|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-256 |
7.54e-140 |
|
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: 393.25 E-value: 7.54e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMDCE 242
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 521288620 243 VTKDPLFGTPHCIP 256
Cdd:COG1120 241 VIEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-255 |
1.98e-114 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 329.28 E-value: 1.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILP 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMDCEV 243
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|..
gi 521288620 244 TKDPLFGTPHCI 255
Cdd:PRK11231 242 HPEPVSGTPMCV 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-259 |
7.21e-107 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 310.38 E-value: 7.21e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP 86
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 167 TTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMDCEVTKD 246
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDD 250
|
250
....*....|...
gi 521288620 247 PLFGTPHCIPYGR 259
Cdd:PRK10253 251 PVAGTPLVVPLGR 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-258 |
8.02e-97 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 284.28 E-value: 8.02e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILP 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKQGRYPY-QNWLkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYsKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMDCE 242
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIE 238
|
250
....*....|....*.
gi 521288620 243 VTKDPlfGTPHCIPYG 258
Cdd:COG4604 239 VEEID--GKRICVYFR 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
1.93e-86 |
|
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: 255.44 E-value: 1.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 5 STETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQ 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 gpsapegltvlqlvkqgrypyqnwlkqwsaedeeavqkALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-240 |
8.05e-75 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 228.05 E-value: 8.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklPTKEVAKELA 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEG--LTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIkDKKIYAEGRPESIINCKLVQDVFE 238
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYG 236
|
..
gi 521288620 239 MD 240
Cdd:COG1121 237 GP 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-252 |
1.20e-71 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 220.81 E-value: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQLVKQG 101
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 RYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDL 181
Cdd:PRK10575 110 RYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 182 LFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMDCEVTKDPLFGTP 252
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAP 260
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-256 |
1.62e-69 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 214.98 E-value: 1.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILP 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKQGRYPYQnwlkQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ------- 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNeHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDV 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250 260
....*....|....*....|
gi 521288620 237 FEMDCEVTKDPLFGTPHCIP 256
Cdd:COG4559 237 YGADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-252 |
1.33e-65 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 205.01 E-value: 1.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQnwlkQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ------ 156
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHG----LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDV 236
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250
....*....|....*.
gi 521288620 237 FEMDCEVTKDPLFGTP 252
Cdd:PRK13548 238 YGADVLVQPHPETGAP 253
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-222 |
1.39e-65 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 203.53 E-value: 1.39e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 5 STETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtkevaKELAILPQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 GPSAPEG--LTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEkRTIVMVLHDLNLACRYAHHLVAIkDKKIYAEG 222
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-256 |
1.56e-65 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 209.70 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMD 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDAR 239
|
250
....*....|....*.
gi 521288620 241 CEVTKDPLFGTPHCIP 256
Cdd:PRK09536 240 TAVGTDPATGAPTVTP 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-227 |
2.39e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 191.42 E-value: 2.39e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK--- 77
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 78 ELAILPQGPSAPEGLTVLQLVKQGRYPY----QNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMT 153
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 154 LAQETDIILLDEPTTYLD-MTHQiEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG3638 161 LVQEPKLILADEPVASLDpKTAR-QVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
3.10e-59 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 187.92 E-value: 3.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPS----APeglTVLQLVKQGrypyqnwLKQWSAEDEEA---VQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:COG1122 81 FQNPDdqlfAP---TVEEDVAFG-------PENLGLPREEIrerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
1.29e-55 |
|
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: 178.92 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---VAKEL 79
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQLVKQGRYPY----QNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQ 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
5.31e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.18 E-value: 5.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtKEVAKELAILP 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKqgrypYQNWLKQWS-AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG1131 80 QEPALYPDLTVRENLR-----FFARLYGLPrKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINcKLVQDVF 237
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
3.91e-52 |
|
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: 169.18 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 5 STETLSLGY--GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQgpsAPE----GLTVLQLVKQGryPYQNWLKQwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:cd03225 81 FQ---NPDdqffGPTVEEEVAFG--LENLGLPE--EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKK 217
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-205 |
9.61e-52 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 167.41 E-value: 9.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegssiaklpTKEVAKELAILPQGPSAPEG 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 L--TVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 169
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 521288620 170 LDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACR 205
Cdd:NF040873 150 LDAESRERIIALLAEEHA-RGATVVVVTHDLELVRR 184
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-227 |
1.41e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 166.32 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---VAKEL 79
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQLVKQGRYPYQN----WLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
5.38e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 166.62 E-value: 5.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MS-AISTETLSLGY--GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG---GSVLLEGSSIAKLPTKE 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 75 VAKELAILPQGP-SAPEGLTVLQlvkQGRYPYQNwLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMT 153
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGD---QIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 154 LAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-227 |
3.52e-47 |
|
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: 157.33 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtKEVAKELAILP 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKqgrypYQNWLKQ-WSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG4555 81 DERGLYDRLTVRENIR-----YFAELYGlFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-218 |
4.76e-47 |
|
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: 154.86 E-value: 4.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtKEVAKELAILP 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKqgrypyqnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:cd03230 80 EEPSLYENLTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-222 |
4.88e-47 |
|
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: 156.51 E-value: 4.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 8 TLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA---KELAILPQ 84
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 GPSA---PeGLTVLQLVKQgryPYQNWLKQWSAEDEEAVQKALKatRMEELAERTVDS----LSGGQRQRAWIAMTLAQE 157
Cdd:cd03257 90 DPMSslnP-RMTIGEQIAE---PLRIHGKLSKKEARKEAVLLLL--VGVGLPEEVLNRypheLSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-231 |
7.87e-47 |
|
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: 156.29 E-value: 7.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---VAKEL 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGpsapeG-----LTVLQ-----LVKQGRYPyqnwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAW 149
Cdd:COG1127 85 GMLFQG-----GalfdsLTVFEnvafpLREHTDLS--------EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 150 IAMTLAQETDIILLDEPTTYLD--MThqIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
....
