|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-246 |
7.03e-107 |
|
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: 309.67 E-value: 7.03e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVK 240
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
....*.
gi 547260874 241 LMLHPD 246
Cdd:COG1120 241 VIEDPV 246
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-247 |
8.56e-77 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 233.37 E-value: 8.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTC 92
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:PRK11231 94 RELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 173 QYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEapVKLMLHPDP 247
Cdd:PRK11231 174 QVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFD--VEAEIHPEP 245
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-245 |
1.01e-74 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 228.52 E-value: 1.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTC 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:PRK10575 103 RELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 173 QYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVKLMLHP 245
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHP 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-246 |
8.50e-71 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 218.03 E-value: 8.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAF 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDdVS-LTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGLTCRELVRLGRFPWRGlfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVM 159
Cdd:COG4604 80 LRQENHINSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 160 ILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPV 239
Cdd:COG4604 158 LLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDI 237
|
....*..
gi 547260874 240 KLMLHPD 246
Cdd:COG4604 238 EVEEIDG 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-251 |
3.35e-69 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 214.21 E-value: 3.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLGRFPWrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQ------ 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 155 ASP-VMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRT 233
Cdd:COG4559 157 GGPrWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250
....*....|....*...
gi 547260874 234 LFEAPVKLMLHPDPPAAY 251
Cdd:COG4559 236 VYGADLRVLAHPEGGCPQ 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-220 |
8.46e-69 |
|
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: 210.37 E-value: 8.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 klpasegltcrelvrlgrfpwrglfgrwraedeaavdeALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILD 162
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 163 EPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-246 |
2.45e-66 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 206.93 E-value: 2.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLGRFPWrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQ------ 154
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 155 ASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTL 234
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250
....*....|..
gi 547260874 235 FEAPVKLMLHPD 246
Cdd:PRK13548 238 YGADVLVQPHPE 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-239 |
6.82e-63 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 198.29 E-value: 6.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELVRLGRF 101
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLE 181
Cdd:PRK10253 108 PHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 182 RLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG------AELLHSEENLR-TLFEAPV 239
Cdd:PRK10253 188 ELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGApkeivtAELIERIYGLRcMIIDDPV 252
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-244 |
5.11e-62 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 195.31 E-value: 5.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlseRERAQRAAFLP 81
Cdd:COG1121 8 ELENLTVSYGGRPVLEdVS-LTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 QKLPASEG--LTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVM 159
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 160 ILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGkVLFSGGAELLHSEENLRTLFEAPV 239
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGPV 239
|
....*
gi 547260874 240 KLMLH 244
Cdd:COG1121 240 ALLAH 244
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-237 |
5.02e-60 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 195.06 E-value: 5.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEA 237
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDA 238
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
8.06e-55 |
|
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: 175.80 E-value: 8.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsERERAqRAAFLPQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERK-RIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEG--LTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKeGKVLFSG 220
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-235 |
9.31e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.47 E-value: 9.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMV-RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQRA- 77
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 -AFLPQKLPASEGLTCRELV---RLGRFP-WRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:COG3638 82 iGMIFQQFNLVPRLSVLTNVlagRLGRTStWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 153 AQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLhSEENLR 232
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVLR 240
|
...
gi 547260874 233 TLF 235
Cdd:COG3638 241 EIY 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-235 |
2.67e-48 |
|
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: 160.04 E-value: 2.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQRA--AFLPQKLPASE 88
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLRRqiGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRELVRLGRFP----WRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEP 164
Cdd:cd03256 92 RLSVLENVLSGRLGrrstWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 165 TSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLhSEENLRTLF 235
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDEIY 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-232 |
4.80e-46 |
|
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: 154.03 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQklpaseglt 91
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 crelvrlgrFPWRGLF---------------GRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQAS 156
Cdd:COG1122 83 ---------NPDDQLFaptveedvafgpenlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 157 PVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHSEENLR 232
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTpREVFSDYELLE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-215 |
3.29e-45 |
|
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: 151.08 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDisLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKlPASE--GLTCRELVRLGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:cd03225 81 FQN-PDDQffGPTVEEEVAFGL----ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-211 |
2.16e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 145.84 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTkleggdlftlsERERAQRAAFLPQK--LPASEGLTCRELVRLG 99
Cdd:NF040873 13 LTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRseVPDSLPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 RFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLAL 179
Cdd:NF040873 82 RWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIAL 161
|
170 180 190
....*....|....*....|....*....|..
gi 547260874 180 LERLnRETGRGVIAIIHDINLALRfATHIVAL 211
Cdd:NF040873 162 LAEE-HARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-250 |
6.48e-43 |
|
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: 152.75 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 7 IRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDA---GTTKLEGGDLFTLSERERAQRAAFLPQK 83
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 -----LPASEGLTCRELVRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:COG1123 92 pmtqlNPVTVGDQIAEALENLGLS--------RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAP 238
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE---------EILAAP 234
|
250
....*....|..
gi 547260874 239 VKLMLHPDPPAA 250
Cdd:COG1123 235 QALAAVPRLGAA 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
8.02e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.57 E-value: 8.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMV----RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQ- 75
Cdd:COG1136 4 LLELRNLTKSygtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 76 RAA---FLPQK---LPaseGLTCRELVRLgrfPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWIS 149
Cdd:COG1136 84 RRRhigFVFQFfnlLP---ELTALENVAL---PLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 150 MLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLAlRFATHIVALKEGKV 216
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-228 |
5.80e-42 |
|
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: 143.98 E-value: 5.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQ---RAAFLPQKLPASE 88
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRIGMIFQHYNLIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRELV---RLGRFP-WRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQaSPVMIL-DE 163
Cdd:TIGR02315 93 RLTVLENVlhgRLGYKPtWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ-QPDLILaDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 164 PTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSE 228
Cdd:TIGR02315 172 PIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-227 |
8.31e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.28 E-value: 8.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaQRAAFLPQ 82
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEGLTCRELVRLgrfpWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILD 162
Cdd:COG1131 81 EPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 163 EPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHS 227
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTpDELKAR 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-223 |
1.31e-41 |
|
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: 149.28 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSE---RERAQRAAFLPQKlPAS---EGLTCREL 95
Cdd:COG1123 286 LTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQD-PYSslnPRMTVGDI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRlgrFPWRGLFGRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQY 174
Cdd:COG1123 365 IA---EPLRLHGLLSRAERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQA 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 547260874 175 GTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:COG1123 442 QILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-235 |
6.16e-40 |
|
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: 138.45 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFtlSERERAQRA-AF 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KEPREARRQiGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGLTCRELVR-LGRfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRyFAE-----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELL---HSEENLRTLF 235
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELreeIGEENLEDAF 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-216 |
1.91e-39 |
|
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: 136.47 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMV----RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE----RA 74
Cdd:cd03255 2 ELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 75 QRAAFLPQK---LPaseGLTCRELVRLGRFpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISML 151
Cdd:cd03255 82 RHIGFVFQSfnlLP---DLTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 152 LAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLAlRFATHIVALKEGKV 216
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-208 |
2.35e-38 |
|
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: 133.37 E-value: 2.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRAAFL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLgrfpWRGLFGrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 161 LDEPTSALDVRhqyGTLALLERLNRETGRGVIAII--HDiNLALRFATHI 208
Cdd:COG4133 155 LDEPFTALDAA---GVALLAELIAAHLARGGAVLLttHQ-PLELAAARVL 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-241 |
4.98e-38 |
|
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: 133.67 E-value: 4.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTT------KLEGGDLFTLsereRaQR 76
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWEL----R-KR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 ----AAFLPQKLPASEglTCRELVRLGRFpwrGLFGRWR---AEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVwis 149
Cdd:COG1119 80 iglvSPALQLRFPRDE--TVLDVVLSGFF---DSIGLYReptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 150 mLLAQA----SPVMILDEPTSALDV--RHQYgtLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:COG1119 152 -LIARAlvkdPELLILDEPTAGLDLgaRELL--LALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
250
....*....|....*...
gi 547260874 224 LLHSEENLRTLFEAPVKL 241
Cdd:COG1119 229 EVLTSENLSEAFGLPVEV 246
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-223 |
3.41e-37 |
|
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: 131.02 E-value: 3.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA---AF-LPQKLPaseGLTCRELVR 97
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGigrTFqIPRLFP---ELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRFPWRG---LFGRWRAEDEAA---VDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03219 98 VAAQARTGsglLLARARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 547260874 172 HQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:cd03219 178 ETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-237 |
1.98e-36 |
|
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: 129.54 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGI----RMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQR 76
Cdd:COG1124 1 MLEVRNLsvsyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFLPQKLPAS--EGLTCRELVRLgrfPWRGLFgrwRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLA 153
Cdd:COG1124 81 VQMVFQDPYASlhPRHTVDRILAE---PLRIHG---LPDREERIAELLEQVGlPPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 154 QASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHS---EEN 230
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAgpkHPY 234
|
....*..
gi 547260874 231 LRTLFEA 237
Cdd:COG1124 235 TRELLAA 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-216 |
1.27e-35 |
|
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: 126.85 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA---AFLPQKLPAS--EGLTCRELV 96
Cdd:cd03257 26 FSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRkeiQMVFQDPMSSlnPRMTIGEQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RlgrFPWRGLFGRWRAED-EAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQY 174
Cdd:cd03257 106 A---EPLRIHGKLSKKEArKEAVLLLLVGVGlPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 547260874 175 GTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03257 183 QILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-241 |
1.54e-35 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 127.26 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVkPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELVRLGRFPwrglf 107
Cdd:COG4138 23 ELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQPA----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 108 GRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV-------MILDEPTSALDVRHQYGTLALL 180
Cdd:COG4138 97 GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTinpegqlLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 181 ERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVKL 241
Cdd:COG4138 177 REL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRR 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
3.29e-35 |
|
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: 123.51 E-value: 3.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 klpasegltcrelvrlgrfpwrglfgrwraedeaavdealaatgtahyaqsyvddLSGGERQRVWISMLLAQASPVMILD 162
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 547260874 163 EPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-217 |
7.31e-35 |
|
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: 124.55 E-value: 7.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRA 77
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNigmvfQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQklpasegLTCRELVRlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASP 157
Cdd:cd03259 82 ALFPH-------LTVAENIA---FGLK-LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 158 VMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVL 217
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-230 |
8.86e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.87 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRmVRNDRTILSIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:COG3840 1 MLRLDDLT-YRYGDFPLRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASegLTCRELVRLGRFPwrGLfgRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:COG3840 79 ENNLFPH--LTVAQNIGLGLRP--GL--KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 161 LDEPTSALD--VRHQygTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEEN 230
Cdd:COG3840 153 LDEPFSALDpaLRQE--MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-249 |
2.97e-34 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 124.55 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISG-LVKPDA-------GTTKLEGGDLFTLSERE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 73 RAQRAAFLPQKLPASEGLTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 153 AQASP---------VMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:PRK13547 161 AQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....*...
gi 547260874 224 LLHSEENLRTLFEAPVKLMLHPD--PPA 249
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDgvPPV 268
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-230 |
4.31e-34 |
|
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: 123.00 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERER---AQRAA 78
Cdd:cd03261 2 ELRGLTKSFGGRTVLKgVD-LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FLPQKLPASEGLTCRELVrlgRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENV---AFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEEN 230
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-234 |
1.11e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.92 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdLFTLSE---RERAQRAAFLPQKlPASE--GLTCRELV 96
Cdd:TIGR04520 23 LSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEenlWEIRKKVGMVFQN-PDNQfvGATVEDDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLG----RFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:TIGR04520 100 AFGlenlGVP--------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 173 QYGTLALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGG-AELLHSEENLRTL 234
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTpREIFSQVELLKEI 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-228 |
6.67e-33 |
|
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: 120.08 E-value: 6.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA---QRAA 78
Cdd:COG1127 7 EVRNLTKSFGDRVVLDgVS-LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FLPQklpasEG-----LTCRE-----LVRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWI 148
Cdd:COG1127 86 MLFQ-----GGalfdsLTVFEnvafpLREHTDLS--------EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 149 SMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHS 227
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTpEELLAS 232
|
.
gi 547260874 228 E 228
Cdd:COG1127 233 D 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
1.87e-32 |
|
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: 118.84 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMV----RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQ 75
Cdd:cd03258 1 MIELKNVSKVfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 76 RA--AFLPQKLPASEGLTCRELVRLgrfPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLA 153
Cdd:cd03258 81 RRriGMIFQHFNLLSSRTVFENVAL---PLE-IAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 154 QASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-214 |
7.31e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.88 E-value: 7.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMV----RNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlseRERAQRA 77
Cdd:COG1116 9 ELRGVSKRfptgGGGVTALDdVS-LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQK---LPAsegLTCRELVRLGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQ 154
Cdd:COG1116 83 GVVFQEpalLPW---LTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 155 ASPVMILDEPTSALDV--RHQygtL-ALLERLNRETGRGVIAIIHDINLALRFATHIVALKEG 214
Cdd:COG1116 156 DPEVLLMDEPFGALDAltRER---LqDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-220 |
1.19e-31 |
|
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: 116.05 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASegLTCRELVRLGRF 101
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAH--LTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PwrGLfgRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLE 181
Cdd:cd03298 97 P--GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 182 RLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-216 |
2.32e-31 |
|
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: 114.03 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaQRAAFLP 81
Cdd:cd03230 2 EVRNLSKRYGKKTALDdIS-LTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 QKLPASEGLTCRELVRlgrfpwrglfgrwraedeaavdealaatgtahyaqsyvddLSGGERQRVWISMLLAQASPVMIL 161
Cdd:cd03230 80 EEPSLYENLTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
2.89e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.91 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQ 82
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KlPASEGLTCRELVRlgrFPWRGlfgRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:COG4619 82 E-PALWGGTVRDNLP---FPFQL---RERKFDRERALELLERLGlPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-166 |
5.04e-31 |
|
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: 112.74 E-value: 5.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 97 RLGRFpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDD----LSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:pfam00005 81 RLGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-223 |
8.98e-31 |
|
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: 115.43 E-value: 8.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE----RAQRAAFLPQKLPASEGLTCRELVR 97
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQSFALLPHRTVLENVA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VRHQYG 175
Cdd:cd03294 125 FGL----EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRREMQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547260874 176 TLALleRLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:cd03294 201 DELL--RLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-220 |
1.67e-30 |
|
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: 113.37 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHL--EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftLSERERA-QRAAF 79
Cdd:cd03263 2 QIRNLTKTYKKGTKPAVDDLslNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAArQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGLTCRELVRL-GRFpwRGLFgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyARL--KGLP---KSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRetGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-228 |
2.05e-30 |
|
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: 119.09 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQK--LPASeglTCRELVRLG 99
Cdd:COG4988 358 LTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNpyLFAG---TIRENLRLG 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 RfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDD-----------LSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:COG4988 435 R----------PDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 169 DVRHQYGTLALLERLNRetGRGVIAIIHDINLaLRFATHIVALKEGKVLFSGG-AELLHSE 228
Cdd:COG4988 505 DAETEAEILQALRRLAK--GRTVILITHRLAL-LAQADRILVLDDGRIVEQGThEELLAKN 562
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-211 |
5.24e-30 |
|
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: 112.18 E-value: 5.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlseRERAQRAAFLPQKlpasEGLtcrelvrlgrF 101
Cdd:cd03293 25 LSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQ----DAL----------L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWR--------GLFGRW--RAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDV- 170
Cdd:cd03293 86 PWLtvldnvalGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAl 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 547260874 171 -RHQYGTlaLLERLNRETGRGVIAIIHDINLALRFATHIVAL 211
Cdd:cd03293 166 tREQLQE--ELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-238 |
1.02e-29 |
|
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: 114.44 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFT------LSERERA-----QRAAFLPQklpasegL 90
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRigyvfQEARLFPH-------L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRlgrfpwrglFGRWRA---EDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSA 167
Cdd:TIGR02142 91 SVRGNLR---------YGMKRArpsERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 168 LDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAP 238
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARED 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-215 |
3.73e-29 |
|
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: 108.43 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA--AFL 80
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRriGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLGrfpwrglfgrwraedeaavdealaatgtahyaqsyvddLSGGERQRVWISMLLAQASPVMI 160
Cdd:cd03229 82 FQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-228 |
5.07e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDA---------GTTKLEGGDLFTLSERERAQrAAFLPQKLPASEGLTC 92
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRAN-TGYIFQQFNLVNRLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELV---RLGRFP-WRGLFgRW--RAEDEAAVdEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:PRK09984 104 LENVligALGSTPfWRTCF-SWftREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 167 ALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSE 228
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-216 |
7.70e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 7.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFT-LSERERaqRAAFLPQKlPA-----------SEG 89
Cdd:COG1118 23 LEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRER--RVGFVFQH-YAlfphmtvaeniAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 90 LTCRelvrlgrfpwrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:COG1118 100 LRVR--------------PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 170 --VRHQygtL-ALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:COG1118 166 akVRKE---LrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-220 |
8.22e-28 |
|
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: 106.23 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDhLEIPThELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFT------LSERERA-----QRAAFLPQkLP 85
Cdd:cd03297 15 LKID-FDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKiglvfQQYALFPH-LN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 86 ASEGLTCrelvrlgrfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPT 165
Cdd:cd03297 92 VRENLAF------------GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 166 SALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-239 |
1.51e-27 |
|
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: 108.65 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTlsererAQRAAFLPqklpasegltcRELVRLG-- 99
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD------SARGIFLP-----------PHRRRIGyv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 ----R-FPW---RG--LFGRWRA---EDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAqASPVMIL-DEPT 165
Cdd:COG4148 83 fqeaRlFPHlsvRGnlLYGRKRApraERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALL-SSPRLLLmDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 166 SALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHS--------EENLRTLFE 236
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPlAEVLSRpdllplagGEEAGSVLE 241
|
...
