 |
|
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: 61.85 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 16 TRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklsanelarKVAFLPQVLPIPEGvSVR 95
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 96 QLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LDTLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:TIGR01271 505 DNIIFGLS-----------YDEYrytSVIKACQLEEdIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLLD 573
|
170 180 190
....*....|....*....|....*....|..
gi 499585766 165 EPTTYLDISHQVELLD--LMRELSAEGKTVIT 194
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFEscLCKLMSNKTRILVT 605
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-230 |
9.36e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 22 LSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVR-QLVAY 100
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-PVLFSGTVRfNLDPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 101 GRSPHNSLWgrlsgadqhsvdQALQRMEL-DTLAERPL----------SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PLN03130 1337 NEHNDADLW------------ESLERAHLkDVIRRNSLgldaevseagENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 170 LDISHQVELLDLMRElsaEGK--TVITVLHDINQA--CryaDHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:PLN03130 1405 VDVRTDALIQKTIRE---EFKscTMLIIAHRLNTIidC---DRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-218 |
1.01e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAFLPQVLPIPEGVSVRQLVAYGRSPHN 106
Cdd:PRK10982 23 PHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDNMWLGRYPTK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 107 SLWgrlsgadqhsVDQAlqRMELDTLA-----------ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL---DI 172
Cdd:PRK10982 103 GMF----------VDQD--KMYRDTKAifdeldididpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 173 SHqveLLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:PRK10982 171 NH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-230 |
1.25e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 7 QQLDIGYGATRIV-QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQV 85
Cdd:PRK10790 344 DNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 86 lPIPEGVSVRQLVAYGRSphnslwgrlsgADQHSVDQALQRMELDTLAeRPLSD------------LSGGQRQRAWLAMI 153
Cdd:PRK10790 424 -PVVLADTFLANVTLGRD-----------ISEEQVWQALETVQLAELA-RSLPDglytplgeqgnnLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 154 LAQDAAIVLLDEPTTYLD------ISHQvelLDLMRELSaegkTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK10790 491 LVQTPQILILDEATANIDsgteqaIQQA---LAAVREHT----TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
...
gi 499585766 228 TAE 230
Cdd:PRK10790 563 AAQ 565
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-215 |
1.34e-10 |
|
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: 60.26 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 15 ATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklsanelarKVAFLPQVLPIPEGvSV 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 95 RQLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LDTLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03291 115 KENIIFGVS-----------YDEYrykSVVKACQLEEdITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499585766 164 DEPTTYLDISHQVELLD-LMRELSAEgKTVITVLHDINQaCRYADHLAVMQGG 215
Cdd:cd03291 184 DSPFGYLDVFTEKEIFEsCVCKLMAN-KTRILVTSKMEH-LKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-226 |
1.45e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 22 LSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVLPIPEGvSVRQLVayg 101
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 102 rSPhnslwgrLSGADQHSVDQALqrmELDTLAERPLSDLSG--------------GQRQRAWLA-MILAQDAAIVLLDEP 166
Cdd:PTZ00243 1405 -DP-------FLEASSAEVWAAL---ELVGLRERVASESEGidsrvleggsnysvGQRQLMCMArALLKKGSGFILMDEA 1473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 167 TTYLD--ISHQVElLDLMRELSAegKTVITVLHDINQACRYaDHLAVMQGGRMVTCGAPSDV 226
Cdd:PTZ00243 1474 TANIDpaLDRQIQ-ATVMSAFSA--YTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-172 |
1.55e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTLLKafarILtpqAGSLSLDGtayGKLS-ANELarKVAFLPQVLP----------IPEGVS--------- 93
Cdd:PRK11147 34 LVGRNGAGKSTLMK----IL---NGEVLLDD---GRIIyEQDL--IVARLQQDPPrnvegtvydfVAEGIEeqaeylkry 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 94 --VRQLVAYGRSP--------------HNSLWgRLsgadQHSVDQALQRMELDtlAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK11147 102 hdISHLVETDPSEknlnelaklqeqldHHNLW-QL----ENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSN 174
|
170
....*....|....*
gi 499585766 158 AAIVLLDEPTTYLDI 172
Cdd:PRK11147 175 PDVLLLDEPTNHLDI 189
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-230 |
1.95e-10 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 59.54 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVR-QLVAYGRSPHN 106
Cdd:cd03288 46 PGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD-PILFSGSIRfNLDPECKCTDD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 107 SLWGRLSGADQHSVDQALQRmELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS 186
Cdd:cd03288 125 RLWEALEIAQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAF 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499585766 187 AEgKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSDVLTAE 230
Cdd:cd03288 204 AD-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
121-228 |
2.23e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 121 DQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDIN 200
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
|
90 100
....*....|....*....|....*...