gi 521288620 228 INCK 231
Cdd:COG1127 230 LASD 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-229 |
1.02e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 163.15 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLP---TKEVAKELAILPQGPSA-- 88
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsl 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 -PEgLTVLQ-----LVKQGRYPyqnwlkqwSAEDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:COG1123 356 nPR-MTVGDiiaepLRLHGLLS--------RAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
12-218 |
2.57e-46 |
|
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: 154.57 E-value: 2.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA----KELAILPQGPS 87
Cdd:cd03255 13 GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrRHIGFVFQSFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGLTVLQLVkqgRYPyQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:cd03255 93 LLPDLTALENV---ELP-LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521288620 168 TYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLAcRYAHHLVAIKDKKI 218
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-223 |
1.60e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK----ELAILPQG-- 85
Cdd:COG1136 17 GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrrHIGFVFQFfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 --PSapegLTVLQ-----LVKQGRYPyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:COG1136 97 llPE----LTALEnvalpLLLAGVSR---------KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLAcRYAHHLVAIKDKKIYAEGR 223
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSDER 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-230 |
3.76e-45 |
|
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: 151.89 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---VAKELA 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGLTVLQLVkqgrypyQNWLKQWSAEDE----EAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENV-------AFPLREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 157 ETDIILLDEPTTYLD--MTHQIEilDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINC 230
Cdd:cd03261 154 DPELLLYDEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
1.26e-43 |
|
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: 147.97 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKeLAILP 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 --QGPSAPEGLTVLQLVK---QGRYPYQNWLKQWSAEDEEAVQKA---LKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:cd03219 80 tfQIPRLFPELTVLENVMvaaQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHeKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-218 |
1.26e-43 |
|
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: 147.28 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvaKELAILPQGPSA 88
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLV----KQGRYPyqnwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:cd03259 84 FPHLTVAENIafglKLRGVP--------KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-217 |
2.76e-43 |
|
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: 144.69 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQgpsa 88
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 pegltvlqlvkqgrypyqnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521288620 169 YLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKK 217
Cdd:cd00267 110 GLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
7.38e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.34 E-value: 7.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILP 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGlTVLQLVkqgRYPYQNWLKQWsaeDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG4619 81 QEPALWGG-TVRDNL---PFPFQLRERKF---DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
3.00e-42 |
|
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: 144.95 E-value: 3.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGE----TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE 78
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQGP--SAPEGLTVLQLVKQgryPYQNwlkQWSAEDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAE---PLRI---HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-228 |
8.61e-41 |
|
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: 140.30 E-value: 8.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYG----ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklptkEVAKEL 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQLVkqgRYPYQnwLKQWS-AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNV---ALGLE--LQGVPkAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKdkkiyaeGRPESII 228
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS-------ARPGRIV 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
1.34e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 140.94 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-L 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQ------LVKQGRYPYQNWLKQWS--AEDEEAVQKA---LKATRMEELAERTVDSLSGGQRQRA 148
Cdd:COG0411 82 ARTFQNPRLFPELTVLEnvlvaaHARLGRGLLAALLRLPRarREEREARERAeelLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 149 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIkD--KKIyAEGRPES 226
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL-DfgRVI-AEGTPAE 239
|
250
....*....|
gi 521288620 227 IINCKLVQDV 236
Cdd:COG0411 240 VRADPRVIEA 249
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
6.23e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 6.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----V 75
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvgmV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQgpsapegLTVLQLVKQGrypyqnwLKQW---SAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAM 152
Cdd:COG3842 83 FQDYALFPH-------LTVAENVAFG-------LRMRgvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 153 TLAQETDIILLDEPTTYLD------MthQIEILDLLFELNehekRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPES 226
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDaklreeM--REELRRLQRELG----ITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
.