gi 547260874 237 APV 239
Cdd:COG4148 242 ATV 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-216 |
2.73e-27 |
|
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: 104.65 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlSERERAQRAAFLPQKlPASE--GLT 91
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD-VDYQlfTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRLGRfpwrglfgRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03226 89 VREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 172 HQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-211 |
4.13e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLeGGDLFTLSERERA---QRAAFLPQklpasegLTCRELVRL 98
Cdd:COG4525 28 LTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-DGVPVTGPGADRGvvfQKDALLPW-------LNVLDNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 G-RfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VRHQYG 175
Cdd:COG4525 100 GlR-----LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDalTREQMQ 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 176 TLALleRLNRETGRGVIAIIHDINLALRFATHIVAL 211
Cdd:COG4525 175 ELLL--DVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
5.21e-27 |
|
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: 103.99 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGI--RMVRNDRTILSIDHLE--IPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTlSERERAQR 76
Cdd:cd03266 1 MITADALtkRFRDVKKTVQAVDGVSftVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFLPQKLPASEGLTCRELVRLgrfpWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQAS 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEY----FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 157 PVMILDEPTSALDVrhqYGTLALLE--RLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03266 156 PVLLLDEPTTGLDV---MATRALREfiRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-216 |
7.54e-27 |
|
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: 104.30 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELVRLgrF 101
Cdd:cd03295 22 LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEENIAL--V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PwrGLFGRWRAEDEAAVDEALAATG--TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VRHQYGTl 177
Cdd:cd03295 100 P--KLLKWPKEKIRERADELLALVGldPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpiTRDQLQE- 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 178 aLLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03295 177 -EFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-216 |
1.80e-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: 103.18 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaqRAAFLPQKLPASEGLTCRELV 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:cd03299 93 AYGL----KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 547260874 177 LALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-216 |
3.10e-26 |
|
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: 102.80 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaqRAAFLPQKLPASEGLTCRELVRLGRF 101
Cdd:cd03296 23 LDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFVFQHYALFRHMTVFDNVAFGLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLE 181
Cdd:cd03296 101 VKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLR 180
|
170 180 190
....*....|....*....|....*....|....*
gi 547260874 182 RLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03296 181 RLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-220 |
3.84e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.17 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlFTLSER---ERAQRAAFLPQKlPASE--GLTCRELVRLGrfpwrgL 106
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvwDVRRQVGMVFQN-PDNQfvGATVQDDVAFG------L 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 --FGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLN 184
Cdd:PRK13635 108 enIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLK 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 185 RETGRGVIAIIHDINLALRfATHIVALKEGKVLFSG 220
Cdd:PRK13635 188 EQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-220 |
4.39e-26 |
|
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: 101.50 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRAAFLPQKLPASEGLTCRELV----RLGRFPWRglf 107
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNFTVREFLdyiaWLKGIPSK--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 108 grwraEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNreT 187
Cdd:cd03264 106 -----EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--E 178
|
170 180 190
....*....|....*....|....*....|...
gi 547260874 188 GRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03264 179 DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-215 |
6.55e-26 |
|
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: 99.76 E-value: 6.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlpaseglt 91
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQD-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 crelvrlgrfPWrgLFgrwraedeaavdealaaTGTahyaqsyVDD--LSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:cd03228 85 ----------PF--LF-----------------SGT-------IREniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 547260874 170 VRHQYGTLALLERLNRetGRGVIAIIHDINLaLRFATHIVALKEGK 215
Cdd:cd03228 129 PETEALILEALRALAK--GKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-217 |
7.90e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.72 E-value: 7.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSEREraqRAAFL 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELVRLgrfpWRGLFGRwraeDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEF----WAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 161 LDEPTSALDVRHQygtlALLERLNRE-TGRGVIAIIhdinlalrfATHI-VALKEGKVL 217
Cdd:PRK13539 151 LDEPTAALDAAAV----ALFAELIRAhLAQGGIVIA---------ATHIpLGLPGAREL 196
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-216 |
8.70e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.07 E-value: 8.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 2 YELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSereRAQRAAFL- 80
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN---RAQRKAFRr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 --------------PQKlpaseglTCRELVRLgrfPWRGLFGRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQR 145
Cdd:PRK10419 90 diqmvfqdsisavnPRK-------TVREIIRE---PLRHLLSLDKAERLARASEMLRAVDlDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 146 VWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-252 |
1.07e-25 |
|
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: 102.82 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHElTL-ILGHNGSGKSTLASIISGLVKPDAGTT---KLEGGDLFTLSERE----RAQRAAFLPQklpasEGLTC- 92
Cdd:COG0444 26 FDVRRGE-TLgLVGESGSGKSTLARAILGLLPPPGITSgeiLFDGEDLLKLSEKElrkiRGREIQMIFQ-----DPMTSl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 ----------RELVRLGRfpwrglfGRWRAEDEAAVDEALAATG---TAHYAQSYVDDLSGGERQRVWISMLLAqASP-V 158
Cdd:COG0444 100 npvmtvgdqiAEPLRIHG-------GLSKAEARERAIELLERVGlpdPERRLDRYPHELSGGMRQRVMIARALA-LEPkL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAP 238
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE---------ELFENP 242
|
250
....*....|....
gi 547260874 239 vklmLHPdppaaYT 252
Cdd:COG0444 243 ----RHP-----YT 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-216 |
1.19e-25 |
|
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: 100.97 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 15 TIL-SIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSEReraQRAAFLPQK---------- 83
Cdd:COG4181 26 TILkGIS-LEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED---ARARLRARHvgfvfqsfql 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 LPAsegLTCRELVRLgrfPWRgLFGRWRAEDEAAvdEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDE 163
Cdd:COG4181 102 LPT---LTALENVML---PLE-LAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 547260874 164 PTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKV 216
Cdd:COG4181 173 PTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-217 |
2.16e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.48 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERER-----AQR 76
Cdd:COG3842 7 ELENVSKRYGDVTALDdVS-LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRnvgmvFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFLPQklpasegLTCRELV----RLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:COG3842 86 YALFPH-------LTVAENVafglRMRGVP--------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 153 AQASPVMILDEPTSALDVRHQYGTLALLERLNRETGrgvIAII---HDINLALRFATHIVALKEGKVL 217
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELG---ITFIyvtHDQEEALALADRIAVMNDGRIE 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-220 |
2.83e-25 |
|
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: 99.65 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 8 RMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVkPDAGTTklEGGDLFTLSERERAQ---RAAFLPQKL 84
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTT--SGQILFNGQPRKPDQfqkCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 PASEGLTCRELV------RLGRFpwrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:cd03234 91 ILLPGLTVRETLtytailRLPRK------SSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIH----DInlaLRFATHIVALKEGKVLFSG 220
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-235 |
3.65e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 100.73 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlFTLSERERAQRAAFLPQ--KLPASE 88
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG---QPTRQALQKNLVAYVPQseEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRELVRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 169 DVRHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKeGKVLFSGGAELLHSEENLRTLF 235
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-232 |
8.43e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASE--GLTCRELVRLG 99
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN-PDNQfiGATVEDDIAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 ----RFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYG 175
Cdd:PRK13632 109 lenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 176 TLALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGG-AELLHSEENLR 232
Cdd:PRK13632 181 IKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKpKEILNNKEILE 237
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-201 |
2.03e-24 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 96.92 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE----RAQRAAFLPQKLPAS 87
Cdd:TIGR03608 9 GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfRREKLGYLFQNFALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 88 EGLTCRELVRLGrfpwrgLFG--RWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPT 165
Cdd:TIGR03608 89 ENETVEENLDLG------LKYkkLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 166 SALDVRHQYGTLALLERLNREtGRGVIAIIHDINLA 201
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVA 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-216 |
2.42e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.05 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAqraaFLPQK------ 83
Cdd:COG2884 12 PGGREALSdVS-LEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIP----YLRRRigvvfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 ----LPaseGLTCRELVRlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWIsmllAQA---S 156
Cdd:COG2884 87 dfrlLP---DRTVYENVA---LPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI----ARAlvnR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 157 PVMIL-DEPTSALDVRHQYGTLALLERLNRetgRGVIAII--HDINLALRFATHIVALKEGKV 216
Cdd:COG2884 156 PELLLaDEPTGNLDPETSWEIMELLEEINR---RGTTVLIatHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-220 |
2.58e-24 |
|
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: 97.31 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRAAFLPQklpasegLTCRELV 96
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPvntvfQNYALFPH-------LTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:cd03300 94 A---FGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 177 LALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03300 170 QLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-231 |
3.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 24 IPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSER---ERAQRAAFLPQKlPASE--GLTCRELVRL 98
Cdd:PRK13640 30 IPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwDIREKVGIVFQN-PDNQfvGATVGDDVAF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GrfpwrgLFGRW--RAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:PRK13640 109 G------LENRAvpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 177 LALLERLNRETGRGVIAIIHDINLAlRFATHIVALKEGKVLFSGGAELLHSEENL 231
Cdd:PRK13640 183 LKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
22-229 |
5.23e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASE--GLTCRELVRLG 99
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD-PDDQvfSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 rfPWRglFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLAL 179
Cdd:PRK13647 105 --PVN--MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 180 LERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEE 229
Cdd:PRK13647 181 LDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-217 |
5.94e-24 |
|
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: 97.18 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 2 YELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTL--SERERAQR--- 76
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQRRAFRRdvq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 -------AAFLPQKlpaseglTCRELVRLgrfPWRGLFGRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWI 148
Cdd:TIGR02769 92 lvfqdspSAVNPRM-------TVRQIIGE---PLRHLTSLDESEQKARIAELLDMVGlRSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 149 SMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVL 217
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-225 |
7.31e-24 |
|
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: 95.96 E-value: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKLPASEGLTCRELVRLGR 100
Cdd:cd03224 21 LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGiGYVPEGRRIFPELTVEENLLLGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPwrglfgRWRAEDEAAVDEALA-----------ATGTahyaqsyvddLSGGERQRVWISMLLAQASPVMILDEPTSAL- 168
Cdd:cd03224 101 YA------RRRAKRKARLERVYElfprlkerrkqLAGT----------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLa 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 169 -DVRHQygTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELL 225
Cdd:cd03224 165 pKIVEE--IFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-216 |
8.32e-24 |
|
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: 95.70 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASegLTCRELVRLGRF 101
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAH--LTVRQNIGLGLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PwrGLfgRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLE 181
Cdd:TIGR01277 97 P--GL--KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 547260874 182 RLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-216 |
1.01e-23 |
|
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: 95.40 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRA 77
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDiamvfQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQKlpaseglTCRELVRlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASP 157
Cdd:cd03301 82 ALYPHM-------TVYDNIA---FGLK-LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 158 VMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-220 |
3.03e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQR---------AAFLPQKlpaseglT 91
Cdd:COG1135 26 LTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAARrkigmifqhFNLLSSR-------T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAqASP-VMILDEPTSALD- 169
Cdd:COG1135 99 VAENVA---LPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA-NNPkVLLCDEATSALDp 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 170 -----VrhqygtLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:COG1135 174 ettrsI------LDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-214 |
3.73e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsERERAQRAAFLPQklpasEGLtcrelvrlgrF 101
Cdd:PRK11248 22 LTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVVFQN-----EGL----------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRG----------LFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDV- 170
Cdd:PRK11248 83 PWRNvqdnvafglqLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAf 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 171 -RHQYGTLALleRLNRETGRGVIAIIHDINLALRFATHIVALKEG 214
Cdd:PRK11248 163 tREQMQTLLL--KLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-236 |
3.91e-23 |
|
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: 98.30 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlT 91
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRLGRfPwrglfgrwRAEDEAAVdEALAATGTAHYAQSYVDDL-----------SGGERQRVWISMLLAQASPVMI 160
Cdd:COG4987 425 LRENLRLAR-P--------DATDEELW-AALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 161 LDEPTSALDVRhqygT-LALLERLNRET-GRGVIAIIHDInLALRFATHIVALKEGKVLFSGG-AELLHSEENLRTLFE 236
Cdd:COG4987 495 LDEPTEGLDAA----TeQALLADLLEALaGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGThEELLAQNGRYRQLYQ 568
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-214 |
1.19e-22 |
|
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: 92.91 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERA---QRAAFLPQklpasegLTCRELVRL 98
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRMvvfQNYSLLPW-------LTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GRFpwRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLA 178
Cdd:TIGR01184 78 AVD--RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 179 LLERLNRETGRGVIAIIHDINLALRFATHIVALKEG 214
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-211 |
3.01e-22 |
|
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: 95.43 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlTCRELVRLGRf 101
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-TIAENIRLAR- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 pwrglfgrwRAEDEAAVDEALAATGTAHYAQSY-------VDD----LSGGERQRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:TIGR02857 421 ---------PDASDAEIREALERAGLDEFVAALpqgldtpIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 547260874 171 RHQYGTLALLERLNRetGRGVIAIIHDINLALRfATHIVAL 211
Cdd:TIGR02857 492 ETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-240 |
3.04e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 92.30 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVkPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELVRLGRFPwrglf 107
Cdd:PRK03695 23 EILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQPD----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 108 GRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASP-------VMILDEPTSALDVRHQygtlALL 180
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDVAQQ----AAL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 181 ERLNRE---TGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVK 240
Cdd:PRK03695 173 DRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-235 |
3.89e-22 |
|
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: 91.45 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlSERERAQRAAFLPQK------LPASegltCREL 95
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdFPIS----VAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRLGRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYG 175
Cdd:TIGR03771 72 VMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 176 TLALLERLNREtGRGVIAIIHDINLALRfATHIVALKEGKVLFSGGAELLHSEENLRTLF 235
Cdd:TIGR03771 152 LTELFIELAGA-GTAILMTTHDLAQAMA-TCDRVVLLNGRVIADGTPQQLQDPAPWMTTF 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-199 |
4.10e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.31 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQ 82
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KlPASEGLTCRE-LVrlgrFPWRglfGRWRAEDEAAVDEALAATGTA-HYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK10247 89 T-PTLFGDTVYDnLI----FPWQ---IRNQQPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDIN 199
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-216 |
4.24e-22 |
|
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: 89.41 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERErAQRA--AFLPQklpasegltcrelvrlg 99
Cdd:cd03216 21 LSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAgiAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 rfpwrglfgrwraedeaavdealaatgtahyaqsyvddLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLAL 179
Cdd:cd03216 83 --------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 547260874 180 LERLnRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03216 125 IRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-233 |
5.04e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.21 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTIL-SIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERE-RAQRaa 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLkGIS-LDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDiNKLR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 flpQKLpaseG-----------LTCRELVRLGrfPWRGLfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVW 147
Cdd:COG1126 77 ---RKV----GmvfqqfnlfphLTVLENVTLA--PIKVK-KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 148 ISMLLAQASPVMILDEPTSALD------VrhqygtLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSG- 220
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelvgeV------LDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGp 219
|
250
....*....|...
gi 547260874 221 GAELLHSEENLRT 233
Cdd:COG1126 220 PEEFFENPQHERT 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-216 |
5.16e-22 |
|
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: 90.67 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA--QRAAFLPQKLPASEGLTCRELVRLG 99
Cdd:cd03262 21 LTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQKVGMVFQQFNLFPHLTVLENITLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 rfPwRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD---VRhqyGT 176
Cdd:cd03262 101 --P-IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVG---EV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 547260874 177 LALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03262 175 LDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
22-232 |
6.83e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.92 E-value: 6.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLF--TLSERERAQRAAFLPQKLPASEGLTCRELVRLG 99
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHLTALENVMFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 RFPWRGLFgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VRHQygTL 177
Cdd:PRK09493 102 PLRVRGAS---KEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRHE--VL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 178 ALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHSEENLR 232
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDpQVLIKNPPSQR 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-236 |
1.14e-21 |
|
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: 94.13 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlT 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRLGRfpwrglfgrwRAEDEAAVDEALAATGTAHYAQS-------YVDD----LSGGERQRVWISMLLAQASPVMI 160
Cdd:COG2274 565 IRENITLGD----------PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 161 LDEPTSALDVRHQygtLALLERLNRET-GRGVIAIIHDINLaLRFATHIVALKEGKVLFSGG-AELLHSEENLRTLFE 236
Cdd:COG2274 635 LDEATSALDAETE---AIILENLRRLLkGRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGThEELLARKGLYAELVQ 708
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-217 |
1.15e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.44 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERER-----AQRA 77
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniamvFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQklpasegLTCRE-----LvRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:COG3839 85 ALYPH-------MTVYEniafpL-KLRKVP--------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 153 AQASPVMILDEPTSALDV--RHQygTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVL 217
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAklRVE--MRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-216 |
1.21e-21 |
|
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: 90.10 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA----QRAAFLPQ---KL 84
Cdd:TIGR02211 16 LDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQfhhLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 P---ASEGLTCRELVRlgrfpwrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:TIGR02211 96 PdftALENVAMPLLIG----------KKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVaLKEGKV 216
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLE-MKDGQL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-225 |
1.26e-21 |
|
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: 89.74 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRAAFLPQKLPASEGLTCRE-LVRLGR 100
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVFQDLSVDDELTGWEnLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 fpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALL 180
Cdd:cd03265 100 -----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 181 ERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELL 225
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-232 |
1.49e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 4 LNGIRMVRNDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlsereraQRAAFLPQ 82
Cdd:COG0488 1 LENLSKSFGGRPLLDdVS-LSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEGLTCRELVRLGRFPWRGLFGRWRA----------------------------EDEAAVDEALAATG-TAHYAQS 133
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGfPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 134 YVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTLALLER-LNRETGrGVIAIIHD---INlalRFATHIV 209
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE----SIEWLEEfLKNYPG-TVLVVSHDryfLD---RVATRIL 220
|
250 260
....*....|....*....|....*.