gi 499585766 201 QACRYADHLAVMQGGRMVTCGAPSDVLT 228
Cdd:NF000106 206 EAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-198 |
5.18e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.41 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygklsanelarKVAFLPQVLPIPEgVSVRQLVAYGRSPHNS 107
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNW-----------QLAWVNQETPALP-QPALEYVIDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 108 LWGRLSGADQHSVDQALQRM--ELDTLA----------------------ERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10636 94 LEAQLHDANERNDGHAIATIhgKLDAIDawtirsraasllhglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 499585766 164 DEPTTYLDIShqvELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10636 174 DEPTNHLDLD---AVIWLEKWLKSYQGTLILISHD 205
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-218 |
5.46e-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: 56.95 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLkafariltpqagslsLDGtaygkLSANELARKVAFLPQVLPIPEgVSVRQLv 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEG-----LYASGKARLISFLPKFSRNKL-IFIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 aygrsphnslwgrlsgadQHSVDQALQRMELDtlaeRPLSDLSGGQRQRAWLAMILAQDA--AIVLLDEPTTYLDISHQV 176
Cdd:cd03238 69 ------------------QFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499585766 177 ELLDLMRELSAEGKTVITVLHDINQACrYADHLAVM------QGGRMV 218
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVV 173
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-197 |
7.33e-10 |
|
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: 58.48 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 17 RIVQDLSFSPPPaQVTALIGPNGCGKSTLLKAFARILTPQAG-SLSLD-------------------GTAYGKL------ 70
Cdd:COG3593 12 RSIKDLSIELSD-DLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEdfylgddpdlpeieieltfGSLLSRLlrlllk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 71 --SANELARKVAFLPQVLpIPEGVSVRQLV-----AYGRSPHNSLwgRLSGADQHSVDQALqRMELDTLAERPLSDLSGG 143
Cdd:COG3593 91 eeDKEELEEALEELNEEL-KEALKALNELLseylkELLDGLDLEL--ELSLDELEDLLKSL-SLRIEDGKELPLDRLGSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 144 QRQRAWLAMILA-------QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3593 167 FQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-198 |
7.49e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 4 LKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLsldgtaygKLSANElarKVAFLP 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 84 Q--VLPIPEGVSVRQLVAYGRSPhnslwgrlsGADQHSVDQALQRM---ELDtlAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK15064 389 QdhAYDFENDLTLFDWMSQWRQE---------GDDEQAVRGTLGRLlfsQDD--IKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499585766 159 AIVLLDEPTTYLDIsHQVELLDLMRELsAEGkTVITVLHD 198
Cdd:PRK15064 458 NVLVMDEPTNHMDM-ESIESLNMALEK-YEG-TLIFVSHD 494
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-221 |
7.64e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTP---QAGSLSLDGtayGKLSANeLARKVAFLPQV-LPIPEgVSVR---QLVAY 100
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG---RPLDSS-FQRSIGYVQQQdLHLPT-STVReslRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 101 GRSPHNslwgrLSGADQHS-VDQALQRMELDTLAER----PLSDLSGGQRQRAWLAMIL-AQDAAIVLLDEPTTYLDISH 174
Cdd:TIGR00956 863 LRQPKS-----VSKSEKMEyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQT 937
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 175 QVELLDLMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRMVTCG 221
Cdd:TIGR00956 938 AWSICKLMRKLADHGQAILCTIHqpsaILFEE---FDRLLLLQkGGQTVYFG 986
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-194 |
1.18e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAygkLSANELARKVAFL 82
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVSVRQLVAYgrspHNSLWGRLSgadQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13543 88 GHLPGLKADLSTLENLHF----LCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|....