gi 521288620 227 I 227
Cdd:COG3842 223 I 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-210 |
2.53e-39 |
|
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: 136.07 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTkEVAKELAILP 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVkqgrypyQNWLKQWSAE-DEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:COG4133 82 HADGLKPELTVRENL-------RFWAALYGLRaDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521288620 163 LDEPTTYLDmTHQIEILDLLfeLNEH--EKRTIVMVLHDLnLACRYAHHL 210
Cdd:COG4133 155 LDEPFTALD-AAGVALLAEL--IAAHlaRGGAVLLTTHQP-LELAAARVL 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-227 |
2.71e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 135.27 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYG-----ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA---KLPTKEV 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQgpsAPE----GLTVLQLVKQGryPyQNwLKQWSAEDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWI 150
Cdd:TIGR04521 81 RKKVGLVFQ---FPEhqlfEETVYKDIAFG--P-KN-LGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 151 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-215 |
3.94e-38 |
|
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: 131.93 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKL--PTKEVAKELAILPQGP 86
Cdd:cd03229 6 VSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGLTVLQLVkqgRYPyqnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:cd03229 86 ALFPHLTVLENI---ALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521288620 167 TTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKD 215
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-200 |
4.97e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 4.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGY----GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTkeva 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 kELAILPQGPSAPEGLTVLQ-----LVKQGRYPyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIA 151
Cdd:COG1116 81 -DRGVVFQEPALLPWLTVLDnvalgLELRGVPK---------AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521288620 152 MTLAQETDIILLDEPTTYLD-MThQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDaLT-RERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-227 |
7.06e-38 |
|
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: 133.07 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL-----MKPKGGSVLLEGSSIAKLPTK--EVA 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSaPEGLTVLQLVkqgRYPYQNWLKQWSAEDEEAVQKAL-KATRMEELAERT-VDSLSGGQRQRAWIAMTL 154
Cdd:cd03260 81 RRVGMVFQKPN-PFPGSIYDNV---AYGLRLHGIKLKEELDERVEEALrKAALWDEVKDRLhALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 155 AQETDIILLDEPTTYLD--MTHQIEilDLLFELNehEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:cd03260 157 ANEPEVLLLDEPTSALDpiSTAKIE--ELIAELK--KEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-229 |
1.04e-37 |
|
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: 133.54 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----------VAKELAIL 82
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkismVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQgpsapegLTVLQ-----LVKQGRYPyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQE 157
Cdd:cd03294 115 PH-------RTVLEnvafgLEVQGVPR---------AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-237 |
2.32e-37 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 133.03 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 17 IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM----KPKG----GSVLLEGSSIAKLPTKEVAKELAILPQGPSA 88
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ---------ETD 159
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVF 237
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
2.58e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.92 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQLV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 99 KQGRYPyQNWLKQWSAEDeeaVQKALKATRMEELAERTVD----SLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:pfam00005 81 RLGLLL-KGLSKREKDAR---AEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-213 |
2.66e-37 |
|
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: 134.03 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG---GSVLLEGSSIAKLPTKEV----AKELAILPQGPSA--- 88
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELrkirGREIQMIFQDPMTsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PeGLTVLQLVKQgryPYQNWLKQWSAEDEEAVQKALKATRMEElAERTVDS----LSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:COG0444 101 P-VMTVGDQIAE---PLRIHGGLSKAEARERAIELLERVGLPD-PERRLDRypheLSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHlVAI 213
Cdd:COG0444 176 EPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR-VAV 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-229 |
7.02e-37 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.25 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-LAIL 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQNwlkqwsAEDEEAVQKALKA-TRMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-229 |
7.54e-37 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 130.50 E-value: 7.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-------VAKELAILPQgpsapeg 91
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkigyVIQQIGLFPH------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQ---LVKQgrypyqnwLKQWSAED-EEAVQKALKATRME--ELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03295 90 MTVEEniaLVPK--------LLKWPKEKiRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 166 PTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-218 |
1.75e-36 |
|
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: 128.53 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 5 STETLSLGYGETI-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlptKEVAKELAILP 83
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGP-------SAPEGLTVlqlvkqgrypyqnWLKQwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:cd03226 78 QDVdyqlftdSVREELLL-------------GLKE-LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
2.38e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 127.11 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPsapegltvlqlvkqgrypyqnWLkqwsaedeeavqkaLKATRMEELaertvdsLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03228 81 VPQDP---------------------FL--------------FSGTIRENI-------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELneHEKRTIVMVLHDLNLAcRYAHHLVAIKDKK 217
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-229 |
3.80e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.57 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAkLPTKEVAK---ELA 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQG----PSapegLTVLQLVKQGrypyQNWLKQWSAEdeEAVQKA---LKATRMEELAERTVDSLSGGQRQRAWIAMT 153
Cdd:COG1126 81 MVFQQfnlfPH----LTVLENVTLA----PIKVKKMSKA--EAEERAmelLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 154 LAQETDIILLDEPTTYLD--MTHqiEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDpeLVG--EVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
4.26e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 129.47 E-value: 4.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPE-GLTVLQLVKQGryPYQNWLKQwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:PRK13647 84 VFQDPDDQVfSSTVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQ 234
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-225 |
1.77e-35 |
|
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: 126.33 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTkEVAKELAILP 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQ-LVKQGR-YPYQNwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARlYGVPG------AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPE 225
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
2.24e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----V 75
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniamV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQgpsapegLTVlqlvkqgrypYQN-----WLKQWSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAW 149
Cdd:COG3839 81 FQSYALYPH-------MTV----------YENiafplKLRKVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 150 IAMTLAQETDIILLDEPTTYLD------MthQIEILDLLFELneheKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGR 223
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveM--RAEIKRLHRRL----GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
....