gi 547260874 210 ALKEGKV-LFSGG--AELLHSEENLR 232
Cdd:COG0488 221 ELDRGKLtLYPGNysAYLEQRAERLE 246
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-226 |
1.54e-21 |
|
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: 90.01 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGlvKPD----AGTTKLEGGDLFTLSERERAQRAAFL-PQKLPA 86
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLLELEPDERARAGLFLaFQYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 87 SEGLTCRELVRlgrfpwRGLFGRWRAEDEAAVD---------EALAATG-TAHYAQSYVDD-LSGGERQRVWIsMLLAQA 155
Cdd:TIGR01978 89 IPGVSNLEFLR------SALNARRSARGEEPLDlldfekllkEKLALLDmDEEFLNRSVNEgFSGGEKKRNEI-LQMALL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 156 SPVM-ILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLaLRFAT--HIVALKEGKVLFSGGAELLH 226
Cdd:TIGR01978 162 EPKLaILDEIDSGLDIDALKIVAEGINRL-REPDRSFLIITHYQRL-LNYIKpdYVHVLLDGRIVKSGDVELAK 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-216 |
2.35e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERErAQRA--AFLPQKLPASEGLTCRELVRLGRFPWRGLFGR 109
Cdd:COG1129 35 LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiAIIHQELNLVPNLSVAENIFLGREPRRGGLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 WRAEDEAAvDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL---DVRHqygTLALLERLnRE 186
Cdd:COG1129 114 WRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLterEVER---LFRIIRRL-KA 188
|
170 180 190
....*....|....*....|....*....|
gi 547260874 187 TGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:COG1129 189 QGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-203 |
3.43e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 23 EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA----QRAAFLPQKLPASEGLTCRELVRL 98
Cdd:PRK11629 31 SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFTALENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GRFpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLA 178
Cdd:PRK11629 111 PLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180
....*....|....*....|....*
gi 547260874 179 LLERLNRETGRGVIAIIHDINLALR 203
Cdd:PRK11629 187 LLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-226 |
3.93e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 3.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTIL-SIDhLEIPTHELTLILGHNGSGKSTLASIISGL--VKPDAGTTKLEGGDLFTLSERERAQRAAFL----PQKL 84
Cdd:COG0396 11 EGKEILkGVN-LTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLafqyPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 PaseGLTCRELVRLGRFPWRGLFGRwRAEDEAAVDEALAATG-TAHYAQSYVDD-LSGGERQRVWISMLLAQASPVMILD 162
Cdd:COG0396 90 P---GVSVSNFLRTALNARRGEELS-AREFLKLLKEKMKELGlDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 163 EPTSALDVRhqygtlAL------LERLnRETGRGVIAIIHDINLaLRF--ATHIVALKEGKVLFSGGAELLH 226
Cdd:COG0396 166 ETDSGLDID------ALrivaegVNKL-RSPDRGILIITHYQRI-LDYikPDFVHVLVDGRIVKSGGKELAL 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
4.65e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 4 LNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA--QRAAFLP 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLmfQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 -QKLPASEGLtcrelvrlgrfpwrGLFGRWRaedeAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK11247 95 wKKVIDNVGL--------------GLKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-220 |
4.84e-21 |
|
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: 88.04 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSE-RERA----QRAAFLPQklpas 87
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEaLRRIgaliEAPGFYPN----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 88 egLTCRELVRlgrfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSA 167
Cdd:cd03268 87 --LTARENLR--------LLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 168 LDvrhQYGTLALLE--RLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03268 157 LD---PDGIKELREliLSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-223 |
7.18e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 7.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 21 HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLeGGDLFTLSERERAQRAafLPQKLpaseGLtcrelvrLGR 100
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLKP--LRKKV----GI-------VFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPWRGLF---------------GRWRAEDEAAVDEALAATGTAHyaqSYVD----DLSGGERQRVWISMLLAQASPVMIL 161
Cdd:PRK13634 93 FPEHQLFeetvekdicfgpmnfGVSEEDAKQKAREMIELVGLPE---ELLArspfELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-237 |
8.02e-21 |
|
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: 89.86 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRAAFLPQklpasegLTCRELVRlgrFPWRgL 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHinmvfQSYALFPH-------MTVEENVA---FGLK-M 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 FGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRE 186
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 547260874 187 TGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENlrTLFEA 237
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA--NLFVA 198
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-220 |
1.13e-20 |
|
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: 87.62 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVK-----PDAGTTKLEGGDLFTLSER--ERAQ 75
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 76 RAAFLPQKlPASEGLTCRELVRLGrfPW-RGLfgRWRAEDEAAVDEAL--AATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:cd03260 82 RVGMVFQK-PNPFPGSIYDNVAYG--LRlHGI--KLKEELDERVEEALrkAALWDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 153 AQASPVMILDEPTSALDVRhqyGTLA---LLERLNRETgrGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPI---STAKieeLIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-251 |
1.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLegGD------LFTLSERERAQRAAFLPQKLPASEGL--TCR 93
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDyaipanLKKIKEVKRLRKEIGLVFQFPEYQLFqeTIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 94 ELVRLGRFPwrglFGRWRAEDEAAVDEALAATGTAH-YAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:PRK13645 110 KDIAFGPVN----LGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 173 QYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEApvklmlhpDPPAAY 251
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEI--------DPPKLY 256
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
13-220 |
1.56e-20 |
|
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: 90.55 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlTC 92
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELVRlgrfpwrglFGRWRAEDEAAVDEALAATgtahYAQSYVDD---------------LSGGERQRVWISMLLAQASP 157
Cdd:TIGR02203 423 ANNIA---------YGRTEQADRAEIERALAAA----YAQDFVDKlplgldtpigengvlLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 158 VMILDEPTSALDVRHQYGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVLFSG 220
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-238 |
1.65e-20 |
|
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: 90.51 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHElTL-ILGHNGSGKS-TLASIISGLVKPDA---GTTKLEGGDLFTLSERE----RAQRAAFLPQklpasEGLTC 92
Cdd:COG4172 31 FDIAAGE-TLaLVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLSERElrriRGNRIAMIFQ-----EPMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 -----------RELVRLGRfpwrglfGRWRAEDEAAVDEALAATGTAHYAQ---SYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:COG4172 105 lnplhtigkqiAEVLRLHR-------GLSGAAARARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAP 238
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA---------ELFAAP 248
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
12-267 |
2.14e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDlfTLSE------RERA--------- 74
Cdd:PRK13633 19 ESTEKLALDDvnLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEenlwdiRNKAgmvfqnpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 75 --------QRAAFLPQKLpaseGLTCRELvrlgrfpwrglfgRWRaedeaaVDEALAATGTAHYAQSYVDDLSGGERQRV 146
Cdd:PRK13633 97 qivativeEDVAFGPENL----GIPPEEI-------------RER------VDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 147 WISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGGAELLH 226
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 547260874 227 SEenlrtlfeapVKLMlhpdppaaytggkKQLPLDVAVVCE 267
Cdd:PRK13633 233 KE----------VEMM-------------KKIGLDVPQVTE 250
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-208 |
2.78e-20 |
|
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: 85.87 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 10 VRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSErERAQRAAFLPQkLPASEG 89
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGH-LPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 90 -LTCRELVRLgrfpWRGLFGrwraEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:TIGR01189 87 eLSALENLHF----WAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 547260874 169 DVRhqyGTLALLERLNRETGRGVIAIIhdinlalrfATHI 208
Cdd:TIGR01189 159 DKA---GVALLAGLLRAHLARGGIVLL---------TTHQ 186
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
28-220 |
4.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlsereraqraaflPQKLPASEGLTCRELVRL-GRFPWRGL 106
Cdd:PRK13639 29 EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-----------------PIKYDKKSLLEVRKTVGIvFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 FGRWRAED---------------EAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:PRK13639 92 FAPTVEEDvafgplnlglskeevEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 547260874 172 HQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
6.62e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTtkleggdlFTLSERER----AQRAA 78
Cdd:COG0488 317 ELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT--------VKLGETVKigyfDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FLPQKL-------PASEGLTCRELV-RLGRFpwrgLFgrwRAEDeaavdealaatgtahyAQSYVDDLSGGERQRVWISM 150
Cdd:COG0488 389 ELDPDKtvldelrDGAPGGTEQEVRgYLGRF----LF---SGDD----------------AFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 151 LLAQASPVMILDEPTSALDVRhqygTLALLER-LNRETGrGVIAIIHDINLALRFATHIVALKEGKV-LFSGG 221
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIE----TLEALEEaLDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVrEYPGG 513
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-220 |
1.11e-19 |
|
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: 88.53 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 18 SIDHLEIPTHE--LTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaQRAAFLPQKLPASEGLTCREL 95
Cdd:TIGR01257 945 AVDRLNITFYEnqITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRLgrfpWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYG 175
Cdd:TIGR01257 1024 ILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 176 TLALLerLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-220 |
1.20e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKLPASEGLTCRELVRLGR 100
Cdd:PRK09700 26 LTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGiGIIYQELSVIDELTVLENLYIGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPWRGLFG----RWRAEDEAAvDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:PRK09700 106 HLTKKVCGvniiDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 177 LALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK09700 185 FLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
22-215 |
1.39e-19 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 84.22 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSEReraqRAAFLPQK----------LPAsegLT 91
Cdd:TIGR02673 23 LHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGR----QLPLLRRRigvvfqdfrlLPD---RT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRLgrfPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:TIGR02673 96 VYENVAL---PLE-VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 172 HQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:TIGR02673 172 LSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-197 |
1.47e-19 |
|
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: 87.80 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASEGLTCRELVRLGRf 101
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQD-AHLFDTTVRENLRLAR- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 pwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDL-----------SGGERQRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:TIGR02868 434 ---------PDATDEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*...
gi 547260874 171 RhqyGTLALLERLNR-ETGRGVIAIIHD 197
Cdd:TIGR02868 505 E---TADELLEDLLAaLSGRTVVLITHH 529
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-220 |
1.53e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 84.98 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGG-----DLFTLSERERaqraaflpqklpasegltcRELVR-----LGRF 101
Cdd:PRK11701 37 IVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER-------------------RRLLRtewgfVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRGLfgRWRAEDEAAVDEALAATGTAHY----------------AQSYVDDL----SGGERQRVWISMLLAQASPVMIL 161
Cdd:PRK11701 98 PRDGL--RMQVSAGGNIGERLMAVGARHYgdiratagdwlerveiDAARIDDLpttfSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK11701 176 DEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-226 |
1.54e-19 |
|
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: 83.73 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGL--VKPDAGTTKLEGGDLFTLSERERAQRAAFL 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 -PQKLPASEGLTCRELVRlgrfpwrglfgrwraedeaavdealaatgtahyaqsYVDD-LSGGERQRVWISMLLAQASPV 158
Cdd:cd03217 82 aFQYPPEIPGVKNADFLR------------------------------------YVNEgFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHdinlALRFATHIVA-----LKEGKVLFSGGAELLH 226
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITH----YQRLLDYIKPdrvhvLYDGRIVKSGDKELAL 193
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-220 |
1.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.56 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLegGDLFTLS-----ERERAQRAAFLPQKLPASE 88
Cdd:PRK13643 20 RALFDID-LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV--GDIVVSStskqkEIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRELVRLGRFPWRglFGRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSA 167
Cdd:PRK13643 97 LFEETVLKDVAFGPQN--FGIPKEKAEKIAAEKLEMVGlADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 547260874 168 LDVRHQYGTLALLERLNrETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13643 175 LDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-220 |
1.89e-19 |
|
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: 83.87 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSEreraQRAAFLPQ 82
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR----NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEGLTCRE-LVRLGRfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:cd03269 78 ERGLYPKMKVIDqLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 162 DEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-242 |
2.17e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 21 HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASE--GLTCRELVRL 98
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQfvGRTVEEDLAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GR----FPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqy 174
Cdd:PRK13644 102 GPenlcLP--------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD--- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 175 GTLALLERLNR--ETGRGVIAIIHDINlALRFATHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVKLM 242
Cdd:PRK13644 171 SGIAVLERIKKlhEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLI 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-258 |
2.37e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.80 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 24 IPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASE--GLTCRELVRLG-- 99
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN-PDNQfvGSIVKYDVAFGle 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 --RFPWRGLFGRwraedeaaVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTL 177
Cdd:PRK13648 111 nhAVPYDEMHRR--------VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 178 ALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGGA-ELLHSEENLRTL---FEAPVK---LMLHPDPPAA 250
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPtEIFDHAEELTRIgldLPFPIKinqMLGHQTSFLT 261
|
....*...
gi 547260874 251 YTGGKKQL 258
Cdd:PRK13648 262 YEGLVDQL 269
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-235 |
2.64e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.24 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE----RAQRAAFLPQKLPASEGLTCRELVR 97
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTL 177
Cdd:PRK10070 129 FGM----ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 178 ALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGA-ELLHSEEN--LRTLF 235
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPdEILNNPANdyVRTFF 265
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
12-235 |
2.80e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 83.86 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKLPASEGL 90
Cdd:TIGR04406 12 KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGiGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRE-----LVRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDE-- 163
Cdd:TIGR04406 92 TVEEnimavLEIRKDLD--------RAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEpf 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 164 ----PTSALDVRHQYGTLallerlnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLF 235
Cdd:TIGR04406 164 agvdPIAVGDIKKIIKHL-------KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-225 |
3.02e-19 |
|
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: 83.81 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGl 90
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGRfpwrglfGRWRAEDEAAVDEALAAT--------GTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILD 162
Cdd:cd03254 92 TIMENIRLGR-------PNATDEEVIEAAKEAGAHdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 163 EPTSALDVRHQYGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVLFSGGAELL 225
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-218 |
3.26e-19 |
|
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: 86.53 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRtiLSIDHLE--IPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLegGDLFTLSERERaQRAAFL 80
Cdd:TIGR03719 324 EAENLTKAFGDK--LLIDDLSfkLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GETVKLAYVDQ-SRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKL---PASEGLtcrELVRLGRF--PWRGLFGRW--RAEDEaavdealaatgtahyaQSYVDDLSGGERQRVWISMLLA 153
Cdd:TIGR03719 399 PNKTvweEISGGL---DIIKLGKReiPSRAYVGRFnfKGSDQ----------------QKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 154 QASPVMILDEPTSALDVRhqygTLALLERLNRETGRGVIAIIHDINLALRFATHIVALK-EGKVLF 218
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE----TLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEW 521
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-237 |
3.34e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 86.76 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGl 90
Cdd:COG1132 351 GDRPVLKdIS-LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSG- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGRfpwrglfgrwRAEDEAAVDEALAATGtAH---------YaQSYVDD----LSGGERQRVWIS-MLLAQAs 156
Cdd:COG1132 429 TIRENIRYGR----------PDATDEEVEEAAKAAQ-AHefiealpdgY-DTVVGErgvnLSGGQRQRIAIArALLKDP- 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 157 PVMILDEPTSALDVRHQYgtlALLERLNRET-GRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELLHSEENLRTL 234
Cdd:COG1132 496 PILILDEATSALDTETEA---LIQEALERLMkGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGThEELLARGGLYARL 571
|
...
gi 547260874 235 FEA 237
Cdd:COG1132 572 YRL 574
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
12-232 |
6.31e-19 |
|
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: 82.98 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKLPASEGL 90
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGiGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGrfpwRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD- 169
Cdd:cd03218 91 TVEENILAV----LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 170 --VRHQYGTLALLerlnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLR 232
Cdd:cd03218 167 iaVQDIQKIIKIL----KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-220 |
9.40e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.13 E-value: 9.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERE----RAQRAAFLPQklpASE 88
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGllalRQQVATVFQD---PEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRELVRLGRFPWRGLfgrWRAEDEAA--VDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRNL---GVPEAEITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 547260874 167 ALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-246 |
1.11e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTlsererAQRAAFLPQklpasegltcrELV 96
Cdd:PRK11144 15 LTVN-LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD------AEKGICLPP-----------EKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLG------R-FPW---RG--LFGrWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEP 164
Cdd:PRK11144 77 RIGyvfqdaRlFPHykvRGnlRYG-MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 165 TSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE------LLH---SEENLRTLF 235
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEevwassAMRpwlPKEEQSSIL 235
|
250
....*....|.
gi 547260874 236 EAPVkLMLHPD 246
Cdd:PRK11144 236 KVTV-LEHHPH 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-216 |
1.17e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERErAQRA--AFLPQ--KLpaSEGLTCRELVRLGRFPWRGLF 107
Cdd:COG3845 36 LLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIALgiGMVHQhfML--VPNLTVAENIVLGLEPTKGGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 108 GRWRAEdEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL---DVRHQYGTLALLerln 184
Cdd:COG3845 113 LDRKAA-RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEILRRL---- 187
|
170 180 190
....*....|....*....|....*....|..
gi 547260874 185 RETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:COG3845 188 AAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
1.30e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.44 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMV-----RNDRTIL-SIDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA 74
Cdd:COG1101 1 MLELKNLSKTfnpgtVNEKRALdGLN-LTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 75 QRAAFLPQ--KLPASEGLTCRE--LVRLGRFPWRGLFGRWRAEDEAAVDEALAAT--GTAHYAQSYVDDLSGGERQRVwi 148
Cdd:COG1101 80 KYIGRVFQdpMMGTAPSMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQAL-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 149 SMLLAQASP--VMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLF 218
Cdd:COG1101 158 SLLMATLTKpkLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-216 |
1.35e-18 |
|
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: 81.69 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLsereRAQRAAFLPQKLpaseGLTCRELvRLgrF 101
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL----RGRAIPYLRRKI----GVVFQDF-RL--L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRGLF----------GRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03292 91 PDRNVYenvafalevtGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 172 HQYGTLALLERLNReTGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03292 171 TTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-202 |
1.36e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEI-PTHELTLiLGHNGSGKSTLASIISGLVKPDAGTTkleggdlftlsERERAQRAAF 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELkPGKILTL-LGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQK--LPASEGLTCRELVRLGRfpwrglfgrwrAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASP 157
Cdd:PRK09544 72 VPQKlyLDTTLPLTVNRFLRLRP-----------GTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 158 VMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLAL 202
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVM 185
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-220 |
1.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL----------------------FTLSERERAQRAAF 79
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvklsdirkkvglvfqypeYQLFEETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGltcrelvrlgrfpwrglfgrwraEDEAAVDEALAATGTAHyaQSYVD----DLSGGERQRVWISMLLAQA 155
Cdd:PRK13637 108 GPINLGLSEE-----------------------EIENRVKRAMNIVGLDY--EDYKDkspfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 156 SPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-220 |
2.34e-18 |
|
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: 81.10 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 2 YELNGIRMVRNDRTI--LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAF 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGlTCRELVRLGRfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVD-----------DLSGGERQRVWI 148
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA----------PLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 149 SMLLAQASPVMILDEPTSALDVRhqyGTLALLERLNRET-GRGVIAIIHDINLaLRFATHIVALKEGKVLFSG 220
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMN---SEERLKERLRQLLgDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-216 |
3.30e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRA 77
Cdd:PRK09452 16 ELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHvntvfQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQklpasegLTCRELV----RLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLA 153
Cdd:PRK09452 96 ALFPH-------MTVFENVafglRMQKTP--------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 154 QASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-198 |
6.27e-18 |
|
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: 82.91 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGttkleggdlftlsERERAQRAAFLPQKLPASEGLTCRELV 96
Cdd:COG1245 356 LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------------EVDEDLKISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 R---LGRFP--WrglfgrWRAEdeaaVDEALaatGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:COG1245 423 RsanTDDFGssY------YKTE----IIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180
....*....|....*....|....*..