gi 499585766 163 LDEPTTYLDIShQVELLDLM--RELSAEGKTVIT 194
Cdd:PRK13543 161 LDEPYANLDLE-GITLVNRMisAHLRGGGAALVT 193
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-185 |
1.56e-09 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 56.93 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPaQVTALIGPNGCGKSTLLKAFARILTPQAGSLSL--------------------------------DGTAYG 68
Cdd:COG3950 18 EIDFDNPP-RLTVLVGENGSGKTTLLEAIALALSGLLSRLDDvkfrkllirngefgdsaklilyygtsrllldgPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 69 KLSANELARKVAFLPQvlpIPEGVSVRQLVAYGRSPHNSLWGR-------------------LSGADQHSVD-QALQRME 128
Cdd:COG3950 97 RLKEEYFSRLDGYDSL---LDEDSNLREFLEWLREYLEDLENKlsdeldekleavrealnklLPDFKDIRIDrDPGRLVI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 129 LDTLAER-PLSDLSGGQRQR-AWLAMILAQDA-------------AIVLLDEPTTYLDISHQVELLDLMREL 185
Cdd:COG3950 174 LDKNGEElPLNQLSDGERSLlALVGDLARRLAelnpalenplegeGIVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-205 |
2.96e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 34 LIGPNGCGKSTLLKAFARILTPqagslsLDGTAYgkLSANelaRKVAFLPQVLPIPEGVSVRQLV--------------- 98
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKE------FEGEAR--PAPG---IKVGYLPQEPQLDPEKTVRENVeegvaevkaaldrfn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 ----AYGRSPHNS---------LWGRLSGADQHSVDQALQrMELDTL----AERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11819 107 eiyaAYAEPDADFdalaaeqgeLQEIIDAADAWDLDSQLE-IAMDALrcppWDAKVTKLSGGERRRVALCRLLLEKPDML 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499585766 162 LLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:PRK11819 186 LLDEPTNHLD-AESVAWLE--QFLHDYPGTVVAVTHD-----RY 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-227 |
3.43e-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: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 129 LDTLA-ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLdisHQVE---LLDLMRELSAEGKTVITVLHDiNQA 202
Cdd:TIGR00630 477 LDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDnrrLINTLKRLRDLGNTLIVVEHD-EDT 552
|
90 100 110
....*....|....*....|....*....|.
gi 499585766 203 CRYADHL------AVMQGGRMVTCGAPSDVL 227
Cdd:TIGR00630 553 IRAADYVidigpgAGEHGGEVVASGTPEEIL 583
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-198 |
6.25e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSL-DGTAYGKLSANELarkvaf 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQL------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 lpqvlpipegvsvrqlvAYGRSPHNSLwgrlsgadQHSVDQALQRMEL-------------DTLAErPLSDLSGGQRQRA 148
Cdd:PRK10636 386 -----------------EFLRADESPL--------QHLARLAPQELEQklrdylggfgfqgDKVTE-ETRRFSGGEKARL 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsaEGKTVItVLHD 198
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVV-VSHD 486
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-227 |
6.48e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.21 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklSANELARKVAFLPQVLPIpEGVSVRQL- 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTGI-ENIEFKMLc 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLwgrlsgadqhsVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:PRK13546 113 MGFKRKEIKAM-----------TPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 178 LLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVL 227
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-221 |
6.60e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.87 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQVlPIPEGVSVRQL 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-PFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRsphnslwgrlSGADQHSVDQA--LQRMELDTL----------AERPLSdLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK10789 409 IALGR----------PDATQQEIEHVarLASVHDDILrlpqgydtevGERGVM-LSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499585766 166 PTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRMVTCG 221
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-197 |
7.10e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDgtAYGKLsanelarkvAFLPQVLPIPEGvSVRQL 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--AKGKL---------FYVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRLSGADqhsVDQALQRMELDTLAERPLS---------DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKD---LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|
gi 499585766 169 ylDISHQVEllDLMRELSAE-GKTVITVLH 197
Cdd:TIGR00954 612 --AVSVDVE--GYMYRLCREfGITLFSVSH 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-194 |
9.92e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTP-QAGSLSLDGTaygklsanelarkVAFLPQVlPIPEGVSVRQL 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS-------------VAYVPQV-SWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYGRSPHNSLWGRL--SGADQHSVDQALQRmELDTLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--IS 173
Cdd:PLN03232 699 ILFGSDFESERYWRAidVTALQHDLDLLPGR-DLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVA 776
|
170 180
....*....|....*....|.