gi 521288620 224 PESI 227
Cdd:COG3839 218 PEEL 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
2.33e-35 |
|
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: 132.96 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGlTVLQLVKQGRypyqnwlkqwSAEDEEAVQKALKATRMEELAERTVD-----------SLSGGQRQRAW 149
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 150 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDLNLACRYAHHLVaIKDKKIYAEGRPE 225
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQADRILV-LDDGRIVEQGTHE 556
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
24-237 |
2.38e-35 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 126.12 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 24 LTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklPTKEVAKELAILPQ----GPSAPegLTVLQLVK 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQrhefAWDFP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 100 QGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEIL 179
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 180 DLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIkDKKIYAEGRPESIINCKLVQDVF 237
Cdd:TIGR03771 154 ELFIELAG-AGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTF 209
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-240 |
2.50e-35 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 126.88 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQLVKQG 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 RYPYQNwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ-------ETDIILLDEPTTYLDMTH 174
Cdd:COG4138 94 QPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 175 QIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMD 240
Cdd:COG4138 169 QAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-246 |
1.02e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 125.20 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVL------LEGSSIAklptkEVAKELAILpqgp 86
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVW-----ELRKRIGLV---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SA------PEGLTVLQLVKQGRY----PYQnwlkQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:COG1119 84 SPalqlrfPRDETVLDVVLSGFFdsigLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDV 236
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEA 239
|
250
....*....|
gi 521288620 237 FEMDCEVTKD 246
Cdd:COG1119 240 FGLPVEVERR 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-229 |
3.60e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.33 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIidELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtkeVAKE-LAILPQg 85
Cdd:COG3840 5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAERpVSMLFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 psapEG-----LTVLQLVKQGRYPYqnwLKqWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:COG3840 79 ----ENnlfphLTVAQNIGLGLRPG---LK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-224 |
6.98e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 122.23 E-value: 6.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtKEVAKELAILPQGPSAPEG 91
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQLVKqgrypYQNWLKQWSAEDEEAVQKA-LKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:cd03263 90 LTVREHLR-----FYARLKGLPKSEIKEEVELlLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 171 DMTHQIEILDLLfeLNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRP 224
Cdd:cd03263 165 DPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
9-222 |
8.51e-34 |
|
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: 121.83 E-value: 8.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIidELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvaKELAILPQGPSA 88
Cdd:cd03298 6 IRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVKQGRYPYqnwLKqWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:cd03298 82 FAHLTVEQNVGLGLSPG---LK-LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 169 YLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
8.82e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 123.65 E-value: 8.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA--KLPTKEVAKELA 80
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPS----APeglTVLQLVKQGryPYQNWLKQwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:PRK13639 82 IVFQNPDdqlfAP---TVEEDVAFG--PLNLGLSK--EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-228 |
1.17e-33 |
|
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: 128.35 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGY--GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGP---SApeglTV---LQLVKQGrypyqnwlkqwsAEDEEAVQkALKATRMEELAERTVD-----------SLSGG 143
Cdd:COG4987 413 VVPQRPhlfDT----TLrenLRLARPD------------ATDEELWA-ALERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 144 QRQRAWIAMTLAQETDIILLDEPTTYLD-MTHQiEILDLLFELNEHekRTIVMVLHDLNLAcRYAHHLVAIKDKKIYAEG 222
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDaATEQ-ALLADLLEALAG--RTVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
....*.
gi 521288620 223 RPESII 228
Cdd:COG4987 552 THEELL 557
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-218 |
1.31e-33 |
|
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: 121.48 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSI--AKLPTKEVAKELAI 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGLTVLQLVKQGrypyQNWLKQWS-AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA----PIKVKGMSkAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 161 ILLDEPTTYLD--MTHqiEILDLLFELnEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03262 157 MLFDEPTSALDpeLVG--EVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-223 |
1.65e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.31 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 10 SLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK----------E 78
Cdd:COG2884 8 SKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrrigvvfqD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQgpsapegLTV-------LQLVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIA 151
Cdd:COG2884 88 FRLLPD-------RTVyenvalpLRVTGKSR-----------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGR 223
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGT-TVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-229 |
4.86e-33 |
|
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: 127.26 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYG--ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:COG2274 473 DIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGlTVlqlvkqgrypYQNwLKQWSAE-DEEAVQKALKATRMEELAER------TV-----DSLSGGQRQRA 148
Cdd:COG2274 553 VVLQDVFLFSG-TI----------REN-ITLGDPDaTDEEIIEAARLAGLHDFIEAlpmgydTVvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 149 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLAcRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
.
gi 521288620 229 N 229
Cdd:COG2274 698 A 698
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
8.31e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 119.70 E-value: 8.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-L 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQG----PSapegLTV---LQLvkqGRYPyqnwlkqwsAEDEEAVQKALKAT-----RMEELAERTVDSLSGGQRQR 147
Cdd:COG0410 81 GYVPEGrrifPS----LTVeenLLL---GAYA---------RRDRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 148 AWIAMTLAQETDIILLDEPTTYL--DMTHqiEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPE 225
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLapLIVE--EIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
....