gi 547260874 172 HQYGTLALLERLNRETGRGVIAIIHDI 198
Cdd:COG1245 490 QRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
7.76e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 7.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILsiDHL--EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsERERAQRAA 78
Cdd:COG4152 1 MLELKGLTKRFGDKTAV--DDVsfTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FLP------QKLPASEgltcrELVRLGRfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRV-WISML 151
Cdd:COG4152 75 YLPeerglyPKMKVGE-----QLVYLAR-----LKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIAAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 152 LAQasP-VMILDEPTSALD---VRhqygTL--ALLERlnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:COG4152 145 LHD--PeLLILDEPFSGLDpvnVE----LLkdVIREL--AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
30-252 |
9.61e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.32 E-value: 9.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 30 TL-ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQR-----------AAFLPQKlpaseglTCRELV 96
Cdd:COG4608 46 TLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElRPLRrrmqmvfqdpyASLNPRM-------TVGDII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RlgrFPWR--GLFGRwrAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ 173
Cdd:COG4608 119 A---EPLRihGLASK--AERRERVAELLELVGlRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 174 YGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAPvklmLHPdppaaYT 252
Cdd:COG4608 194 AQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRD---------ELYARP----LHP-----YT 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-238 |
1.00e-17 |
|
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: 82.42 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHElTL-ILGHNGSGKSTLASIISGLVkPDAGTTKLEGGDLFTLSERE-RAQR-----------AAFLPQklpase 88
Cdd:COG4172 307 LTLRRGE-TLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlRPLRrrmqvvfqdpfGSLSPR------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 gLTCRELVRLG---RFPwrglfGRWRAEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEP 164
Cdd:COG4172 379 -MTVGQIIAEGlrvHGP-----GLSAAERRARVAEALEEVGlDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 165 TSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAP 238
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE---------QVFDAP 517
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-196 |
1.11e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMV--RNDRTILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQ 75
Cdd:PRK11153 1 MIELKNISKVfpQGGRTIHALNNvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 76 RaaflpQK---------LPASEglTCRELVRlgrFPWRgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRV 146
Cdd:PRK11153 81 R-----RQigmifqhfnLLSSR--TVFDNVA---LPLE-LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 147 WISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIH 196
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-216 |
1.12e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaqRAAFLPQ 82
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEGLTCRELVRLGrfpWRGLFGRWR---AEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVM 159
Cdd:PRK10851 82 HYALFRHMTVFDNIAFG---LTVLPRRERpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 160 ILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-220 |
1.20e-17 |
|
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: 78.36 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKP--DAGTTKLEGgdlFTLSERERAQRAAFLPQKLPASEGLTCRElvrlgrfpwrg 105
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTLTVRE----------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 106 lfgrwraedeaAVDEALAATGtahyaqsyvddLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLnR 185
Cdd:cd03213 102 -----------TLMFAAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-A 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 186 ETGRGVIAIIHDI-NLALRFATHIVALKEGKVLFSG 220
Cdd:cd03213 159 DTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-232 |
1.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 21 HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTkLEGGDLFTLSereraqRAAFLpqKLPASEGLTCRElvrlgr 100
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYS------RKGLM--KLRESVGMVFQD------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 fPWRGLFGRWRAED---------------EAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPT 165
Cdd:PRK13636 91 -PDNQLFSASVYQDvsfgavnlklpedevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 166 SALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHSEENLR 232
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAEKEMLR 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-215 |
1.64e-17 |
|
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: 79.37 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsereraqraAFLPQKLPASEGLTCRELV 96
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RlGRFPWRGLFGRWRAE--DEAAVDEALaatgtahyaQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQY 174
Cdd:cd03237 83 S-SITKDFYTHPYFKTEiaKPLQIEQIL---------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 547260874 175 GTLALLERLNRETGRGVIAIIHDINLALRFATHIVALkEGK 215
Cdd:cd03237 153 MASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-220 |
1.97e-17 |
|
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: 81.71 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQK---------- 83
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEpyifsgsile 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 ---LPASEGLTCRELVRLGRFpwrglfgrwrAEDEAAVDEALAATGTAHYAQSYvdDLSGGERQRVWISMLLAQASPVMI 160
Cdd:TIGR01193 567 nllLGAKENVSQDEIWAACEI----------AEIKDDIENMPLGYQTELSEEGS--SISGGQKQRIALARALLTDSKVLI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETgrgVIAIIHDINLALRfATHIVALKEGKVLFSG 220
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-246 |
2.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASE--GLTCRELVRLGrFPWRGLFgr 109
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN-PDNQfvGATVEDDVAFG-LENKGIP-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 wRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGR 189
Cdd:PRK13650 114 -HEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQM 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 190 GVIAIIHDIN-LALrfATHIVALKEGKV--------LFSGGAELLhsEENLRTLFEAPVKLMLHPD 246
Cdd:PRK13650 193 TVISITHDLDeVAL--SDRVLVMKNGQVeststpreLFSRGNDLL--QLGLDIPFTTSLVQSLRQN 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
12-215 |
2.65e-17 |
|
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: 76.33 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLeggdlftlsereraqraaflpqklpaseglt 91
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 crelvrlgrfpwrglfgrwraedeaavdeaLAATGTAHYAQsyvddLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03221 60 ------------------------------GSTVKIGYFEQ-----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 172 hqygTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:cd03221 105 ----SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-225 |
5.08e-17 |
|
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: 77.66 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL--FTLSERERaqRAAFLPQKLPASEGlTCRELVRlg 99
Cdd:cd03251 23 LDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdYTLASLRR--QIGLVSQDVFLFND-TVAENIA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 rfpwrglFGRWRAEDEAAVDEALAAtgtahYAQSYVDD---------------LSGGERQRVWISMLLAQASPVMILDEP 164
Cdd:cd03251 98 -------YGRPGATREEVEEAARAA-----NAHEFIMElpegydtvigergvkLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 165 TSALDVRHQYGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELL 225
Cdd:cd03251 166 TSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGThEELL 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-238 |
7.44e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 7.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 6 GIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLA-SIISGLVKPDA----GTTKLEGGDLFTLSERE----RAQR 76
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPVvypsGDIRFHGESLLHASEQTlrgvRGNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFLPQKLPAS--------EGLTcrELVRLGRfpwrglfGRWRaedEAAVDEALAA---TGTAHYAQSYVD---DLSGGE 142
Cdd:PRK15134 94 IAMIFQEPMVSlnplhtleKQLY--EVLSLHR-------GMRR---EAARGEILNCldrVGIRQAAKRLTDyphQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 143 RQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLfsgga 222
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV----- 236
|
250
....*....|....*..
gi 547260874 223 ellhsEENL-RTLFEAP 238
Cdd:PRK15134 237 -----EQNRaATLFSAP 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
22-223 |
8.43e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQ----RAAFLPQKLPASEGLTCRELVR 97
Cdd:PRK10535 29 LDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYHLLSHLTAAQNVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRFpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTL 177
Cdd:PRK10535 109 VPAV----YAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 547260874 178 ALLERLnRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGGAE 223
Cdd:PRK10535 185 AILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-201 |
1.79e-16 |
|
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: 75.61 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFtlSERERAQRAAFLPQKLPASEG- 89
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD--FQRDSIARGLLYLGHAPGIKTt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 90 LTCRELVRLgrfpwrglfgrWRAE-DEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:cd03231 88 LSVLENLRF-----------WHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 169 DVRhqyGTLALLERLNRETGRGVIAII---HDINLA 201
Cdd:cd03231 157 DKA---GVARFAEAMAGHCARGGMVVLtthQDLGLS 189
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
28-216 |
1.85e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASEGLTCRELVrlgrfpwrgLF 107
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVRENI---------AY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 108 GRWRAEDE---AAVDEALAATGTAHYAQSYVDD-------LSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYgtl 177
Cdd:TIGR00958 578 GLTDTPDEeimAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ--- 654
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 178 aLLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKV 216
Cdd:TIGR00958 655 -LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-238 |
2.66e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRmVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPD----AGTTKLEGGDLFTLSERER----- 73
Cdd:PRK10418 6 ELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALRGRkiati 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 74 --AQRAAFLPQKLPASEGL-TCRELVRLGrfpwrglfgrwraeDEAAVDEALAATG---TAHYAQSYVDDLSGGERQRVW 147
Cdd:PRK10418 85 mqNPRSAFNPLHTMHTHAReTCLALGKPA--------------DDATLTAALEAVGlenAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 148 ISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhs 227
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVE---- 226
|
250
....*....|.
gi 547260874 228 eenlrTLFEAP 238
Cdd:PRK10418 227 -----TLFNAP 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
17-198 |
5.45e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.16 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEggdlftlsereraQRAAFLPQKLPASEGLTCRELV 96
Cdd:PRK13409 355 LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLGRFPWRGLFgrWRAEdeaaVDEALaatGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:PRK13409 422 RSITDDLGSSY--YKSE----IIKPL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180
....*....|....*....|..
gi 547260874 177 LALLERLNRETGRGVIAIIHDI 198
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDI 514
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-238 |
5.46e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLegGDLFTLSERERAQRAAfL 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARSLSQQKG-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRELvrlGRFPWRGLF-----------GRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWIS 149
Cdd:PRK11264 80 IRQLRQHVGFVFQNF---NLFPHRTVLeniiegpvivkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 150 MLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETgRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAellhsee 229
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPA------- 228
|
....*....
gi 547260874 230 nlRTLFEAP 238
Cdd:PRK11264 229 --KALFADP 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-225 |
5.76e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 74.62 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 21 HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASegLTCRELVRLGR 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSH--LTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPwrGLfgRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VRHQygTLA 178
Cdd:PRK10771 97 NP--GL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQE--MLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547260874 179 LLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELL 225
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPtDELL 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-232 |
6.04e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.41 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRAAFLPQklpasegLTCRELV 96
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPinmmfQSYALFPH-------MTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLG----RFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDV-- 170
Cdd:PRK11607 113 AFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKkl 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 171 --RHQYGTLALLERLnretGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLR 232
Cdd:PRK11607 185 rdRMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-216 |
6.40e-16 |
|
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: 77.10 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQK---LPASegltcrelVR--LGRFPwrgl 106
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDvelFDGT--------IAenIARFG---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 fgrwRAEDEAAVDEALAAtGtAH-----YAQSY---VDD----LSGGERQRVwismLLAQA---SPVMI-LDEPTSALDV 170
Cdd:COG4618 431 ----DADPEKVVAAAKLA-G-VHemilrLPDGYdtrIGEggarLSGGQRQRI----GLARAlygDPRLVvLDEPNSNLDD 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547260874 171 RhqyGTLALLERLN--RETGRGVIAIIHDINLaLRFATHIVALKEGKV 216
Cdd:COG4618 501 E---GEAALAAAIRalKARGATVVVITHRPSL-LAAVDKLLVLRDGRV 544
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
12-216 |
8.43e-16 |
|
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: 73.02 E-value: 8.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlpaseglt 91
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 crelvrlgrfpwrglfgrwraedeaavDEALAATgtahyaqsyVDD--LSGGERQRVwismLLAQA---SP-VMILDEPT 165
Cdd:cd03246 85 ---------------------------DELFSGS---------IAEniLSGGQRQRL----GLARAlygNPrILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 547260874 166 SALDVRHQYGTLALLERLnRETGRGVIAIIHDINLaLRFATHIVALKEGKV 216
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPET-LASADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-225 |
9.68e-16 |
|
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: 74.11 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASEGL 90
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGRFPwrglfgRWRAEDEAAVDEALAATGTAHYAQSY---VDD----LSGGERQRVWISMLLAQASPVMILDE 163
Cdd:cd03249 92 TIAENIRYGKPD------ATDEEVEEAAKKANIHDFIMSLPDGYdtlVGErgsqLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 164 PTSALDVRHQYGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELL 225
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGThDELM 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-220 |
1.36e-15 |
|
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: 73.91 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSID--HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQK----- 83
Cdd:cd03267 29 RKYREVEALKgiSFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKtqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 -LPASEGLtcRELVRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILD 162
Cdd:cd03267 109 dLPVIDSF--YLLAAIYDLP--------PARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 163 EPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-201 |
2.42e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsereRAQRAAFL 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 pqklpasegltcRELVRLGRF--------PWRGLfgRWRAE-----DEAAVDEALAATGTAHYAQSYVDDLSGGERQRVW 147
Cdd:PRK13538 74 ------------QDLLYLGHQpgikteltALENL--RFYQRlhgpgDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 148 ISMLLAQASPVMILDEPTSALDVRhqyGTLALLERLNRETGRGVIAII---HDINLA 201
Cdd:PRK13538 140 LARLWLTRAPLWILDEPFTAIDKQ---GVARLEALLAQHAEQGGMVILtthQDLPVA 193
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-220 |
2.74e-15 |
|
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: 71.96 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLsERERAQRAAFLPQKlPASEGLT 91
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISVLNQR-PYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRElvRLGRfpwrglfgrwraedeaavdealaatgtahyaqsyvdDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03247 91 LRN--NLGR------------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 547260874 172 HQYGTLALLERLNREtgRGVIAIIHDInLALRFATHIVALKEGKVLFSG 220
Cdd:cd03247 133 TERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-216 |
4.65e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSEREraqrAAFLPQKL----PASEGLTCRELVRLGRFPW 103
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE----VPFLRRQIgmifQDHHLLMDRTVYDNVAIPL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 104 rgLFGRWRAED-EAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLER 182
Cdd:PRK10908 105 --IIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE 182
|
170 180 190
....*....|....*....|....*....|....
gi 547260874 183 LNReTGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK10908 183 FNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-220 |
4.74e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFL-PQKLPASEGLTCRE--LVRLGRfpwrglfg 108
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLvPQEPLLFPNLSVKEniLFGLPK-------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 rwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDvrhQYGTLALLERLN--RE 186
Cdd:PRK15439 114 --RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT---PAETERLFSRIRelLA 188
|
170 180 190
....*....|....*....|....*....|....
gi 547260874 187 TGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK15439 189 QGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-231 |
5.90e-15 |
|
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: 72.13 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTL-SERERAQRAAFLPQKLpasegltcrelvrlgr 100
Cdd:cd03252 23 LRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQVGVVLQENV---------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 fpwrgLFGRWRAEDEAAVDEAL--------AATGTAH---------YAQSYVDD---LSGGERQRVWISMLLAQASPVMI 160
Cdd:cd03252 87 -----LFNRSIRDNIALADPGMsmervieaAKLAGAHdfiselpegYDTIVGEQgagLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNreTGRGVIAIIHDINlALRFATHIVALKEGKVLFSGGAELLHSEENL 231
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-218 |
6.14e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.00 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLegGDLFTLSERERaQRAAFLPQKL---PASEGLtcrELVRLGRF--PWRGL 106
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKI--GETVKLAYVDQ-SRDALDPNKTvweEISGGL---DIIKVGNReiPSRAY 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 FGRW--RAEDEaavdealaatgtahyaQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTL-ALLERL 183
Cdd:PRK11819 429 VGRFnfKGGDQ----------------QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE----TLrALEEAL 488
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 184 NRETGRGVIaIIHDINLALRFATHIVALK-EGKVLF 218
Cdd:PRK11819 489 LEFPGCAVV-ISHDRWFLDRIATHILAFEgDSQVEW 523
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-196 |
6.24e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRA--AFLPQKLPASEGLTCRELVRLGRFPwRGLFGR 109
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSSQEAgiGIIHQELNLIPQLTIAENIFLGREF-VNRFGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 --WRAEDEAAvDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL-DVRhqygTLALLERLN-- 184
Cdd:PRK10762 113 idWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE----TESLFRVIRel 187
|
170
....*....|..
gi 547260874 185 RETGRGVIAIIH 196
Cdd:PRK10762 188 KSQGRGIVYISH 199
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-225 |
7.37e-15 |
|
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: 71.88 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPasegL-- 90
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV----Lfn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 -TCRELVRlgrfpwrglFGRWRAEDEAAVDEALAATgtahyaqsyVDD-------------------LSGGERQRVWISM 150
Cdd:cd03253 89 dTIGYNIR---------YGRPDATDEEVIEAAKAAQ---------IHDkimrfpdgydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 151 LLAQASPVMILDEPTSALDV---RHQYGTLALLerlnrETGRGVIAIIHdinlalRFAT-----HIVALKEGKVLFSGG- 221
Cdd:cd03253 151 AILKNPPILLLDEATSALDThteREIQAALRDV-----SKGRTTIVIAH------RLSTivnadKIIVLKDGRIVERGTh 219
|
....