gi 499585766 174 HQVELLDLMRELSAEGKTVIT 194
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVT 797
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-231 |
9.97e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDI-GYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL-ARKV 79
Cdd:COG3845 256 VVLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 80 AFlpqvlpIPE-----GV----SVRQ--LVAYGRSPHNSLWGRLSgadqhsvdqalqRMELDTLAER------------- 135
Cdd:COG3845 336 AY------IPEdrlgrGLvpdmSVAEnlILGRYRRPPFSRGGFLD------------RKAIRAFAEElieefdvrtpgpd 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 136 -PLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQG 214
Cdd:COG3845 398 tPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
250
....*....|....*..
gi 499585766 215 GRMVTCGAPSDVLTAEL 231
Cdd:COG3845 478 GRIVGEVPAAEATREEI 494
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-200 |
1.39e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLdgtaygklsanelarkvaflpqvlpipegvsvrqlvaygrsphns 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 108 lwgrLSGADQHSVDQALQRMELDTlaeRPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD------L 181
Cdd:smart00382 36 ----IDGEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170
....*....|....*....
gi 499585766 182 MRELSAEGKTVITVLHDIN 200
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEK 127
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-232 |
1.48e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtayGKLSANELA--RKVAFLPQVLPIPEGVSVRQ 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDIAtrRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 -LVAYGRSPHnslwgrLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLA--MILAQDaaIVLLDEPTTYLDI 172
Cdd:NF033858 359 nLELHARLFH------LPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLAvaVIHKPE--LLILDEPTSGVDP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 173 SHQVELLDLMRELSAEGKTVITV-LHDINQACRyADHLAVMQGGRMVTCGAPsdvltAELV 232
Cdd:NF033858 431 VARDMFWRLLIELSREDGVTIFIsTHFMNEAER-CDRISLMHAGRVLASDTP-----AALV 485
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-217 |
1.55e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANE-LARKVAFLPQ-------VLpipe 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEdrkrdglVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 GVSVRQ---LVAYGRspHNSLWGRLSGAD-QHSVDQALQRMELDTLA-ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK10762 344 GMSVKEnmsLTALRY--FSRAGGSLKHADeQQAVSDFIRLFNIKTPSmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499585766 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-217 |
1.73e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GY-GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSL--------------SLDGTaygKLSANELA 76
Cdd:PLN03073 517 GYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGL---DLSSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQVlpiPEGVSVRQLVAYGrsphnslwgrLSGadqhsvdqalqrmeldTLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PLN03073 594 YMMRCFPGV---PEQKLRAHLGSFG----------VTG----------------NLALQPMYTLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499585766 157 DAAIVLLDEPTTYLDIShQVELldLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:PLN03073 645 KPHILLLDEPSNHLDLD-AVEA--LIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-221 |
2.31e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.94 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 35 IGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL--ARK---VAFLPQVLPIPEGVSVRQLVAygrSPHNSLW 109
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSdiqMIFQDPLASLNPRMTIGEIIA---EPLRTYH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 110 GRLSGADqhsVDQALQRME-----LDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRE 184
Cdd:PRK15079 130 PKLSRQE---VKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 499585766 185 LSAE-GKTVITVLHDINQACRYADHLAVMQGGRMVTCG 221
Cdd:PRK15079 207 LQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-218 |
2.72e-08 |
|
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: 52.65 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILtpqAGSLSLDGT-AYGKLSANELARK----VAFLPQV-LPIPEg 91
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDiHYNGIPYKEFAEKypgeIIYVSEEdVHFPT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 92 VSVRQLVAYGRsphnslwgRLSGADQhsvdqalqrmeldtlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03233 98 LTVRETLDFAL--------RCKGNEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499585766 172 ISHQVELLDLMRELSAEGKTVITVlhDINQACR--YA--DHLAVMQGGRMV 218
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTFV--SLYQASDeiYDlfDKVLVLYEGRQI 199
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-218 |
2.74e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 20 QDLSFSPPPAQVTALIGPNGCGKSTLLKafarILT---PQA---GSLSLDGT--AYGKLSANElARKVAFLPQVLP-IPE 90
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMK----VLSgvyPHGsyeGEILFDGEvcRFKDIRDSE-ALGIVIIHQELAlIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 gVSVRQLVAYGRSPhnSLWGRLSGADQHS-VDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:NF040905 93 -LSIAENIFLGNER--AKRGVIDWNETNRrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRMV 218
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-171 |
4.10e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 11 IGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKafarILT---PQAGSLSLdgTAYGKLSAN-----ELARKVAFL 82
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITgdhPQGYSNDL--TLFGRRRGSgetiwDIKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 83 PQVLPIPEGVS--VRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDT-LAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK10938 342 SSSLHLDYRVStsVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170
....*....|..