gi 521288620 226 SIIN 229
Cdd:COG0410 222 ELLA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-222 |
9.18e-33 |
|
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: 119.22 E-value: 9.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGeITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKeVAKELAILP 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKqgrypYQNWLKQWSAEDEEA-VQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLH---DLNLACryaHHLVAIKDKKIYAEG 222
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHiveDVESLC---NQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-229 |
1.09e-32 |
|
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: 119.65 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKE 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQgpsapegLTVLQLVKqgrYPYQnwLKQWS-AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQE 157
Cdd:cd03300 81 YALFPH-------LTVFENIA---FGLR--LKKLPkAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 158 TDIILLDEPTTYLDMTHQieiLDLLFELNEHEKR---TIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03300 149 PKVLLLDEPLGALDLKLR---KDMQLELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-222 |
2.81e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMK--PKG---GSVLLEGSSIAKLPTKEV 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQGPSAPEGLTVLQLVKQGryPYQNWLKQWSAEDEEAVQKAL-KATRMEELAER---TVDSLSGGQRQRAWIA 151
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALeKAQLWDEVKDRldaPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-227 |
4.16e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGET--IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAP-EGLTVLQLVKQGrypYQNwlkQWSAEDE--EAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK13635 86 VFQNPDNQfVGATVQDDVAFG---LEN---IGVPREEmvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-205 |
8.61e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.83 E-value: 8.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--------MKpkgGSVLLEGSSI--AKLP 71
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgarVE---GEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 72 TKEVAKELAILPQGP-----SAPE----GLTVlqlvkQGRYPyqnwlkqwSAEDEEAVQKALKATRM-EELAERTVDS-- 139
Cdd:COG1117 87 VVELRRRVGMVFQKPnpfpkSIYDnvayGLRL-----HGIKS--------KSELDEIVEESLRKAALwDEVKDRLKKSal 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 140 -LSGGQRQRAWIAMTLAQETDIILLDEPTTYLD--MTHQIEilDLLFELNehEKRTIVMVLHDLNLACR 205
Cdd:COG1117 154 gLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILELK--KDYTIVIVTHNMQQAAR 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-229 |
2.76e-31 |
|
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: 115.76 E-value: 2.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 6 TETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEV---AKELAIL 82
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKqgrYPYQNWlKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:cd03258 88 FQHFNLLSSRTVFENVA---LPLEIA-GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-214 |
5.93e-31 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 116.14 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGY--GETIIIDElNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegsSIAKLPTKEVAKE- 78
Cdd:PRK15056 5 AGIVVNDVTVTWrnGHTALRDA-SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 -LAILPQGPSAPEGLTVL--QLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK15056 79 lVAYVPQSEEVDWSFPVLveDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIK 214
Cdd:PRK15056 159 QQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-218 |
6.20e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 114.27 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKELAILPQgps 87
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamVFQNYALYPH--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 apegLTV-------LQLVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:cd03301 87 ----MTVydniafgLKLRKVPK-----------DEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
7.57e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 7.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGYG--ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKEL 79
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGP-SAPEGLTVLQLVKQG----RYPYQnwlKQWSAEDEEAvqkalKATRMEELAERTVDSLSGGQRQRAWIAMTL 154
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAFGlenkKVPPK---KMKDIIDDLA-----KKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESIINCK 231
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-227 |
1.86e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.86 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKELAILPQgpsapegLT 93
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPH-------MT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQLV----KQGRYPyqnwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 169
Cdd:PRK11607 108 VEQNIafglKQDKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 170 LDMT----HQIEILDLLfelnEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK11607 180 LDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-230 |
2.28e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPsapEGLTV 94
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNP---DNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVKqgrYPYQNWLKQWSAEDEEA---VQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK13648 98 GSIVK---YDVAFGLENHAVPYDEMhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 172 MTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESIINC 230
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
4.67e-30 |
|
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: 117.85 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSApEGLTVLQLVKQGRyPyqnwlkqwSAEDEEaVQKALKATRMEELAERTVD-----------SLSGGQRQRAWIA 151
Cdd:TIGR02868 415 AQDAHL-FDTTVRENLRLAR-P--------DATDEE-LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDL 200
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
15-220 |
1.23e-29 |
|
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: 111.29 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK----ELAILPQ------ 84
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQfhhllp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 GPSAPEGLTVLQLVKqgrypyqnwlKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:TIGR02211 97 DFTALENVAMPLLIG----------KKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVaIKDKKIYA 220
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLE-MKDGQLFN 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-205 |
2.20e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 111.41 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--MKPK---GGSVLLEGSSI--AKLPTKEVA 76
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSaPEGLTVLQLVKQG-RYpyqNWLKQWSAEDEeAVQKALK-ATRMEELAERTVDS---LSGGQRQRAWIA 151
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGlRL---KGIKDKQVLDE-AVEKSLKgASIWDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACR 205
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLK--DDYTMLLVTRSMQQASR 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
4.58e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.65 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA------KLptKEVAKELAILPQGPSA 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKL--KPLRKKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 ---PEglTVLQLVKQGryPyQNWlkqwSAEDEEAVQKALKATRM----EELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK13634 97 qlfEE--TVEKDICFG--P-MNF----GVSEEDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