gi 547260874 222 AELL 225
Cdd:cd03253 220 EELL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-216 |
8.63e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL---------FTLSERERAQ----RAAFLPQKLPASEGLTCRELVRL 98
Cdd:PRK10619 36 IIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKVADKNQLRllrtRLTMVFQHFNLWSHMTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GRFPWRGLFgrwRAEDEAAVDEALAATGTAHYAQ-SYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTL 177
Cdd:PRK10619 116 APIQVLGLS---KQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVL 192
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 178 ALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK10619 193 RIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
8.95e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVK--PDA---GTTKLEGGDLFTLSE---RERA 74
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVielRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 75 QRAAFLPQKLPaseGLTCRELVRLGrfPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVD----DLSGGERQRVWISM 150
Cdd:PRK14247 85 QMVFQIPNPIP---NLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 151 LLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETgrGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-235 |
9.40e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 9.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKLPASEGLTC 92
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGiGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELVrLGRFPWRGLFGRWRAEDEAavDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:PRK10895 96 YDNL-MAVLQIRDDLSAEQREDRA--NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 173 QYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLF 235
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-225 |
9.49e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLeGGDLFTLSERERAQRAAFLPQ 82
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI-AGHQFDFSQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KL----------PAsegLTCRElvRLGRFPWRGLfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLL 152
Cdd:COG4161 83 KVgmvfqqynlwPH---LTVME--NLIEAPCKVL-GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 153 AQASPVMILDEPTSALDVRHQYGTLALLERLNrETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELL 225
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHF 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-198 |
9.72e-15 |
|
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: 71.63 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGG-----DLFTLSE--------RERAQRAAFLPQ---KLPASEGLT 91
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdeilDEFRGSElqnyftklLEGDVKVIVKPQyvdLIPKAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 92 CRELVRlgrfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVR 171
Cdd:cd03236 107 VGELLK-------------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*..
gi 547260874 172 HQYGTLALLERLNREtGRGVIAIIHDI 198
Cdd:cd03236 174 QRLNAARLIRELAED-DNYVLVVEHDL 199
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-239 |
1.11e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASE--GLTCRELVRLGRFPWrGLfgr 109
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN-PDDQifSPTVEQDIAFGPINL-GL--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 wraeDEAA----VDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNR 185
Cdd:PRK13652 110 ----DEETvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 186 ETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENL--RTLFEAPV 239
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLlaRVHLDLPS 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-216 |
1.40e-14 |
|
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: 70.96 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRAAFLPQKLPASEGL 90
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI-SQYEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGrfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDD-------LSGGERQRVWISMLLAQASPVMILDE 163
Cdd:cd03248 103 SLQDNIAYG------LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 547260874 164 PTSALDVRHQYGTLALLERLNREtgRGVIAIIHDINLALRfATHIVALKEGKV 216
Cdd:cd03248 177 ATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
32-245 |
1.40e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.08 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLV----KPDAGTTKLEGGDLFTLSERERAQ----RAAFLPQKLPAS------EGLTCRELVR 97
Cdd:PRK11022 38 IVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNlvgaEVAMIFQDPMTSlnpcytVGFQIMEAIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTL 177
Cdd:PRK11022 118 VHQ----GGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 178 ALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAPvklmLHP 245
Cdd:PRK11022 194 ELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAH---------DIFRAP----RHP 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-223 |
1.54e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 21 HLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLeGGDLFTLSERERAQRAAFLPQKL----------PAsegL 90
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI-AGNHFDFSKTPSDKAIRELRRNVgmvfqqynlwPH---L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRElvRLGRFPWRGLfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:PRK11124 98 TVQQ--NLIEAPCRVL-GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 547260874 171 RHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:PRK11124 175 EITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-198 |
1.58e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 30 TL-ILGHNGSGKSTLASIISGLVKPD---AGTTKLEGGDLFTLSERE----RAQRAAFLPQK--------LPASEGLTcr 93
Cdd:PRK09473 44 TLgIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklRAEQISMIFQDpmtslnpyMRVGEQLM-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 94 ELVRLGRfpwrglfGRWRAEdeaAVDEALAATGTAHYAQS------YVDDLSGGERQRVWISMLLAQASPVMILDEPTSA 167
Cdd:PRK09473 122 EVLMLHK-------GMSKAE---AFEESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190
....*....|....*....|....*....|.
gi 547260874 168 LDVRHQYGTLALLERLNRETGRGVIAIIHDI 198
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-237 |
1.68e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.06 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERA-----QRAAFLPQklpasegltcrelV 96
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDicmvfQSYALFPH-------------M 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLGRFPWRGL--FGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDvrhqy 174
Cdd:PRK11432 94 SLGENVGYGLkmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD----- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 175 gtlALLERLNRETGRGV--------IAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENlrTLFEA 237
Cdd:PRK11432 169 ---ANLRRSMREKIRELqqqfnitsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA--SRFMA 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-169 |
1.84e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASEGL 90
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD-PVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLGrfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVD-----------DLSGGERQRVWISMLLAQASPVM 159
Cdd:PRK10790 430 TFLANVTLG-----------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQIL 498
|
170
....*....|
gi 547260874 160 ILDEPTSALD 169
Cdd:PRK10790 499 ILDEATANID 508
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-220 |
2.18e-14 |
|
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: 70.25 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGD--LFTLSereraqrAAFLPQklpasegLTCRELVRL- 98
Cdd:cd03220 43 FEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVssLLGLG-------GGFNPE-------LTGRENIYLn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GRfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLA 178
Cdd:cd03220 109 GR-----LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 547260874 179 LLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:cd03220 184 RLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-203 |
2.33e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 25 PTHELTLIlGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQ-RA---AFLPQKLPASEGLTCRELVRLGR 100
Cdd:PRK10584 35 RGETIALI-GESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlRAkhvGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDvRHQYGTLA-L 179
Cdd:PRK10584 114 L----LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD-RQTGDKIAdL 188
|
170 180
....*....|....*....|....
gi 547260874 180 LERLNRETGRGVIAIIHDINLALR 203
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDLQLAAR 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-223 |
2.70e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.50 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEG--GDLFTLSereraqrAAFLPQklpasegLTCRELVRL-GRfpwrgLFG 108
Cdd:COG1134 57 IIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvSALLELG-------AGFHPE-------LTGRENIYLnGR-----LLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 RWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLnRETG 188
Cdd:COG1134 118 LSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESG 196
|
170 180 190
....*....|....*....|....*....|....*
gi 547260874 189 RGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:COG1134 197 RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-229 |
2.82e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlFTLSERERAQRA--AFL 80
Cdd:PRK13536 43 DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARLARAriGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 81 PQKLPASEGLTCRE-LVRLGRFpwrglFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVM 159
Cdd:PRK13536 120 PQFDNLDLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 160 ILDEPTSALD--VRHqygtlALLERLNRETGRG--VIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEE 229
Cdd:PRK13536 195 ILDEPTTGLDphARH-----LIWERLRSLLARGktILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-228 |
2.97e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERaQRAAFLPQ 82
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-QRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 83 KLPASEGLTCRE-LVRLGRFpwrglFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:PRK13537 88 FDNLDPDFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 162 DEPTSALD--VRHqygtlALLERLNRETGRG--VIAIIHDINLALRFATHIVALKEGKVLFSGGA-ELLHSE 228
Cdd:PRK13537 163 DEPTTGLDpqARH-----LMWERLRSLLARGktILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPhALIESE 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-220 |
3.18e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEggDLFTLSERE-RAQRAAFLPQKLPASEGLtcRELVRL-GRFPWRGLFGR 109
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIYIGDKKNnHELITNPYSKKIKNFKEL--RRRVSMvFQFPEYQLFKD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 WRAED------EAAVDEALAATGTAHY------AQSYVD----DLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ 173
Cdd:PRK13631 133 TIEKDimfgpvALGVKKSEAKKLAKFYlnkmglDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGE 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 547260874 174 YGTLALLERlNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13631 213 HEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-228 |
4.20e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLvkPDAGTtklegGDLftlsERERAQRAAFLPQK--LPasEG 89
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--WPYGS-----GRI----ARPAGARVLFLPQRpyLP--LG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 90 lTCRELVRLGRFPwrglfgrwRAEDEAAVDEALAATGTAHYAQSyVDD-------LSGGERQRVWISMLLAQASPVMILD 162
Cdd:COG4178 441 -TLREALLYPATA--------EAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 163 EPTSALDVRHQYGTLALLERLNRETgrGVIAIIHDINLAlRFATHIVALKEGkvlfsGGAELLHSE 228
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGT--TVISVGHRSTLA-AFHDRVLELTGD-----GSWQLLPAE 568
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-220 |
5.49e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPD---AGTTKLEGgdlFTLSERERAQRAAFLPQ------KLPASEGLTCRELVRL 98
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG---MPIDAKEMRAISAYVQQddlfipTLTVREHLMFQAHLRM 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 GRfpwrglfGRWRAEDEAAVDEALAATGTAHYAQS------YVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:TIGR00955 129 PR-------RVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 547260874 173 QYGTLALLERLNrETGRGVIAIIHDINLAL-RFATHIVALKEGKVLFSG 220
Cdd:TIGR00955 202 AYSVVQVLKGLA-QKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLG 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-197 |
5.92e-14 |
|
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: 71.12 E-value: 5.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlsereraQRAAFLPQKLPASEGLTCRELVRLGRFPWRGLFGRWR 111
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG-----------IKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 ----------------AEDEAAVDEALAATGtAHYAQSYVD----------------DLSGGERQRVWISMLLAQASPVM 159
Cdd:TIGR03719 105 eisakyaepdadfdklAAEQAELQEIIDAAD-AWDLDSQLEiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 547260874 160 ILDEPTSALDVRhqygTLALLERLNRETGRGVIAIIHD 197
Cdd:TIGR03719 184 LLDEPTNHLDAE----SVAWLERHLQEYPGTVVAVTHD 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
9.10e-14 |
|
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: 68.61 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVrndrtILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKL--EGG--DLFTLSERE---- 72
Cdd:COG4778 16 LHLQGGKRLP-----VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGwvDLAQASPREilal 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 73 RAQRAAFLPQKL------PASEgLTCRELVRLGrfpwrglFGRWRAEDEAA-------VDEALAATGTAHYaqsyvddlS 139
Cdd:COG4778 91 RRRTIGYVSQFLrviprvSALD-VVAEPLLERG-------VDREEARARARellarlnLPERLWDLPPATF--------S 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 140 GGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEG 214
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-231 |
1.01e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.35 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlftlsERERAQRAAFLPQKL------PASE--GLTCR 93
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG-------ELLTAENVWNLRRKIgmvfqnPDNQfvGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 94 ELVRLGRFPWrglfGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ 173
Cdd:PRK13642 101 DDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 174 YGTLALLERLNRETGRGVIAIIHDINLALRfATHIVALKEGKVLFSGG-AELLHSEENL 231
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAApSELFATSEDM 234
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
32-237 |
1.02e-13 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 70.69 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQklpaSEGL---TCRELVRLGRfpwrglfg 108
Cdd:TIGR01192 366 IVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQ----DAGLfnrSIRENIRLGR-------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 rwraedEAAVDEALAATGTAHYAQSYVDD---------------LSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ 173
Cdd:TIGR01192 434 ------EGATDEEVYEAAKAAAAHDFILKrsngydtlvgergnrLSGGERQRLAIARAILKNAPILVLDEATSALDVETE 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 174 YGTLALLERLNREtgRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELLHSEENLRTLFEA 237
Cdd:TIGR01192 508 ARVKNAIDALRKN--RTTFIIAHRLS-TVRNADLVLFLDQGRLIEKGSfQELIQKDGRFYKLLRR 569
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
33-229 |
1.88e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 67.75 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 33 LGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRA-AFLPQKlpAS--EGLTCR-------ELVRLGrfp 102
Cdd:COG1137 35 LGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGiGYLPQE--ASifRKLTVEdnilavlELRKLS--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 103 wrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAqASP-VMILDE------PTSALDVRHqyg 175
Cdd:COG1137 110 --------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA-TNPkFILLDEpfagvdPIAVADIQK--- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 176 tlaLLERLnRETGRGViaIIHDIN----LAL--RfaTHIvaLKEGKVLFSGGA-ELLHSEE 229
Cdd:COG1137 178 ---IIRHL-KERGIGV--LITDHNvretLGIcdR--AYI--ISEGKVLAEGTPeEILNNPL 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-230 |
2.89e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.88 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTtkLEGGDLFTLSE------RERAQRAAFLPQkLPAS---EGLTCRELvrlgrfp 102
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGT--VTVDDITITHKtkdkyiRPVRKRIGMVFQ-FPESqlfEDTVEREI------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 103 wrgLFG--RWRAEDEAAVDEA---LAATGTAHYAQSYVD-DLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGT 176
Cdd:PRK13646 108 ---IFGpkNFKMNLDEVKNYAhrlLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 547260874 177 LALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEEN 230
Cdd:PRK13646 185 MRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-196 |
3.27e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 33 LGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERER-AQRAAFLPQKLPASEGLTCRELVRLGRFPWR-GLFGRW 110
Cdd:PRK11288 36 MGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlAAGVAIIYQELHLVPEMTVAENLYLGQLPHKgGIVNRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 111 RAEDEAAvdEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLnRETGRG 190
Cdd:PRK11288 116 LLNYEAR--EQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRV 192
|
....*.
gi 547260874 191 VIAIIH 196
Cdd:PRK11288 193 ILYVSH 198
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-220 |
4.78e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.46 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE---RAQRAAFLPQKLPASEGL--TCRELV 96
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQFPESQLFeeTVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 RLGrfPWRglFGRWRAEDEAAVDEALAATGTAhyaQSYVD----DLSGGERQRVWISMLLAQASPVMILDEPTSALDVRH 172
Cdd:PRK13649 108 AFG--PQN--FGVSQEEAEALAREKLALVGIS---ESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547260874 173 QYGTLALLERLNrETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-252 |
5.30e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIptHELtliLGHNGSGKSTLASIISGLVKPD----AGTTKLEGGDLFTLSERER----AQRAAFLPQKl 84
Cdd:COG4170 24 DRVSLTLNEGEI--RGL---VGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrkiiGREIAMIFQE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 PAS-------------EGLTCRELVrlGRFpWRglfgRWRAEDEAAVdEALAATGT---AHYAQSYVDDLSGGERQRVWI 148
Cdd:COG4170 98 PSScldpsakigdqliEAIPSWTFK--GKW-WQ----RFKWRKKRAI-ELLHRVGIkdhKDIMNSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 149 SMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhse 228
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTE----- 244
|
250 260
....*....|....*....|....
gi 547260874 229 enlrTLFEAPvklmLHPdppaaYT 252
Cdd:COG4170 245 ----QILKSP----HHP-----YT 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-198 |
6.23e-13 |
|
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: 68.27 E-value: 6.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGG-----DLFTLSE--------RERAQRAAFLPQ---KLPASEGLTCREL 95
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdevlKRFRGTElqdyfkklANGEIKVAHKPQyvdLIPKVFKGTVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRlgrfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqyg 175
Cdd:COG1245 184 LE-------------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY---- 246
|
170 180 190
....*....|....*....|....*....|.
gi 547260874 176 tlallERLN-----RE---TGRGVIAIIHDI 198
Cdd:COG1245 247 -----QRLNvarliRElaeEGKYVLVVEHDL 272
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-230 |
8.21e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGG------DLFTLSERERA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 75 QRAAFLPQKLPASEGLTCRELVRlgrFPWRGLFGRWRAEDEAAVDEALAATG----TAHYAQSYVDDLSGGERQRVWISM 150
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 151 LLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETgrGVIAIIHDINLALRFATHIVALKEGKVLFSGGA-ELLHSEE 229
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSnEIFTSPK 244
|
.
gi 547260874 230 N 230
Cdd:PRK14246 245 N 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
134-223 |
1.17e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 134 YVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKE 213
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
90
....*....|
gi 547260874 214 GKVLFSGGAE 223
Cdd:PRK10261 245 GEAVETGSVE 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-198 |
1.19e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGG-----DLFTLSE--------RERAQRAAFLPQ---KLPASEGLTCREL 95
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDYEEEPSwdevlKRFRGTElqnyfkklYNGEIKVVHKPQyvdLIPKVFKGKVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRlgrfpwrglfgrwRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqyg 175
Cdd:PRK13409 184 LK-------------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR---- 246
|
170 180 190
....*....|....*....|....*....|
gi 547260874 176 tlallERLN-----RE--TGRGVIAIIHDI 198
Cdd:PRK13409 247 -----QRLNvarliRElaEGKYVLVVEHDL 271
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-214 |
1.78e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.04 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAG----TTKLEGGDLFTLSERERAQRAAFLPQKlPASEGLTC 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSVAYAAQK-PWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 93 RELVRLGRfPWRGlfGRWRAEDEAAV---DEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:cd03290 96 EENITFGS-PFNK--QRYKAVTDACSlqpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 170 VR-----HQYGTLALLerlnRETGRGVIAIIHDINLaLRFATHIVALKEG 214
Cdd:cd03290 173 IHlsdhlMQEGILKFL----QDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-169 |
2.96e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 5 NGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlFTLSERERAQRAAFLPQkL 84
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGH-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 PA-SEGLTCRELVRLgrfpWRGLFGRwRAEDEAAvdEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDE 163
Cdd:PRK13543 91 PGlKADLSTLENLHF----LCGLHGR-RAKQMPG--SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*.