gi 499585766 160 IVLLDEPTTYLD 171
Cdd:PRK10938 422 LLILDEPLQGLD 433
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
19-197 |
5.55e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 52.08 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPpaqVTALIGPNGCGKSTLLKAFARiltpQAGSLSLDGTAYGKLSANELARKvafLPQVLpipegvsvrQLV 98
Cdd:COG3910 30 LEGLEFHPP---VTFFVGENGSGKSTLLEAIAV----AAGFNPEGGSKNFRFSTRESESA---LGEYL---------RLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 99 aygRSPHNSLWGR-LSGADQHSVDQALQRMELDTLA------ERPLSDLSGGQrqrAWLAMILA--QDAAIVLLDEPTTY 169
Cdd:COG3910 91 ---RGLPKPRDGFfLRAESFFNVATYLDELAAEGPGildsygGRSLHEQSHGE---SFLALFENrfRGNGLYLLDEPEAA 164
|
170 180
....*....|....*....|....*...
gi 499585766 170 LDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3910 165 LSPSRQLALLALIHDLVREGSQFIIATH 192
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
122-223 |
1.27e-07 |
|
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: 51.46 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 122 QALQRMELD--TLAeRPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVI 193
Cdd:cd03271 151 QTLCDVGLGyiKLG-QPATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKK---LLEVLQRLVDKGNTVV 226
|
90 100 110
....*....|....*....|....*....|....*.
gi 499585766 194 TVLHDINQAcRYADHLAVM------QGGRMVTCGAP 223
Cdd:cd03271 227 VIEHNLDVI-KCADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-221 |
1.39e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTpqAGSLSLDGTAYGKLSANE-LARKVAFLPQVLPIPEGVSVRQLVAYgrSPHN 106
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIRISGFPKKQEtFARISGYCEQNDIHSPQVTVRESLIY--SAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 107 SLWGRLSGADQHS-VDQALQRMELDTLAER-----PLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:PLN03140 981 RLPKEVSKEEKMMfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499585766 181 LMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRMVTCG 221
Cdd:PLN03140 1061 TVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKrGGQVIYSG 1103
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-234 |
1.72e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 33 ALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQ------VLPIPE--GVSVRQLVAYGrSP 104
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQrnntdmLSPGEDdtGRTTAEIIQDE-VK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 105 HNSLWGRLSgadqhsvdqalQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRE 184
Cdd:PRK10938 112 DPARCEQLA-----------QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499585766 185 LSAEGKTVITVLHDINQACRYADHLAVMQGGRMVTCGAPSDVLTAELVCQ 234
Cdd:PRK10938 181 LHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQ 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
134-221 |
3.02e-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: 49.95 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 134 ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVid 210
|
90
....*....|....*.