9.33e-29 |
|
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: 114.31 E-value: 9.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGlTVLQLVKQGRyPYQnwlkqwsaeDEEAVQKALKATRMEELA-------ERTVDS----LSGGQRQRAW 149
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLAR-PDA---------SDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 150 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRyAHHLVAI 213
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.21e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.55 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG-----GSVLLEGSSI--AKLPTK 73
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 74 EVAKELAILPQGPSAPEGLTVLQLVKQGRYpyQNWLKQWSAEDEEAVQKALK-ATRMEELAERTVD---SLSGGQRQRAW 149
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVK--LNGLVKSKKELDERVEWALKkAALWDEVKDRLNDypsNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 150 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELK--KEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
2.49e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYG----ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaklptkeva 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 kelailpQGPSAPEGLtVLQlvKQGRYPYQNWL----------KQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQ 146
Cdd:COG4525 72 -------TGPGADRGV-VFQ--KDALLPWLNVLdnvafglrlrGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 147 RAWIAMTLAQETDIILLDEPTTYLD-MTHQiEILDLLFELNEHEKRTIVMVLHD 199
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDaLTRE-QMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-227 |
2.59e-28 |
|
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: 108.20 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvaKELAIL 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-222 |
2.61e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 106.63 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE--TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLpTKEVAKELAI 81
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPsapegltvlqlvkqgrYPYQnwlkqwsaedeeavqkalkATRMEELAERtvdsLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03247 80 LNQRP----------------YLFD-------------------TTLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFElnEHEKRTIVMVLHDLnLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-229 |
2.65e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---------VAKELAILP 83
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeagmVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QgpsapegLTVLQLVKQGryPYQnwLKQWSAEDEEAVQKALKA-TRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:PRK09493 91 H-------LTALENVMFG--PLR--VRGASKEEAEKQARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-227 |
3.28e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.24 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSaISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSI-AKLPTKE----- 74
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRErrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 75 ------------VAKELAIlpqgpsapeGLTVLQLVKqgrypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSG 142
Cdd:COG1118 80 vfqhyalfphmtVAENIAF---------GLRVRPPSK--------------AEIRARVEELLELVQLEGLADRYPSQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDmTH---QIEilDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIY 219
Cdd:COG1118 137 GQRQRVALARALAVEPEVLLLDEPFGALD-AKvrkELR--RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
....*...
gi 521288620 220 AEGRPESI 227
Cdd:COG1118 214 QVGTPDEV 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-219 |
3.65e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegsSIAKlptkevAKELAILPQGPSA 88
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPK------GLRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVKQGRYPYQNWLKQW-------SAEDEEAVQKALKATRMEEL----------------------AERTVDS 139
Cdd:COG0488 73 DDDLTVLDTVLDGDAELRALEAELeeleaklAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpeedLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 140 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLLfE--LNEHEKrTIVMVLHDlnlacRY-----AHHLVA 212
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWL-EefLKNYPG-TVLVVSHD-----RYfldrvATRILE 221
|
....*..
gi 521288620 213 IKDKKIY 219
Cdd:COG0488 222 LDRGKLT 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-222 |
5.73e-28 |
|
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: 106.68 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPtKEVAKELAILPQGPSAPEGLTVLQLV 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 kqGRYPYQNWLKQwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEI 178
Cdd:cd03266 100 --EYFAGLYGLKG--DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 179 LDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03266 176 REFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-229 |
1.01e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.12 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA----KE 78
Cdd:PRK10070 28 GLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQGPSAPEGLTVLQLVKQGrypyQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK10070 184 DILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-229 |
1.93e-27 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 105.88 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGEtIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvaKELAILPQGP 86
Cdd:cd03299 4 ENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGLTV-------LQLVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETD 159
Cdd:cd03299 81 ALFPHMTVykniaygLKKRKVDK-----------KEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.81e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKEL 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPS----APeglTVLQLVKQGryPYQNWLkqwsaeDEEA----VQKALKATRMEELAERTVDSLSGGQRQRAWIA 151
Cdd:PRK13652 81 GLVFQNPDdqifSP---TVEQDIAFG--PINLGL------DEETvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-225 |
7.88e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.10 E-value: 7.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPS 87
Cdd:COG1132 345 VSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 apegL---TVLQLVKQGRypyqnwlkqWSAEDEEaVQKALKATRMEELAER------TV-----DSLSGGQRQRAWIAMT 153
Cdd:COG1132 425 ----LfsgTIRENIRYGR---------PDATDEE-VEEAAKAAQAHEFIEAlpdgydTVvgergVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 154 LAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPE 225
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHE 559
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-229 |
1.09e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 104.71 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM---KPKGGSVLLEGSSI------AKLPT 72
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 73 KEVAKELAILPQGpSAPEGLTVLQLV---KQGRYPYQNWLKQWSAEDEEavQKALKA-TR--MEELAERTVDSLSGGQRQ 146
Cdd:PRK09984 83 KSRANTGYIFQQF-NLVNRLSVLENVligALGSTPFWRTCFSWFTREQK--QRALQAlTRvgMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 147 RAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPES 226
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
...