gi 547260874 164 PTSALD 169
Cdd:PRK13543 164 PYANLD 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-228 |
3.20e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 37 GSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERErAQRA--AFLPQ--KlpaSEGL----TCRE---LVRLGRFPWRG 105
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-AIRAgiAYVPEdrK---GEGLvldlSIREnitLASLDRLSRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 106 LFgRWRAEDEAAvDEALAATG--TAHYAQSyVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERL 183
Cdd:COG1129 364 LL-DRRRERALA-EEYIKRLRikTPSPEQP-VGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL 440
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 184 NREtGRGVIAIIHDINLALRFATHIVALKEGKVlfsgGAELLHSE 228
Cdd:COG1129 441 AAE-GKAVIVISSELPELLGLSDRILVMREGRI----VGELDREE 480
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-242 |
5.41e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQ-RAAFLPQKLpaseG------LTCRE 94
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCpRIAYMPQGL----GknlyptLSVFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 95 LVRL-GRfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD--VR 171
Cdd:NF033858 98 NLDFfGR-----LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 172 HQYGTlaLLERLNRET-GRGVIAIIHDINLALRFAtHIVALKEGKVLFSGGAELLHSEENLRTLFEAPVKLM 242
Cdd:NF033858 173 RQFWE--LIDRIRAERpGMSVLVATAYMEEAERFD-WLVAMDAGRVLATGTPAELLARTGADTLEAAFIALL 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-197 |
5.78e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlsereraQRAAFLPQKLPASEGLTCRELVRLGRFPWRGLFGRWR 111
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-----------IKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 ------AEDEAAVDEALA---------ATGTAHYAQSY----------------VDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK11819 107 eiyaayAEPDADFDALAAeqgelqeiiDAADAWDLDSQleiamdalrcppwdakVTKLSGGERRRVALCRLLLEKPDMLL 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 547260874 161 LDEPTSALDVRhqygTLALLER-LNRETGrGVIAIIHD 197
Cdd:PRK11819 187 LDEPTNHLDAE----SVAWLEQfLHDYPG-TVVAVTHD 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-225 |
1.06e-11 |
|
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: 64.46 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILS-IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlseRERAQ---RAAF--LPQklpa 86
Cdd:COG5265 370 ERPILKgVS-FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-----RDVTQaslRAAIgiVPQ---- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 87 segltcrELVrlgrfpwrgLF----------GRWRAeDEAAVDEALAAtgtAHyaqsyVDD------------------- 137
Cdd:COG5265 440 -------DTV---------LFndtiayniayGRPDA-SEEEVEAAARA---AQ-----IHDfieslpdgydtrvgerglk 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWIS-MLLAQAsPVMILDEPTSALDVRHQYGTLALLERLNRetGRGVIAIIHdinlalRFAT-----HIVAL 211
Cdd:COG5265 495 LSGGEKQRVAIArTLLKNP-PILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH------RLSTivdadEILVL 565
|
250
....*....|....*
gi 547260874 212 KEGKVLFSGG-AELL 225
Cdd:COG5265 566 EAGRIVERGThAELL 580
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
1.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.57 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTT--KLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCREL-VRL 98
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKIKEIrRRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 G---RFPWRGLFGRWRAEDEA------AVDEALAATGTAHY------AQSYVD----DLSGGERQRVWISMLLAQASPVM 159
Cdd:PRK13651 108 GvvfQFAEYQLFEQTIEKDIIfgpvsmGVSKEEAKKRAAKYielvglDESYLQrspfELSGGQKRRVALAGILAMEPDFL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 160 ILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGA-ELLHSEENLRTLFEAP 238
Cdd:PRK13651 188 VFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTyDILSDNKFLIENNMEP 266
|
....
gi 547260874 239 VKLM 242
Cdd:PRK13651 267 PKLL 270
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
22-230 |
1.11e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLvkpdagtTKLEGGDLFTLSER-------ERA-----QRAAFLPQklpaseg 89
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGL-------EDITSGDLFIGEKRmndvppaERGvgmvfQSYALYPH------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 90 LTCRELVRLGRfpwrGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:PRK11000 90 LSVAENMSFGL----KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 170 VRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGA-ELLHSEEN 230
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPlELYHYPAN 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-198 |
1.39e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 30 TL-ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQRA--AFLPQKLPASegLTCRelVRLGRF---P 102
Cdd:PRK15079 49 TLgVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwRAVRSdiQMIFQDPLAS--LNPR--MTIGEIiaeP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 103 WRGLFGRW-RAEDEAAVDEALAATGT-AHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALL 180
Cdd:PRK15079 125 LRTYHPKLsRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204
|
170
....*....|....*...
gi 547260874 181 ERLNRETGRGVIAIIHDI 198
Cdd:PRK15079 205 QQLQREMGLSLIFIAHDL 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-220 |
1.67e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPD--AGTTKLEGGDLftlsERERAQRAAFLPQKLPASEGL 90
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRE---LVRLGRFPwRGLFG--RWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPT 165
Cdd:PLN03211 156 TVREtlvFCSLLRLP-KSLTKqeKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 166 SALDVRHQYGTLALLERLNREtGRGVIAIIHD-INLALRFATHIVALKEGKVLFSG 220
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-198 |
2.65e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 30 TL-ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRaaflpqklpasegltcRELVRLgRF--PWRGL 106
Cdd:PRK11308 43 TLaVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLL----------------RQKIQI-VFqnPYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 FGRW-----------------RAEDEAAVDEALAATG--TAHYaQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSA 167
Cdd:PRK11308 106 NPRKkvgqileepllintslsAAERREKALAMMAKVGlrPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190
....*....|....*....|....*....|.
gi 547260874 168 LDVRHQYGTLALLERLNRETGRGVIAIIHDI 198
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
112-238 |
4.54e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 AEDEAAVDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRG 190
Cdd:PRK15134 399 AQREQQVIAVMEEVGlDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLA 478
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 547260874 191 VIAIIHDINLALRFATHIVALKEGKVLFSGGAEllhseenlrTLFEAP 238
Cdd:PRK15134 479 YLFISHDLHVVRALCHQVIVLRQGEVVEQGDCE---------RVFAAP 517
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
28-225 |
4.98e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.13 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIISGLVKPDAGTT----KLEGGDLFTLSERERAQRAAF-------LPQK-LPASEGLTcREL 95
Cdd:PRK15093 34 EIRGLVGESGSGKSLIAKAICGVTKDNWRVTadrmRFDDIDLLRLSPRERRKLVGHnvsmifqEPQScLDPSERVG-RQL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VRL-------GRfpWRGLFGrWRAEDEAavdEALAATG-TAHYA--QSYVDDLSGGERQRVWISMLLAQASPVMILDEPT 165
Cdd:PRK15093 113 MQNipgwtykGR--WWQRFG-WRKRRAI---ELLHRVGiKDHKDamRSFPYELTEGECQKVMIAIALANQPRLLIADEPT 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 166 SALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELL 225
Cdd:PRK15093 187 NAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-232 |
5.61e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSER---ERAQRAAF 79
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 80 LPQKLPASEGLTCRELVrlgRFPWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVM 159
Cdd:PRK11831 89 LFQSGALFTDMNVFDNV---AYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 160 ILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLR 232
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-220 |
5.81e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 16 ILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAF-------LPQKLPA 86
Cdd:PRK11300 18 LLAVNNvnLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrtfqhvrLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 87 SEGLTCRELVRLGRFPWRGLF---GRWRAEDEaAVDEA---LAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:PRK11300 98 IENLLVAQHQQLKTGLFSGLLktpAFRRAESE-ALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSG 220
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-227 |
7.81e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlpasEGL---TCRELVRLGRfpwrglfg 108
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD----AGLfnrSIEDNIRVGR-------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 rwraedEAAVDEALAATGTAHYAQSYVDD---------------LSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ 173
Cdd:PRK13657 434 ------PDATDEEMRAAAERAQAHDFIERkpdgydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 174 YGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELLHS 227
Cdd:PRK13657 508 AKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSfDELVAR 559
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-225 |
1.35e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL--FTLSEReRAQrAAFLPQKLpasegltcrelvrlg 99
Cdd:PRK11176 364 FKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdYTLASL-RNQ-VALVSQNV--------------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 rfpwrGLFgrwraEDEAAVDEALAATG-----------TAHYAQSYVDD---------------LSGGERQRVWISMLLA 153
Cdd:PRK11176 427 -----HLF-----NDTIANNIAYARTEqysreqieeaaRMAYAMDFINKmdngldtvigengvlLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 154 QASPVMILDEPTSALDVRHQYGTLALLERLNREtgRGVIAIIHDINlALRFATHIVALKEGKVLFSGG-AELL 225
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEKADEILVVEDGEIVERGThAELL 566
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-223 |
1.76e-10 |
|
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: 60.97 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFT------LSERERAQR-AAFLPQK---LPAS---E 88
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVdmtkpgPDGRGRAKRyIGILHQEydlYPHRtvlD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTcrELVRLgRFPwrglfgrwraeDEAAVDEA---LAATG-TAHYAQS----YVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:TIGR03269 385 NLT--EAIGL-ELP-----------DELARMKAvitLKMVGfDEEKAEEildkYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 161 LDEPTSALD--VRHQYGTLALLERlnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAE 223
Cdd:TIGR03269 451 LDEPTGTMDpiTKVDVTHSILKAR--EEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
32-227 |
1.86e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.80 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlpASEGLTCRElvRLGR---FPWRGLFG 108
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD--PSTSLNPRQ--RISQildFPLRLNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 RWRAEDEAAVDEALAATGT-AHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRET 187
Cdd:PRK15112 120 LEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQ 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 547260874 188 GRGVIAIIHDINLALRFATHIVALKEGKVLFSGG-AELLHS 227
Cdd:PRK15112 200 GISYIYVTQHLGMMKHISDQVLVMHQGEVVERGStADVLAS 240
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-230 |
2.49e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGlvKPD----AGTTKLEGGDLFTLSERERAQR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFL----PQKLPaseGLTCRELVRLG---RFPWRGLFGRWRAEDEAAVDEALAATG-TAHYAQSYVDD-LSGGERQRVW 147
Cdd:CHL00131 85 GIFLafqyPIEIP---GVSNADFLRLAynsKRKFQGLPELDPLEFLEIINEKLKLVGmDPSFLSRNVNEgFSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 148 ISMLLAQASPVMILDEPTSALDVRhqygtlAL---LERLN--RETGRGVIAIIHDINLaLRFA----THIvaLKEGKVLF 218
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDID------ALkiiAEGINklMTSENSIILITHYQRL-LDYIkpdyVHV--MQNGKIIK 232
|
250
....*....|..
gi 547260874 219 SGGAELLHSEEN 230
Cdd:CHL00131 233 TGDAELAKELEK 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-217 |
3.20e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.46 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE---RAQRAAFLPQKLPASEGL--TCRELVRLGrfPWRgl 106
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkKLRKKVSLVFQFPEAQLFenTVLKDVEFG--PKN-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 107 FGrwrAEDEAAVDEALAATGTAHYAQSYVD----DLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLER 182
Cdd:PRK13641 114 FG---FSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD 190
|
170 180 190
....*....|....*....|....*....|....*
gi 547260874 183 LNREtGRGVIAIIHDINLALRFATHIVALKEGKVL 217
Cdd:PRK13641 191 YQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-211 |
4.18e-10 |
|
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: 57.16 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGT-TKLEGGDLFtlsereraqraaFLPQK--LPASe 88
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRiGMPEGEDLL------------FLPQRpyLPLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 glTCRELVRlgrFPWRglfgrwraedeaavdealaatgtahyaqsyvDDLSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:cd03223 79 --TLREQLI---YPWD-------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 547260874 169 DVrhqyGTLALLERLNRETGRGVIAIIHDINLaLRFATHIVAL 211
Cdd:cd03223 123 DE----ESEDRLYQLLKELGITVISVGHRPSL-WKFHDRVLDL 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-216 |
5.19e-10 |
|
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: 57.81 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGLTCRELVRLGRFpwrglfgrwr 111
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEY---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 aeDEAAVDEALAATGTAhyaqsyvDDLSGGERQRVWISMLLAQASPVMILDEPTSALDvrhqYGTLALLERLNRE--TGR 189
Cdd:cd03369 109 --SDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLVLDEATASID----YATDALIQKTIREefTNS 175
|
170 180
....*....|....*....|....*..
gi 547260874 190 GVIAIIHDINLALRFAtHIVALKEGKV 216
Cdd:cd03369 176 TILTIAHRLRTIIDYD-KILVMDAGEV 201
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-215 |
9.90e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 9.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL-FTLSERERAQRAAFLPQKLPASEGLTCRELVRLGR 100
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQELNLVLQRSVMDNMWLGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPWRGLF---GRWRAEDEAAVDEalaaTGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL---DVRHQY 174
Cdd:PRK10982 99 YPTKGMFvdqDKMYRDTKAIFDE----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNHLF 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 547260874 175 GTLALLerlnRETGRGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:PRK10982 175 TIIRKL----KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-216 |
2.16e-09 |
|
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: 55.52 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDHLEIPTHE----LTL-------ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQR-AAFLP 81
Cdd:cd03215 2 EPVLEVRGLSVKGAVrdvsFEVrageivgIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 QKlpasegltcrelvRLGRfpwrGLFGrwraedEAAVDEALAATgtahyaqsyvDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:cd03215 82 ED-------------RKRE----GLVL------DLSVAENIALS----------SLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 162 DEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-196 |
3.35e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 6 GIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVK--PDAGTTKLEGGDlftlsereraqraafLPQK 83
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ---------------FGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 LPASEGLtcrelvrlgrfpwrglfgrWRAEDEAAVDEALAATGTAHyAQSY---VDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:COG2401 100 ASLIDAI-------------------GRKGDFKDAVELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIH 196
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-215 |
4.12e-09 |
|
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: 55.17 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 16 ILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlftlsereraqRAAFLPQKlpasegltcrel 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQE------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 vrlgrfPW------RG--LFGRwrAEDEAAVDEALAATgtahyaqSYVDD------------------LSGGERQRvwIS 149
Cdd:cd03250 75 ------PWiqngtiREniLFGK--PFDEERYEKVIKAC-------ALEPDleilpdgdlteigekginLSGGQKQR--IS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547260874 150 mlLAQA----SPVMILDEPTSALDV---RHQYgTLALLERLNRetGRGVIAIIHDINLALRfATHIVALKEGK 215
Cdd:cd03250 138 --LARAvysdADIYLLDDPLSAVDAhvgRHIF-ENCILGLLLN--NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-214 |
4.23e-09 |
|
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: 56.95 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTlSERERAQRAAFLPQKLPASEGLTCRELVRLgrfpWRGLFGRWR 111
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHLYL----YARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 AEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGV 191
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAV 2123
|
170 180
....*....|....*....|...
gi 547260874 192 IAIIHDINLALRFATHIVALKEG 214
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-231 |
5.56e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.39 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 6 GIRMVRNDRTILSID--------HLEIPTHELTLILGHNGSGKSTLASIISGLVkPDAGTTKLEGGDLFTLSERERAQRA 77
Cdd:PRK11174 347 PVTIEAEDLEILSPDgktlagplNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 78 AFLPQ--KLPASeglTCRELVRLGRFpwrglfgrwrAEDEAAVDEALAATgtahYAQSYVDD---------------LSG 140
Cdd:PRK11174 426 SWVGQnpQLPHG---TLRDNVLLGNP----------DASDEQLQQALENA----WVSEFLPLlpqgldtpigdqaagLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 141 GERQRVWISMLLAQASPVMILDEPTSALDVRHQYgtlALLERLNRET-GRGVIAIIHDINlALRFATHIVALKEGKVLFS 219
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ---LVMQALNAASrRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQ 564
|
250
....*....|..
gi 547260874 220 GGAELLHSEENL 231
Cdd:PRK11174 565 GDYAELSQAGGL 576
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-220 |
6.18e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.99 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlTCRELVRLGRF 101
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSA-TLRDNLLLAAP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 pwrglfgrwRAEDEAAVdEALAATGTAHYAQSyvDD------------LSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:PRK11160 440 ---------NASDEALI-EVLQQVGLEKLLED--DKglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 547260874 170 VRHQYGTLALLERLNRetGRGVIAIIHDINLALRFaTHIVALKEGKVLFSG 220
Cdd:PRK11160 508 AETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-196 |
6.47e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsERERA---QRAAFLPQKLPASE 88
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCtyqKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 89 GLTCRElvrlgrfpwRGLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL 168
Cdd:PRK13540 88 YLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 547260874 169 DVRHQYGTLALLERlNRETGRGVIAIIH 196
Cdd:PRK13540 159 DELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-197 |
7.82e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftLSERERAQRAAF--------LPQKLPASEGltcr 93
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYRKLFsavftdfhLFDQLLGPEG---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 94 elvrlgrfpwrglfgrwRAEDEAAVDEALAATGTAHYAQsyVDD-------LSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:PRK10522 418 -----------------KPANPALVEKWLERLKMAHKLE--LEDgrisnlkLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190
....*....|....*....|....*....|....
gi 547260874 167 ALDV---RHQYgtLALLERLnRETGRGVIAIIHD 197
Cdd:PRK10522 479 DQDPhfrREFY--QVLLPLL-QEMGKTIFAISHD 509
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-238 |
2.32e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 25 PTHELTLIlGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERE-RAQR--AAFLPQKLPASegLTCRELVRLGRF 101
Cdd:PRK10261 349 PGETLSLV-GESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlQALRrdIQFIFQDPYAS--LDPRQTVGDSIM 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 PWRGLFGRWRAEDEAA-VDEALAATG-TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLAL 179
Cdd:PRK10261 426 EPLRVHGLLPGKAAAArVAWLLERVGlLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINL 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 180 LERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAellhseenlRTLFEAP 238
Cdd:PRK10261 506 LLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR---------RAVFENP 555
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-228 |
2.44e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDL--FTLSERERAqrAAFLPQKlPASEGLTCRelVRLGRFPWRGLFGR 109
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVakFGLTDLRRV--LSIIPQS-PVLFSGTVR--FNIDPFSEHNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 WRAEDEAAVDEALAATGTAHYAQSYV--DDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTLALLERLNRET 187
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR----TDSLIQRTIREE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 188 GRG--VIAIIHDINLALRfATHIVALKEGKVL-FSGGAELLHSE 228
Cdd:PLN03232 1418 FKSctMLVIAHRLNTIID-CDKILVLSSGQVLeYDSPQELLSRD 1460
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-215 |
2.99e-08 |
|
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: 52.19 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 23 EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlftlsereraQRAAFLPQKLpasegltcrelvrlgrfp 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------ITPVYKPQYI------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 103 wrglfgrwraedeaavdealaatgtahyaqsyvdDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLER 182
Cdd:cd03222 71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|...