gi 499585766 210 ----AVMQGGRMVTCG 221
Cdd:cd03270 211 igpgAGVHGGEIVAQG 226
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
119-226 |
4.51e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 119 SVDQALQRME--------LDTLAE---------RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHq 175
Cdd:COG0178 789 TVEEALEFFEnipkiarkLQTLQDvglgyiklgQPATTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDIRK- 867
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 176 veLLDLMRELSAEGKTVITVLHD---InqacRYADHLAVM------QGGRMVTCGAPSDV 226
Cdd:COG0178 868 --LLEVLHRLVDKGNTVVVIEHNldvI----KTADWIIDLgpeggdGGGEIVAEGTPEEV 921
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-225 |
4.51e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFariltpqagsLSLDGTAYGKLSAnelARKVAFLPQVLPIPEGvSVRQL 97
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL----------LSQFEISEGRVWA---ERSIAYVPQQAWIMNA-TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 98 VAYgRSPHNSlwGRLSGA---DQHSVDQALQRMELDT-LAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDiS 173
Cdd:PTZ00243 741 ILF-FDEEDA--ARLADAvrvSQLEADLAQLGGGLETeIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALD-A 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499585766 174 HQVELldLMREL---SAEGKTVITVLHDINQACRyADHLAVMQGGRMVTCGAPSD 225
Cdd:PTZ00243 816 HVGER--VVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-171 |
5.55e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.71 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVqDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSldgtaYGKLSANELARK-VAF 81
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPyCTY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 82 LPQVLPIPEGVSVRQLVAYGRSPHNSLwgrlsgadqHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK13541 75 IGHNLGLKLEMTVFENLKFWSEIYNSA---------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170
....*....|
gi 499585766 162 LLDEPTTYLD 171
Cdd:PRK13541 146 LLDEVETNLS 155
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-212 |
6.72e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 18 IVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSL-DGTAYGKLSANELARKVAFLPQVlPIPEGVSVRQ 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 97 LVAY------------------------GRSPHNSLWGRLSGaDQHSVDQALQRMEL----------------------- 129
Cdd:PTZ00265 479 NIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAG-DLNDMSNTTDSNELiemrknyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 130 ------------DTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVL 196
Cdd:PTZ00265 558 ihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIA 637
|
250
....*....|....*.
gi 499585766 197 HDINqACRYADHLAVM 212
Cdd:PTZ00265 638 HRLS-TIRYANTIFVL 652
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-201 |
7.97e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGtaygklSANELARKVAFLPQVLPIpEGVSVRQLvay 100
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGL--- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 101 grsphnsLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:PRK13545 112 -------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|.
gi 499585766 181 LMRELSAEGKTVITVLHDINQ 201
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQ 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-217 |
8.00e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 19 VQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANEL----------ARKVAFLPQVLPI 88
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 89 pegvSVRQLVAYGRSPHNSlWGRLSGADQHSVDQ-ALQRMELDTLAER-PLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK10982 344 ----GFNSLISNIRNYKNK-VGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499585766 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRM 217
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-250 |
9.12e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 134 ERPLSDLSGGQRQRAWLAMILAQDAAIV--LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIid 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499585766 210 ----AVMQGGRMVTCGAP------SDVLTAELVCQVFDVQVQIMREPVAGT 250
Cdd:PRK00635 550 igpgAGIFGGEVLFNGSPreflakSDSLTAKYLRQELTIPIPEKRTNSLGT 600
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-226 |
9.33e-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: 49.63 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 135 RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVITVLHDINqACRYADH 208
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVVVIEHNLD-VIKTADY 900
|
90 100
....*....|....*....|....
gi 499585766 209 LAVM------QGGRMVTCGAPSDV 226
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-221 |
1.02e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 2 TILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFA-----RILTpqaGSLSLDGTAYGKLSANELA 76
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKILE---GDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 77 RKVAFLPQVLP--IPeGVSvrqlvaygrsphNSLWGRLSgadQHSVDQALQRMELDTLA-------------------ER 135
Cdd:CHL00131 83 HLGIFLAFQYPieIP-GVS------------NADFLRLA---YNSKRKFQGLPELDPLEfleiineklklvgmdpsflSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 136 PLSD-LSGGQRQR-AWLAMILAqDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdinqacrYA------- 206
Cdd:CHL00131 147 NVNEgFSGGEKKRnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQrlldyik 218
|
250
....*....|....*.
gi 499585766 207 -DHLAVMQGGRMVTCG 221
Cdd:CHL00131 219 pDYVHVMQNGKIIKTG 234
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-209 |
2.27e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 118 HSVDQALQRMELDTLA-ERPLSDLSGGQRQRAWLAMIL---AQDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTV 192
Cdd:PRK00635 787 HEKIHALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH-THDIKaLIYVLQSLTHQGHTV 865
|
90
....*....|....*..