gi 521288620 227 IIN 229
Cdd:PRK09984 240 FDN 242
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-207 |
1.46e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.09 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--MKPKG---GSVLLEGSSI--AKLPTKEVA 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSaPEGLTVLQLVKQGryPYQNWLKqwsAEDEEAVQKALK-ATRMEELAERTVDS---LSGGQRQRAWIAM 152
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYG--ARINGYK---GDMDELVERSLRqAALWDEVKDKLKQSglsLSGGQQQRLCIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 153 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRYA 207
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVS 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-218 |
1.61e-26 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.02 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvaKELAILPQGPSAPEGLTVLQLVKQ 100
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 101 GRYPYqnwLKqWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILD 180
Cdd:TIGR01277 94 GLHPG---LK-LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 521288620 181 LLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-222 |
1.62e-26 |
|
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: 102.74 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaklpTKEVAKELAILP 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVL-QLVKQGRypyqnwLKQWSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03269 77 EERGLYPKMKVIdQLVYLAQ------LKGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-227 |
2.75e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.60 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-VAKELAILPQG 85
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHErARAGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSAPEGLTV---LQLVKQGRypyqnwlKQWSAE-DEEAVQ--KALKatrmeELAERTVDSLSGGQRQRAWIAMTLAQETD 159
Cdd:TIGR03410 84 REIFPRLTVeenLLTGLAAL-------PRRSRKiPDEIYElfPVLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-227 |
4.73e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSI--AKLPTKEVAKELA 80
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGP-----SApeglTVLQLVKQGRYPyqnwLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK13636 86 MVFQDPdnqlfSA----SVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-227 |
5.97e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaklpTKEVAKELAILpqgpsaPE-- 90
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYL------PEer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GL----TVL-QLVKQGRypyqnwLKQWSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:COG4152 81 GLypkmKVGeQLVYLAR------LKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
6.52e-26 |
|
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: 101.14 E-value: 6.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLptKEVAKELAILP 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGP------SAPEGLTVLQLVKQGRYpyqnwlkqwsaedeEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQE 157
Cdd:cd03268 79 EAPgfypnlTARENLRLLARLLGIRK--------------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-239 |
7.58e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 7.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlPTKEVAKELAI 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGLTVLQ-LVKQGRYpyqnwLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:PRK13537 85 VPQFDNLDPDFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEM 239
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
7.76e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 7.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLeGSSIaklptkevakELAILP 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSA-PEGLTVLQlvkqgrypyqnWLKQWSAEDEEAVQKALkATRM---EELAERTVDSLSGGQRQRAWIAMTLAQETD 159
Cdd:COG0488 385 QHQEElDPDKTVLD-----------ELRDGAPGGTEQEVRGY-LGRFlfsGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 160 IILLDEPTTYLDmthqIEILDLLFE-LNEHEKrTIVMVLHDlnlacRY-----AHHLVAIKDKKI 218
Cdd:COG0488 453 VLLLDEPTNHLD----IETLEALEEaLDDFPG-TVLLVSHD-----RYfldrvATRILEFEDGGV 507
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-229 |
8.65e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 101.54 E-value: 8.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYG-ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGpsapeglTVL------QLVKQGRypyqnwlkqWSAEDEEAVQKALKA------TRMEE-----LAERTVdSLSGGQR 145
Cdd:cd03253 81 PQD-------TVLfndtigYNIRYGR---------PDATDEEVIEAAKAAqihdkiMRFPDgydtiVGERGL-KLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 146 QRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPE 225
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHE 220
|
....
gi 521288620 226 SIIN 229
Cdd:cd03253 221 ELLA 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-240 |
9.59e-26 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 101.55 E-value: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQLVKQG 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 RYPYQNwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ-------ETDIILLDEPTTYLDMTH 174
Cdd:PRK03695 94 QPDKTR-----TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 175 QIeILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVFEMD 240
Cdd:PRK03695 169 QA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-211 |
1.36e-25 |
|
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: 101.33 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 25 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKevakelaILPQGPSAPEGLTVLQLVKQGRYP 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 105 YqnwlkqWSAEdeeaVQKALKatrMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFE 184
Cdd:cd03237 94 Y------FKTE----IAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*..
gi 521288620 185 LNEHEKRTIVMVLHDLNLACRYAHHLV 211
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-227 |
1.63e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKE 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQgpsapegLTVLQLVKQGrypyqnwL---KQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK09452 95 YALFPH-------MTVFENVAFG-------LrmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 156 QETDIILLDEPTTYLD------MthQIEILDLLFELNehekRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrkqM--QNELKALQRKLG----ITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-201 |
1.90e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK---GGSVLLEGSSIAKLPTKevAKELAILP 83
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQ-----LVKQ-GRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQE 157
Cdd:COG4136 83 QDDLLFPHLSVGEnlafaLPPTiGR-----------AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLN 201
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-229 |
2.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSaISTETLSLGYG-----ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA--KLPTK 73
Cdd:PRK13637 1 MS-IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 74 EVAKELAILPQGPSapegltvLQLVKQGRY------PyqnwlKQWSAEDEEAVQKALKATRM-----EELAERTVDSLSG 142
Cdd:PRK13637 80 DIRKKVGLVFQYPE-------YQLFEETIEkdiafgP-----INLGLSEEEIENRVKRAMNIvgldyEDYKDKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
....*..