gi 547260874 183 LNRETGRGVIAIIHDInLALRFATHIVALKEGK 215
Cdd:cd03222 117 LSEEGKKTALVVEHDL-AVLDYLSDRIHVFEGE 148
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-199 |
3.15e-08 |
|
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: 52.88 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLPASEGlTCRE-LVRLGR 100
Cdd:cd03244 25 FSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSnLDPFGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 101 FPWRGLfgrWRAEDEAAVDEALAATGTAHYAQsyVDD----LSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygT 176
Cdd:cd03244 104 YSDEEL---WQALERVGLKEFVESLPGGLDTV--VEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPE----T 174
|
170 180
....*....|....*....|....*
gi 547260874 177 LALLERLNRE--TGRGVIAIIHDIN 199
Cdd:cd03244 175 DALIQKTIREafKDCTVLTIAHRLD 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-169 |
3.20e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 33 LGHNGSGKSTLASIISGLVKPDAGTTKLEG-----GDLFTlseReraQRAAFLPQKLPASEGLTCRE-LVRLGRfpwrgL 106
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdaGDIAT---R---RRVGYMSQAFSLYGELTVRQnLELHAR-----L 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 107 FGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRvwISmlLAQA---SP-VMILDEPTSALD 169
Cdd:NF033858 367 FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQR--LS--LAVAvihKPeLLILDEPTSGVD 429
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-170 |
4.07e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGL--VKPDAGTTKLEGGDLFTLSERERAQRAA 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FL----PQKLPA-----------SEGLTCRELVRLGRFPWRGLFgrwraEDEAAVDEALAATGTahyaQSYVDDLSGGER 143
Cdd:PRK09580 81 FMafqyPVEIPGvsnqfflqtalNAVRSYRGQEPLDRFDFQDLM-----EEKIALLKMPEDLLT----RSVNVGFSGGEK 151
|
170 180
....*....|....*....|....*..
gi 547260874 144 QRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-220 |
5.58e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 2 YELNGIRmVRNdrtiLSIDHLEIPTHELTLILGHNGSGKSTLASiisglvkpdAGTTKLEGGDLFTLSERERAQRAAFLP 81
Cdd:cd03238 1 LTVSGAN-VHN----LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 Q-KLPASEGLtcrELVRLGRfpwrglfgrwraedeaavdealaATGTahyaqsyvddLSGGERQRVWISMLLAQASP--V 158
Cdd:cd03238 67 QlQFLIDVGL---GYLTLGQ-----------------------KLST----------LSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLaLRFATHIVALKE------GKVLFSG 220
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-248 |
8.93e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGttkleggdlftlsERE-RAQRAAFLP----QKLPA 86
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG-------------ERQsQFSHITRLSfeqlQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 87 SE----------------GLTCRELVRLGrfpwrglfgrwrAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVwism 150
Cdd:PRK10938 81 DEwqrnntdmlspgeddtGRTTAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKT---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 151 LLAQA---SP-VMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGG----- 221
Cdd:PRK10938 145 LLCQAlmsEPdLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEreeil 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 547260874 222 -----AELLHSEEN----LRTLFEAPVKLMLHPDPP 248
Cdd:PRK10938 224 qqalvAQLAHSEQLegvqLPEPDEPSARHALPANEP 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-216 |
1.07e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 10 VRNDRTILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQR-AAFLP---QK 83
Cdd:COG3845 265 VRDDRGVPALKDvsLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 LPASEGLTCRELVRLGRFpWRGLFGRWRAEDEAAVDEalaatgtahYAQSYVDD--------------LSGGERQRVWIS 149
Cdd:COG3845 345 RGLVPDMSVAENLILGRY-RRPPFSRGGFLDRKAIRA---------FAEELIEEfdvrtpgpdtparsLSGGNQQKVILA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 150 MLLAQASPVMILDEPTSALDVR-----HQygtlALLERlnRETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGaiefiHQ----RLLEL--RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-241 |
1.16e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 17 LSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlsereraqraAFLPQkLPASEGLTCRELV 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSV------------AYVPQ-VSWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 97 rlgrfpwrgLFGR-------WRAEDEAAVDEAL---AATGTAHYAQSYVDdLSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:PLN03232 700 ---------LFGSdfeseryWRAIDVTALQHDLdllPGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 167 ALD--VRHQYGTLALLERLNRETGRGVIAIIHDINLALRfathIVALKEGKVLFSGG-AELLHSEENLRTLFEAPVKL 241
Cdd:PLN03232 770 ALDahVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR----IILVSEGMIKEEGTfAELSKSGSLFKKLMENAGKM 843
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-183 |
1.41e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 2 YELNGIRMVRN-DRTILSIDhleipthELTLIlGHNGSGKSTLASIISGLVKPDAGT----TKLEggdlftlsereraqr 76
Cdd:PRK11147 327 YQIDGKQLVKDfSAQVQRGD-------KIALI-GPNGCGKTTLLKLMLGQLQADSGRihcgTKLE--------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFlpqklpasegltcrelvrlgrfpwrglFGRWRAE--DEAAVDEALA-------ATGTAHYAQSYVDD---------- 137
Cdd:PRK11147 384 VAY---------------------------FDQHRAEldPEKTVMDNLAegkqevmVNGRPRHVLGYLQDflfhpkramt 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 ----LSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTLALLERL 183
Cdd:PRK11147 437 pvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE----TLELLEEL 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-170 |
1.52e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMV-RNDRTILSIDHL----------EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSER 71
Cdd:PRK15439 254 ELPGNRRQqAAGAPVLTVEDLtgegfrnislEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 72 ERAQRA-AFLPQKLPASeGL---------TCRELVRLgrfpwRGLFGRwRAEDEAAVDEALAATGT--AHYAQSyVDDLS 139
Cdd:PRK15439 334 QRLARGlVYLPEDRQSS-GLyldaplawnVCALTHNR-----RGFWIK-PARENAVLERYRRALNIkfNHAEQA-ARTLS 405
|
170 180 190
....*....|....*....|....*....|.
gi 547260874 140 GGERQRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-196 |
1.54e-07 |
|
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: 50.32 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 29 LTLILGHNGSGKSTLASIISGlvKPDAGTTKlegGDLfTLSERER----AQRAAFLPQKLPASEGLTCRELVRLgrfpwr 104
Cdd:cd03232 35 LTALMGESGAGKTTLLDVLAG--RKTAGVIT---GEI-LINGRPLdknfQRSTGYVEQQDVHSPNLTVREALRF------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 105 glfgrwraedeaavdealaatgtahyaQSYVDDLSGGERQRVWISMLLAqASPVMI-LDEPTSALDVRHQYGTLALLERL 183
Cdd:cd03232 103 ---------------------------SALLRGLSVEQRKRLTIGVELA-AKPSILfLDEPTSGLDSQAAYNIVRFLKKL 154
|
170
....*....|...
gi 547260874 184 NrETGRGVIAIIH 196
Cdd:cd03232 155 A-DSGQAILCTIH 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-215 |
4.09e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 34 GHNGSGKSTLASIISGlVKPDA---GTTKLEGGDL--FTLSERERAQrAAFLPQKLPASEGLTCRELVRLGRFPWRGLFG 108
Cdd:PRK13549 38 GENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELqaSNIRDTERAG-IAIIHQELALVKELSVLENIFLGNEITPGGIM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 109 RWRAEDEAAvDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLnRETG 188
Cdd:PRK13549 116 DYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHG 193
|
170 180
....*....|....*....|....*..
gi 547260874 189 RGVIAIIHDINLALRFATHIVALKEGK 215
Cdd:PRK13549 194 IACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
28-189 |
4.28e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 28 ELTLILGHNGSGKSTLASIIS--GLVKPD---AGTTKLEGGDLF-----TLSERERAQRAAFLPQKLPasegLTCRELVR 97
Cdd:PRK14239 32 EITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYsprtdTVDLRKEIGMVFQQPNPFP----MSIYENVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGrFPWRGLfgrwraEDEAAVDEALAATGTAHYAQSYVDD--------LSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:PRK14239 108 YG-LRLKGI------KDKQVLDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180 190
....*....|....*....|....*....|...
gi 547260874 170 -------------VRHQYgTLALLERLNRETGR 189
Cdd:PRK14239 181 pisagkieetllgLKDDY-TMLLVTRSMQQASR 212
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-209 |
4.47e-07 |
|
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: 49.14 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 26 THELTLILGHNGSGKSTLASIIS----GLVKPdaGTTKLEGGDLFTLSERERAQ-RAAFlpqKLPASEGLTC-REL---- 95
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALKyaltGELPP--NSKGGAHDPKLIREGEVRAQvKLAF---ENANGKKYTItRSLaile 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 ----VRLGRFpwrglfgRWRAEDEaavdealaatgtahyaqsyVDDLSGGERQ------RVWISMLLAQASPVMILDEPT 165
Cdd:cd03240 96 nvifCHQGES-------NWPLLDM-------------------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 547260874 166 SALDVRHQYGTLA-LLERLNRETGRGVIAIIHDINLaLRFATHIV 209
Cdd:cd03240 150 TNLDEENIEESLAeIIEERKSQKNFQLIVITHDEEL-VDAADHIY 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-231 |
4.57e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 37 GSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSE-----------RERAQRAAFLPQkLPASEGLTCRELVRLGRfpWRG 105
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavkkgmayiTESRRDNGFFPN-FSIAQNMAISRSLKDGG--YKG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 106 LFGRWRAEDEAAVDEA---LAATGTAHYAQSyVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVrhqyGTLALLER 182
Cdd:PRK09700 376 AMGLFHEVDEQRTAENqreLLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDV----GAKAEIYK 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 547260874 183 LNR---ETGRGVIAIIHDINLALRFATHIVALKEGKV--LFSGGAELlhSEENL 231
Cdd:PRK09700 451 VMRqlaDDGKVILMVSSELPEIITVCDRIAVFCEGRLtqILTNRDDM--SEEEI 502
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-216 |
4.70e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 23 EIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEG-GDLFTLSereraqraAFLPQKLPASEGLTCRELvrlgrf 101
Cdd:PRK13545 46 EVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAIS--------SGLNGQLTGIENIELKGL------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 102 pwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEptsALDVRHQYGTLALLE 181
Cdd:PRK13545 112 ----MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLD 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 547260874 182 RLN--RETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK13545 185 KMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-223 |
5.57e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEggdlftlserERAQrAAFLPQKLPA--SEGLTCrelvrlgrFPWrglFGR 109
Cdd:PRK15064 350 IIGENGVGKTTLLRTLVGELEPDSGTVKWS----------ENAN-IGYYAQDHAYdfENDLTL--------FDW---MSQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 110 WRAE--DEAAVDEALaatG----TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHqygtlalLERL 183
Cdd:PRK15064 408 WRQEgdDEQAVRGTL---GrllfSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES-------IESL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 184 NR--ETGRG-VIAIIHDINLALRFATHIVALKEGKVL-FSGGAE 223
Cdd:PRK15064 478 NMalEKYEGtLIFVSHDREFVSSLATRIIEITPDGVVdFSGTYE 521
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-238 |
6.03e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILSIDhLEIPTHELTLILGHNGSGKSTLASIISGLVK--PDA---GTTKLEGGDLFT-----LSERERAQRAAFLP 81
Cdd:PRK14267 16 SNHVIKGVD-LKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdvdpIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 QKLPAsegLTCRELVRLGrFPWRGLFgRWRAEDEAAVDEALAATG----TAHYAQSYVDDLSGGERQRVWISMLLAQASP 157
Cdd:PRK14267 95 NPFPH---LTIYDNVAIG-VKLNGLV-KSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 158 VMILDEPTSALDVRHQYGTLALLERLNRETgrGVIAIIHDINLALRFATHIVALKEGKVLFSGGAellhseenlRTLFEA 237
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPT---------RKVFEN 238
|
.
gi 547260874 238 P 238
Cdd:PRK14267 239 P 239
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-212 |
8.59e-07 |
|
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: 47.37 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 26 THELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKLpasegltcrelvrlgrfpwrg 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 106 lfgrwraedeaavdealaatgtahyaqsyvdDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQ-----YGTLALL 180
Cdd:smart00382 60 -------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLL 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 547260874 181 ERLNRETGRGVIAIIH------DINLALRFATHIVALK 212
Cdd:smart00382 109 LLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLL 146
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-169 |
1.06e-06 |
|
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: 48.03 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTL----ASIISGLVKPDaGTTKLEGGDLFTLSERERAQrAAFLPQ---K 83
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGE-IIYVSEedvH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 LPAsegLTCRELvrlgrfpwrglfgrwraedeaaVDEALAATGTAhyaqsYVDDLSGGERQRVWISMLLAQASPVMILDE 163
Cdd:cd03233 95 FPT---LTVRET----------------------LDFALRCKGNE-----FVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
....*.
gi 547260874 164 PTSALD 169
Cdd:cd03233 145 STRGLD 150
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
19-216 |
1.28e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.03 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 19 IDhLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLftlserERAQRAAFlpqklpasegltcREL--- 95
Cdd:COG4615 351 ID-LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV------TADNREAY-------------RQLfsa 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 96 VrlgrFP----WRGLFGRWRAEDEAAVDEALAATGTAHyAQSYVD------DLSGGERQRVwiSMLLAQAS--PVMILDE 163
Cdd:COG4615 411 V----FSdfhlFDRLLGLDGEADPARARELLERLELDH-KVSVEDgrfsttDLSQGQRKRL--ALLVALLEdrPILVFDE 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547260874 164 ------PTsaldVRHQYGTlALLERLnRETGRGVIAIIHD---INLALRfathIVALKEGKV 216
Cdd:COG4615 484 waadqdPE----FRRVFYT-ELLPEL-KARGKTVIAISHDdryFDLADR----VLKMDYGKL 535
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-215 |
1.49e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGlVKPdAGTtkLEGGDLF--------TLSERERA------QRAAFLPQklpasegLTCRELVR 97
Cdd:NF040905 32 LCGENGAGKSTLMKVLSG-VYP-HGS--YEGEILFdgevcrfkDIRDSEALgiviihQELALIPY-------LSIAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 98 LGRFPWRGLFGRW-RAEDEAAvdEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSAL---DVRHq 173
Cdd:NF040905 101 LGNERAKRGVIDWnETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSAA- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 547260874 174 ygtlaLLERLNRETGRGVIAII--HDINLALRFATHIVALKEGK 215
Cdd:NF040905 178 -----LLDLLLELKAQGITSIIisHKLNEIRRVADSITVLRDGR 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-237 |
1.53e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTL-ASIISGlvkpdagttkleggdlFTLSE-RERAQRA-AFLPQKlpasegltcrelvrl 98
Cdd:PTZ00243 681 VSVPRGKLTVVLGATGSGKSTLlQSLLSQ----------------FEISEgRVWAERSiAYVPQQ--------------- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 99 grfPW------RG---LFGRWRAEDEAAV--------DEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMIL 161
Cdd:PTZ00243 730 ---AWimnatvRGnilFFDEEDAARLADAvrvsqleaDLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 162 DEPTSALDVRhqygtlaLLERLNRETGRGVIA------IIHDINLALRfATHIVALKEGKVLFSGgaellHSEENLRTLF 235
Cdd:PTZ00243 807 DDPLSALDAH-------VGERVVEECFLGALAgktrvlATHQVHVVPR-ADYVVALGDGRVEFSG-----SSADFMRTSL 873
|
..
gi 547260874 236 EA 237
Cdd:PTZ00243 874 YA 875
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-232 |
4.78e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAG---------TTKLE-------GGDLFT-----LSER----ERAQR 76
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGriiyeqdliVARLQqdpprnvEGTVYDfvaegIEEQaeylKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 77 AAFLPQKLPASEGLtcRELVRL-GRFPWRGLfgrWRAEDEaaVDEALAATGTAhyAQSYVDDLSGGERQRVWISMLLAQA 155
Cdd:PRK11147 104 ISHLVETDPSEKNL--NELAKLqEQLDHHNL---WQLENR--INEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 156 SPVMILDEPTSALDVRhqygTLALLERLNRETGRGVIAIIHDINLALRFATHIVALKEGKVL-FSGGAE--LLHSEENLR 232
Cdd:PRK11147 175 PDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVsYPGNYDqyLLEKEEALR 250
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-220 |
5.30e-06 |
|
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: 46.45 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWISMLLAQASP---VMILDEPTSAL---DVRHqygtlaLLERLNRETGRG--VIAIIHDINLaLRFATHIV 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKK------LLEVLQRLVDKGntVVVIEHNLDV-IKCADWII 242
|
90
....*....|....*..
gi 547260874 210 AL------KEGKVLFSG 220
Cdd:cd03271 243 DLgpeggdGGGQVVASG 259
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-260 |
7.43e-06 |
|
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: 46.93 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWI-SMLLAQASPVM-ILDEPTSALdvrHQYGTLALLERLN--RETGRGVIAIIHDINlALRFATHIVALKE 213
Cdd:TIGR00630 489 LSGGEAQRIRLaTQIGSGLTGVLyVLDEPSIGL---HQRDNRRLINTLKrlRDLGNTLIVVEHDED-TIRAADYVIDIGP 564
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 547260874 214 GKVLFsgGAELLHSeenlrtlfEAPVKLMLHPDP-PAAYTGGKKQLPL 260
Cdd:TIGR00630 565 GAGEH--GGEVVAS--------GTPEEILANPDSlTGQYLSGRKKIEV 602
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-211 |
7.52e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 7.52e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 133 SYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDINlALRFATHIVAL 211
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-205 |
7.91e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDaGTTKLEGGDLF---TLSERE----RAQRAAFL----PQKLPASEGL 90
Cdd:PRK14258 28 MEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRVEFfnqNIYERRvnlnRLRRQVSMvhpkPNLFPMSVYD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVRLgrFPWRGlfgrwRAEDEAAVDEALAATG----TAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTS 166
Cdd:PRK14258 107 NVAYGVKI--VGWRP-----KLEIDDIVESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 547260874 167 ALDVRHQYGTLALLERLNRETGRGVIAIIHDINLALRFA 205
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-227 |
8.79e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.86 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 14 RTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKP-----DAGTTKLEGGDLF----TLSERERAQRAAFLPQKL 84
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFnyrdVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 85 PAS------EGLTCRELVRLGRFpwRGL-------FGRWRAEDEAAVDEALAatgtahyaqsyvddLSGGERQRVWISML 151
Cdd:PRK14271 114 PMSimdnvlAGVRAHKLVPRKEF--RGVaqarlteVGLWDAVKDRLSDSPFR--------------LSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547260874 152 LAQASPVMILDEPTSALDVRHQYGTLALLERL-NRETgrgVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHS 227
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLaDRLT---VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
11-169 |
9.99e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 9.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGdlftlsereraqRAAFLPQkLPASEGL 90
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRG------------TVAYVPQ-VSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELVrlgrfpwrgLFGR-------WRAEDEAAVD---EALAATGTAHYAQSYVDdLSGGERQRVWISMLLAQASPVMI 160
Cdd:PLN03130 694 TVRDNI---------LFGSpfdperyERAIDVTALQhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYI 763
|
....*....