gi 499585766 193 ITVLHDINqACRYADHL 209
Cdd:PRK00635 866 VIIEHNMH-VVKVADYV 881
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-229 |
3.32e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 1 MTILKAQQLDIGY----GATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFARI----LTPQAGSLSLDGTAYGKLSA 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 73 NE----LARKVAFL---PQVLPIPEGVSVRQLV-AYGRSPHNSLWGRLSGADQHSVDQALQRMEL----DTLAERPLsDL 140
Cdd:PRK15093 81 RErrklVGHNVSMIfqePQSCLDPSERVGRQLMqNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkdhkDAMRSFPY-EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVL-HDINQACRYADHLAVMQGGRMVT 219
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIsHDLQMLSQWADKINVLYCGQTVE 239
|
250
....*....|
gi 499585766 220 CGAPSDVLTA 229
Cdd:PRK15093 240 TAPSKELVTT 249
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
131-230 |
3.44e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 131 TLAeRPLSDLSGGQRQRAWLAmilAQdaaI------VL--LDEPTTYLdisHQ------VELLDLMRELsaeGKTVITVL 196
Cdd:PRK00349 482 TLS-RSAGTLSGGEAQRIRLA---TQ---IgsgltgVLyvLDEPSIGL---HQrdndrlIETLKHLRDL---GNTLIVVE 548
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 499585766 197 HDiNQACRYADHL------AVMQGGRMVTCGAPSDVLTAE 230
Cdd:PRK00349 549 HD-EDTIRAADYIvdigpgAGVHGGEVVASGTPEEIMKNP 587
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-221 |
4.17e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 3 ILKAQQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFA--RILTPQAGSLSLDGTAYGKLSANELARKVA 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 81 FLPQVLP--IPeGVSVR-----QLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELDTLAERPLSDLSGGQRQRAWLAMI 153
Cdd:PRK09580 81 FMAFQYPveIP-GVSNQfflqtALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 154 LAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdINQACRY--ADHLAVMQGGRMVTCG 221
Cdd:PRK09580 160 AVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
|
|
| 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 499585766 133 AERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-230 |
1.15e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 137 LSDLSGGQRQRAWLAMIL---AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDInQACRYADHLAVM- 212
Cdd:PRK00635 1697 LSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMg 1775
|
90 100
....*....|....*....|...
gi 499585766 213 -----QGGRMVTCGAPSDVLTAE 230
Cdd:PRK00635 1776 pgsgkTGGKILFSGPPKDISASK 1798
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-201 |
1.21e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 21 DLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTPQA-GSLSLDGTaygklsanelarkVAFLPQVLPIPEGvSVRQLVA 99
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 100 YGrSPHNSlwGRLSGAdqhsVD-QALQRmELDTLAERPLSD-------LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PLN03130 701 FG-SPFDP--ERYERA----IDvTALQH-DLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190
....*....|....*....|....*....|....*
gi 499585766 172 --ISHQVELLDLMRELSaeGKTVITV---LHDINQ 201
Cdd:PLN03130 773 ahVGRQVFDKCIKDELR--GKTRVLVtnqLHFLSQ 805
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
20-55 |
1.58e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.82 E-value: 1.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 499585766 20 QDLSFSPPPAQVTALIGPNGCGKSTLLKAFARILTP 55
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP 48
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
20-61 |
1.82e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 44.41 E-value: 1.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499585766 20 QDLSFSPPpaqVTALIGPNGCGKSTLLKAFARILTPQAGSLS 61
Cdd:pfam13476 12 QTIDFSKG---LTLITGPNGSGKTTILDAIKLALYGKTSRLK 50
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
119-226 |
2.71e-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: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 119 SVDQALQRMELDTLAERPL---SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMREL-SAEGKTVIT 194
Cdd:TIGR03269 145 AVGRAVDLIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVL 224
|
90 100 110
....*....|....*....|....*....|..
gi 499585766 195 VLHDINQACRYADHLAVMQGGRMVTCGAPSDV 226
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
131-230 |
3.32e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 131 TLAeRPLSDLSGGQRQRAWLAmilaqdAAI------VL--LDEPTTYLdisHQ---VELLDLMRELSAEGKTVITVLHDi 199
Cdd:COG0178 478 TLD-RSAGTLSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGL---HQrdnDRLIETLKRLRDLGNTVIVVEHD- 546
|
90 100 110
....*....|....*....|....*....|....*..