gi 547260874 161 LDEPTSALD 169
Cdd:PLN03130 764 FDDPLSALD 772
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
135-212 |
1.10e-05 |
|
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: 44.66 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 135 VDDLSGGERQRVWISMLLAQAS----PVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALrFATHIVA 210
Cdd:cd03227 75 RLQLSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAE-LADKLIH 152
|
..
gi 547260874 211 LK 212
Cdd:cd03227 153 IK 154
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-265 |
1.19e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.85 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 11 RNDRTILSIDH--LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlFTLSERERA---QRAAFLPQK-- 83
Cdd:COG4586 30 REYREVEAVDDisFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEfarRIGVVFGQRsq 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 ----LPASEGLTC-RELVRLGRfpwrglfgrwrAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPV 158
Cdd:COG4586 107 lwwdLPAIDSFRLlKAIYRIPD-----------AEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 159 MILDEPTSALDVRHQYGTLALLERLNRETGRGVIAIIHDIN----LALRfathIVALKEGKVLFSGgaellhSEENLRTL 234
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdieaLCDR----VIVIDHGRIIYDG------SLEELKER 245
|
250 260 270
....*....|....*....|....*....|.
gi 547260874 235 FEAPVKLMLHPDPPAAytggKKQLPLDVAVV 265
Cdd:COG4586 246 FGPYKTIVLELAEPVP----PLELPRGGEVI 272
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-234 |
1.89e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 37 GSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERErAQRA--AFLPQKLPAsEG------------LTCRelvrlGRFP 102
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIRAgiMLCPEDRKA-EGiipvhsvadninISAR-----RHHL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 103 WRGLF--GRWRAEDEAAVDEALAATgTAHYAQSYVDdLSGGERQRVWISMLLAQASPVMILDEPTSALDV--RHQ-YGTL 177
Cdd:PRK11288 362 RAGCLinNRWEAENADRFIRSLNIK-TPSREQLIMN-LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKHEiYNVI 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 178 -ALLERlnretGRGVIAIIHDINLALRFATHIVALKEGKVlfsgGAELLHSEENLRTL 234
Cdd:PRK11288 440 yELAAQ-----GVAVLFVSSDLPEVLGVADRIVVMREGRI----AGELAREQATERQA 488
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
22-235 |
2.23e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.48 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 22 LEIPTHELTLILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLfTLSERERAQRA--AFLPQKLPASEGLTCRELVRLG 99
Cdd:PRK11614 26 LHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTAKIMREavAIVPEGRRVFSRMTVEENLAMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 100 RFpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSyVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD---VRHQYGT 176
Cdd:PRK11614 105 GF----FAERDQFQERIKWVYELFPRLHERRIQR-AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLApiiIQQIFDT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 177 LALLerlnRETGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTLF 235
Cdd:PRK11614 180 IEQL----REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-248 |
2.45e-05 |
|
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: 45.20 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGlVKPDA---GTTKLEGGDLFTLSERERAQRA-A 78
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAGiV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 79 FLPQKLPASEGLTCRELVRLGrfpwrglfgrwraedeaavDEALAATGTAHYAQSY--------------------VDDL 138
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLG-------------------NEITLPGGRMAYNAMYlraknllrelqldadnvtrpVGDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 139 SGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLF 218
Cdd:TIGR02633 143 GGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVA 221
|
250 260 270
....*....|....*....|....*....|
gi 547260874 219 SGGAELLhSEENLRTLFEAPVKLMLHPDPP 248
Cdd:TIGR02633 222 TKDMSTM-SEDDIITMMVGREITSLYPHEP 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-169 |
5.28e-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: 44.02 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRMVRNDRTILSIDHLEIPTHELTLILGHNGSGKSTLASIISGL--VKPDAG------------------------ 56
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGriiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 57 ------TTKLEGGDLFTLSERERA---QRAAFLPQKLPASEGL------TCRELVRLGRfpwrglfgrwraEDEAAVDEA 121
Cdd:TIGR03269 82 cpvcggTLEPEEVDFWNLSDKLRRrirKRIAIMLQRTFALYGDdtvldnVLEALEEIGY------------EGKEAVGRA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 547260874 122 ---LAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:TIGR03269 150 vdlIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
138-225 |
8.29e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 43.55 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNRetGRGVIAIIHDINlALRFATHIVALKEGKVL 217
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
....*...
gi 547260874 218 FSGGAELL 225
Cdd:PRK10789 529 QRGNHDQL 536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
111-198 |
9.06e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 111 RAEDEAAVDEALAA------TGTAHYAQSyvddLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQygtlALLER-- 182
Cdd:PTZ00265 1330 RACKFAAIDEFIESlpnkydTNVGPYGKS----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE----KLIEKti 1401
|
90
....*....|....*...
gi 547260874 183 --LNRETGRGVIAIIHDI 198
Cdd:PTZ00265 1402 vdIKDKADKTIITIAHRI 1419
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-234 |
9.67e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 9 MVRNDRTILSIDHLEIPTHELTL--ILGHNGSG--KSTLASIISGlvkPDAGTTKLEggdLFTLSERERAQRAAF---LP 81
Cdd:NF000106 19 LVKHFGEVKAVDGVDLDVREGTVlgVLGP*GAA**RGALPAHV*G---PDAGRRPWR---F*TWCANRRALRRTIg*hRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 82 QKLPASEGLTCRE-LVRLGRFpwrglFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMI 160
Cdd:NF000106 93 VR*GRRESFSGREnLYMIGR*-----LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547260874 161 LDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKVLFSGGAELLHSEENLRTL 234
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTL 240
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-181 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTIL-SIDHLEIPTHELTLiLGHNGSGKSTLASIISGLVKPDAGTTKLEGG---DLFTLSERE--RAQRAAF--LPQK 83
Cdd:PRK10636 323 GDRIILdSIKLNLVPGSRIGL-LGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklGYFAQHQLEflRADESPLqhLARL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 84 LPASEGLTCRELvrLGRFPWRGlfgrwraedeaavDEALAATGTahyaqsyvddLSGGERQRVWISMLLAQASPVMILDE 163
Cdd:PRK10636 402 APQELEQKLRDY--LGGFGFQG-------------DKVTEETRR----------FSGGEKARLVLALIVWQRPNLLLLDE 456
|
170
....*....|....*....
gi 547260874 164 PTSALDV-RHQYGTLALLE 181
Cdd:PRK10636 457 PTNHLDLdMRQALTEALID 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
138-216 |
1.69e-04 |
|
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: 42.50 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 138 LSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
135-220 |
1.74e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 135 VDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTLALLERLNR---ETGRGVIAIIH--DINLALRFATHIV 209
Cdd:PLN03140 1017 VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR----AAAIVMRTVRntvDTGRTVVCTIHqpSIDIFEAFDELLL 1092
|
90
....*....|.
gi 547260874 210 ALKEGKVLFSG 220
Cdd:PLN03140 1093 MKRGGQVIYSG 1103
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-200 |
1.94e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 138 LSGGERQRVWISMLLAQASP---VMILDEPTSAL---DVRHqygtlaLLERLNRETGRG--VIAIIHdiNL 200
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRK------LLEVLHRLVDKGntVVVIEH--NL 889
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-223 |
2.30e-04 |
|
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: 42.31 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWISMLLAQAS---PVMILDEPTSAL---DVRHqygtlaLLERLNR--ETGRGVIAIIHDINLaLRFATHIV 209
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKK------LLEVLQRlvDKGNTVVVIEHNLDV-IKTADYII 902
|
90 100
....*....|....*....|
gi 547260874 210 AL------KEGKVLFSGGAE 223
Cdd:TIGR00630 903 DLgpeggdGGGTVVASGTPE 922
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-248 |
2.32e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWISMLLAQASP---VMILDEPTSALdvrHQYGTLALLERLNRET--GRGVIAIIHDINLaLRFATHIVAL- 211
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGL---HTHDIKALIYVLQSLThqGHTVVIIEHNMHV-VKVADYVLELg 885
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 547260874 212 -----KEGKVLFSGGAELL-----HSEENLRTLFEAPVKLMLHPDPP 248
Cdd:PRK00635 886 peggnLGGYLLASCSPEELihlhtPTAKALRPYLSSPQELPYLPDPS 932
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-196 |
2.62e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILS-IDHLEIPThELTLILGHNGSGKSTLASIISGLVKpdagTTKLEGGDLFtLSERER----AQRAAFLPQKLPAS 87
Cdd:TIGR00956 775 KRVILNnVDGWVKPG-TLTALMGASGAGKTTLLNVLAERVT----TGVITGGDRL-VNGRPLdssfQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 88 EGLTCRELVRLGRFpWRGLFGRWRAEDEAAVDEALAATGTAHYAQSYV----DDLSGGERQRVWISMLLAqASPVMI--L 161
Cdd:TIGR00956 849 PTSTVRESLRFSAY-LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELV-AKPKLLlfL 926
|
170 180 190
....*....|....*....|....*....|....*
gi 547260874 162 DEPTSALDVRHQYGTLALLERLNrETGRGVIAIIH 196
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-216 |
2.83e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 13 DRTILSIDHLEIPTHELTLI--LGHNGSGKSTLASIISGLVKPDAGTTKLEGgdlftlsERERAQRAAFLPQKLPASEGL 90
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIglVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 91 TCRELvrlgrfpwrgLFGRWRAEDEAAVDEALAATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEptsALDV 170
Cdd:PRK13546 107 EFKML----------CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547260874 171 RHQYGTLALLERLN--RETGRGVIAIIHDINLALRFATHIVALKEGKV 216
Cdd:PRK13546 174 GDQTFAQKCLDKIYefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
3-220 |
4.09e-04 |
|
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: 40.70 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 3 ELNGIRmVRNDRTIlsidHLEIPTHELTLILGHNGSGKSTLA--------------SI-------ISGLVKPDagTTKLE 61
Cdd:cd03270 2 IVRGAR-EHNLKNV----DVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveSLsayarqfLGQMDKPD--VDSIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 62 GgdlftLSEreraqrAAFLPQKL----PASEGLTCREL---VRLgrfpwrgLFGR--WRAEDEAAVDEALAATGTAHYAQ 132
Cdd:cd03270 75 G-----LSP------AIAIDQKTtsrnPRSTVGTVTEIydyLRL-------LFARvgIRERLGFLVDVGLGYLTLSRSAP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 133 SyvddLSGGERQRVWI-SMLLAQASPVM-ILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLaLRFATHIVA 210
Cdd:cd03270 137 T----LSGGEAQRIRLaTQIGSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDT-IRAADHVID 210
|
250
....*....|....*.
gi 547260874 211 L------KEGKVLFSG 220
Cdd:cd03270 211 IgpgagvHGGEIVAQG 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-231 |
4.41e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 135 VDDLSGGERQRVWISMLL-AQASPVM-ILDEPTSALDVRHQYGTLALLERLnRETGRGVIAIIHDINLaLRFATHIVALK 212
Cdd:PRK00635 474 LATLSGGEQERTALAKHLgAELIGITyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQM-ISLADRIIDIG 551
|
90 100
....*....|....*....|....*.
gi 547260874 213 E------GKVLFSGG-AELLHSEENL 231
Cdd:PRK00635 552 PgagifgGEVLFNGSpREFLAKSDSL 577
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
29-64 |
5.68e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 40.87 E-value: 5.68e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 547260874 29 LTLILGHNGSGKSTLASIISGL-----VKPDAGTTKLEGGD 64
Cdd:COG4694 26 LNLIYGENGSGKSTLSRILRSLelgdtSSEVIAEFEIEAGG 66
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
17-62 |
6.04e-04 |
|
ATP-binding cassette domain of eukaryotic SMC5 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: 213244 [Multi-domain] Cd Length: 213 Bit Score: 39.89 E-value: 6.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 547260874 17 LSIDHLEI-PTHELTLILGHNGSGKSTLAS-IISGLvkpdAGTTKLEG 62
Cdd:cd03277 12 VTYDETEFrPGPSLNMIIGPNGSGKSSIVCaICLGL----GGKPKLLG 55
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
138-205 |
6.34e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.15 E-value: 6.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 138 LSGGERQRVWISMLLAQASPVMILDEPTSALDvrhQYGTLAlLERLNRETGR--GVIAIIHDINLALRFA 205
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALD---PISTLR-IEELMHELKEqyTIIIVTHNMQQAARVS 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-170 |
6.67e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNG---SGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERER-AQRAAFLpqklpaSE---------GLTCRE---L 95
Cdd:PRK10762 280 ILGVSGlmgAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlANGIVYI------SEdrkrdglvlGMSVKEnmsL 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547260874 96 VRLGRFPWRGlfGRWRAEDE-AAVDE--ALAATGTAHYAQSyVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDV 170
Cdd:PRK10762 354 TALRYFSRAG--GSLKHADEqQAVSDfiRLFNIKTPSMEQA-IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
18-52 |
7.06e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 7.06e-04
10 20 30
....*....|....*....|....*....|....*
gi 547260874 18 SIDHLEIPTHELTLILGHNGSGKSTLASIISGLVK 52
Cdd:COG4938 11 PFKEAELELKPLTLLIGPNGSGKSTLIQALLLLLQ 45
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-183 |
7.31e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 26 THELTLILGHNGSGKSTL---------------ASIISGLVKPDAGTTKLE-----GGDLFTLsERERAQRAAFLPQKlP 85
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTIleairyalygkarsrSKLRSDLINVGSEEASVElefehGGKRYRI-ERRQGEFAEFLEAK-P 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 86 ASEGLTCRELVRLGRF-PWRGLFGRWRAEDEAAVDEALAATG-TAHYAQSY-----VDDLSGGERQRVWISMLLAqaspv 158
Cdd:COG0419 100 SERKEALKRLLGLEIYeELKERLKELEEALESALEELAELQKlKQEILAQLsgldpIETLSGGERLRLALADLLS----- 174
|
170 180
....*....|....*....|....*
gi 547260874 159 MILDepTSALDVRHQYGTLALLERL 183
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEEL 197
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-200 |
7.44e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 7.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547260874 138 LSGGERQRVWISMLLAQAS---PVMILDEPTSAL---DVRHqygtlaLLERLNR--ETGRGVIAIIHdiNL 200
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRK------LLEVLHRlvDKGNTVVVIEH--NL 893
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-216 |
8.62e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 132 QSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAIIHDINLALRFATHIVAL 211
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVM 464
|
....*
gi 547260874 212 KEGKV 216
Cdd:PRK10982 465 SNGLV 469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-229 |
8.82e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 32 ILGHNGSGKSTLASIISGLVKPDAGTTKLEGGDLFTLSERERAQRAAFLPQKlPASEGLTCRelVRLGRFPWRGLFGRWR 111
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-PVLFSGTVR--FNLDPFNEHNDADLWE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 112 AEDEAAVDEALA--ATGTAHYAQSYVDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRhqygTLALLERLNRETGR 189
Cdd:PLN03130 1347 SLERAHLKDVIRrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR----TDALIQKTIREEFK 1422
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 547260874 190 G--VIAIIHDINLALRfATHIVALKEGKVL-FSGGAELLHSEE 229
Cdd:PLN03130 1423 SctMLIIAHRLNTIID-CDRILVLDAGRVVeFDTPENLLSNEG 1464
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-49 |
9.91e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 9.91e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 547260874 12 NDRTILsiDHL--EIPTHELTLILGHNGSGKSTLASIISG 49
Cdd:PRK10938 271 NDRPIL--HNLswQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
135-194 |
1.23e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547260874 135 VDDLSGGERQRVWISMLLAQASPVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAI 194
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVI 460
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-43 |
1.28e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.28e-03
10 20
....*....|....*....|....*.
gi 547260874 18 SIDHLEIPTHELTLILGHNGSGKSTL 43
Cdd:COG4637 12 SLRDLELPLGPLTVLIGANGSGKSNL 37
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
137-169 |
1.56e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.86 E-value: 1.56e-03
10 20 30
....*....|....*....|....*....|...
gi 547260874 137 DLSGGERQRVWISMLLAQASPVMILDEPTSALD 169
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
16-43 |
2.20e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 2.20e-03
10 20
....*....|....*....|....*....
gi 547260874 16 ILSIDHLEI-PTHELTLILGHNGSGKSTL 43
Cdd:pfam13476 6 FRSFRDQTIdFSKGLTLITGPNGSGKTTI 34
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
137-172 |
3.14e-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: 38.05 E-value: 3.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 547260874 137 DLSGGERQRVWIS----MLLAQASPVMILDEPTSALDVRH 172
Cdd:cd03273 166 ELSGGQRSLVALSlilaLLLFKPAPMYILDEVDAALDLSH 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
127-194 |
3.55e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 3.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547260874 127 TAHYAQSyVDDLSGGERQRVWIS-MLLAQASpVMILDEPTSALDVRHQYGTLALLERLNREtGRGVIAI 194
Cdd:PRK13549 396 TASPELA-IARLSGGNQQKAVLAkCLLLNPK-ILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
18-48 |
3.87e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.87e-03
10 20 30
....*....|....*....|....*....|....
gi 547260874 18 SIDHLEIPTHE---LTLILGHNGSGKSTLASIIS 48
Cdd:COG3950 13 GFEDLEIDFDNpprLTVLVGENGSGKTTLLEAIA 46
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
136-197 |
6.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.71 E-value: 6.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547260874 136 DDLSGGERQ------RVWISMLLAQ------ASPVMILDEPTSALDVRHQYGTLALLERLnRETGRGVIAII-HD 197
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEgiegdaPLPPLILDEPTVFLDSGHVSQLVDLVESM-RRLGVEQIVVVsHD 853
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-56 |
7.78e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.39 E-value: 7.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 547260874 1 MYELNGIRMVRNDRTILSIDHLEIPThELTLILGHNGSGKSTLASIISGLVKPDAG 56
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPS-AITYIKGANGCGKSSLLRMIAGIMQPSSG 55
|
|
| |