gi 499585766 200 NQACRYADHL------AVMQGGRMVTCGAPSDVLTAE 230
Cdd:COG0178 547 EDTIRAADYIidigpgAGEHGGEVVAQGTPEEILKNP 583
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-71 |
4.77e-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: 43.92 E-value: 4.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 499585766 31 VTALIGPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLS 71
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGG 41
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
127-193 |
7.18e-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: 7.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 127 MELDTLAERPLSDLSGGQRQraWLAMILA-----QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:pfam13304 224 LENGGGGELPAFELSDGTKR--LLALLAAllsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-198 |
7.96e-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: 42.64 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 12 GYGATRIVQDLSFSPPPAQVTALI-GPNGCGKSTLLKAFARILTPQAGSLSLDGTAYGKLSANELARKVAFLPQvlpipe 90
Cdd:cd03279 10 NFGPFREEQVIDFTGLDNNGLFLIcGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 91 gvsvrqlvaygRSPHNSLWGRLSGADQHSVDQA--LQRMELDTLAERPLSDLSGGQRQRAWLAM------ILAQDAAIVL 162
Cdd:cd03279 84 -----------LGGKKYRVERSRGLDYDQFTRIvlLPQGEFDRFLARPVSTLSGGETFLASLSLalalseVLQNRGGARL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 499585766 163 ----LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03279 153 ealfIDEGFGTLDPEALEAVATALELIRTENRMVGVISHV 192
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
27-50 |
1.52e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.61 E-value: 1.52e-04
10 20
....*....|....*....|....
gi 499585766 27 PPAQVTALIGPNGCGKSTLLKAFA 50
Cdd:COG4637 19 PLGPLTVLIGANGSGKSNLLDALR 42
|
|
| 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 499585766 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDI 199
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRI 1419
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
140-226 |
2.64e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 LSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVITVLH--DInqaCRYADHLAV 211
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHnlDV---IKTADWIID 904
|
90 100
....*....|....*....|.
gi 499585766 212 M------QGGRMVTCGAPSDV 226
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEV 925
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
140-193 |
4.61e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 4.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 499585766 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-209 |
8.09e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 140 LSGGQRQ------RAWLAMILAQ----DAAI--VLLDEPTTYLD---ISHQVELLDLMRELSAEgkTVITVLHDiNQACR 204
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEgiegDAPLppLILDEPTVFLDsghVSQLVDLVESMRRLGVE--QIVVVSHD-DELVG 858
|
....*
gi 499585766 205 YADHL 209
Cdd:PRK02224 859 AADDL 863
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
20-50 |
9.84e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.03 E-value: 9.84e-04
10 20 30
....*....|....*....|....*....|....
gi 499585766 20 QDLSF---SPPPAQVTALIGPNGCGKSTLLKAFA 50
Cdd:COG1106 17 LTLSMvasGLRLLRVNLIYGANASGKSNLLEALY 50
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
27-56 |
1.20e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 40.11 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|
gi 499585766 27 PPAQVTALIGPNGCGKSTLLKAFARILTPQ 56
Cdd:COG5192 67 PPPFIVAVVGPPGTGKSTLIRSLVRRFTKQ 96
|
|
| 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
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
28-56 |
4.49e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 38.01 E-value: 4.49e-03
10 20
....*....|....*....|....*....
gi 499585766 28 PAQVTALIGPNGCGKSTLLKAFARILTPQ 56
Cdd:TIGR00602 109 PKRILLITGPSGCGKSTTIKILSKELGIQ 137
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-197 |
5.15e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 7 QQLDIGYGATRIVQDLSFSPPPAQVTALIGPNGCGKSTLLKAFA-----------RILTPQAGSLSLDGTAYGKLSANEL 75
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncQILHVEQEVVGDDTTALQCVLNTDI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499585766 76 ARKVAFLPQVLPIPEGVSVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMEL---DTLAERPLSDL------------ 140
Cdd:PLN03073 261 ERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELidaYTAEARAASILaglsftpemqvk 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499585766 141 -----SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVelLDLMRELSAEGKTVITVLH 197
Cdd:PLN03073 341 atktfSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV--LWLETYLLKWPKTFIVVSH 399
|
|
| 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 499585766 137 LSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDISH 174
Cdd:cd03273 164 LTELSGGQRSLVALSLILAlllfKPAPMYILDEVDAALDLSH 205
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
23-48 |
9.72e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 36.29 E-value: 9.72e-03
10 20 30
....*....|....*....|....*....|.
gi 499585766 23 SFSPP-----PAQVTALIGPNGCGKSTLLKA 48
Cdd:cd03278 11 SFADKttipfPPGLTAIVGPNGSGKSNIIDA 41
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