gi 521288620 223 RPESIIN 229
Cdd:PRK13637 228 TPREVFK 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-222 |
2.28e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 99.97 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP-----SAP 89
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVtlfygTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 EGLTVlqlvkqgRYPYqnwlkqwsAEDEEaVQKALKATRMEELA-------ERTV----DSLSGGQRQRAWIAMTLAQET 158
Cdd:cd03245 96 DNITL-------GAPL--------ADDER-ILRAAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHD---LNLACRyahhLVAIKDKKIYAEG 222
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRpslLDLVDR----IIVMDSGRIVADG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-224 |
3.23e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.80 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----V 75
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQgpsapegLTVLQLVKQGrypyqnwLKQWSAEDEEAVQKALKATRMEELA---ERTVDSLSGGQRQRAWIAM 152
Cdd:PRK11000 81 FQSYALYPH-------LSVAENMSFG-------LKLAGAKKEEINQRVNQVAEVLQLAhllDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 153 TLAQETDIILLDEPTTYLD----MTHQIEILDLLFELneheKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRP 224
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRL----GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-229 |
8.13e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 8.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 23 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG-----SSIAKLPTKEVAKELAILPQgpsapegLTVLQL 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhttTPPSRRPVSMLFQENNLFSH-------LTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 VKQGRYPyqnWLKqWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 177
Cdd:PRK10771 92 IGLGLNP---GLK-LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521288620 178 ILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-237 |
1.19e-24 |
|
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: 98.38 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKeLAI-- 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-LGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGLTVLQ---LVKQGRYPYqnwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:cd03218 80 LPQEASIFRKLTVEEnilAVLEIRGLS-------KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEhekRTIVMVLHDLNlacryAHHLVAIKDK-------KIYAEGRPESIINCK 231
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKD---RGIGVLITDHN-----VRETLSITDRayiiyegKVLAEGTPEEIAANE 224
|
....*.
gi 521288620 232 LVQDVF 237
Cdd:cd03218 225 LVRKVY 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-227 |
1.21e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.46 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKG-----GSVLLEGSSIAKLPTKEVAK----ELAIL 82
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPaahpsGSILFDGQDLLGLSERELRRirgnRIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPsapegLTVL--------QL-----VKQGrypyqnwlkqwsAEDEEAVQKA---LKATRMEElAERTVDS----LSG 142
Cdd:COG4172 98 FQEP-----MTSLnplhtigkQIaevlrLHRG------------LSGAAARARAlelLERVGIPD-PERRLDAyphqLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQG 239
|
....*
gi 521288620 223 RPESI 227
Cdd:COG4172 240 PTAEL 244
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-221 |
1.28e-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: 99.11 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKL---PTKEVAKELAILPQ-GPSA--PEg 91
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQdSPSAvnPR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQLVKQgryPYQNWLKQWSAEDEEAVQKALKATRME-ELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:TIGR02769 105 MTVRQIIGE---PLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521288620 171 DMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAE 221
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-229 |
1.41e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.78 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSV--LLEGSSIAKLP-TKEVAKELAILpQGPSAPEGLTVL 95
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTkEKEKVLEKLVI-QKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVKQGRYPYQ----NWLKQWSAED------------EEAVQKALKATRM----EELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK13651 102 EIRRRVGVVFQfaeyQLFEQTIEKDiifgpvsmgvskEEAKKRAAKYIELvgldESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
1.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 2 SAISTETLSLGYGET--IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGS---VLLEGSSIAKLPTKEVA 76
Cdd:PRK13640 4 NIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSAP-EGLTVLQLVKQG----RYPYQNWLKqwsaedeeAVQKALKATRMEELAERTVDSLSGGQRQRAWIA 151
Cdd:PRK13640 84 EKVGIVFQNPDNQfVGATVGDDVAFGlenrAVPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLAcRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-218 |
2.12e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSvLLEGS---SIAKLPTKEVAKELAILPQGpsap 89
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplAEAREDTRLMFQDARLLPWK---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 eglTVLQLVKQGrypyqnwLK-QWsaedEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:PRK11247 97 ---KVIDNVGLG-------LKgQW----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521288620 169 YLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-228 |
2.51e-24 |
|
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: 97.30 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGET-IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:cd03254 3 IEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGlTVLQLVKQGRYpyqnwlkqwSAEDEEaVQKALKATRMEELAER------TV-----DSLSGGQRQRAWIA 151
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRP---------NATDEE-VIEAAKEAGAHDFIMKlpngydTVlgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-224 |
4.55e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.84 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGY---------GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLp 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 72 TKEVAKEL-----AILPQGPSA--PEGlTVLQLVkqgRYPYQNWLKQWSAEDEEAVQKALKATRM-EELAERTVDSLSGG 143
Cdd:PRK10419 80 NRAQRKAFrrdiqMVFQDSISAvnPRK-TVREII---REPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 144 QRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIyAEGR 223
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI-VETQ 234
|
.
gi 521288620 224 P 224
Cdd:PRK10419 235 P 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-228 |
5.77e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 96.84 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTV 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVKQGRYPyqnwlkqwsAEDEEAVQKALKATRME-----------ELAERTVdSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:cd03249 94 AENIRYGKPD---------ATDEEVEEAAKKANIHDfimslpdgydtLVGERGS-QLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELneHEKRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-222 |
9.56e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 9.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegssiaklptkEVAKELAIL 82
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-------------NIAGNHFDF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQNW-------------LKQWSAEDEEAVQKA---LKATRMEELAERTVDSLSGGQRQ 146
Cdd:PRK11124 69 SKTPSDKAIRELRRNVGMVFQQYNLWphltvqqnlieapCRVLGLSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 147 RAWIAMTLAQETDIILLDEPTTYLD--MTHQieILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-227 |
9.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 9.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLP-TKEVAKELAILPQGPS------ 87
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPDnqivat 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 --------APEGLTVLQLvkqgrypyqnwlkqwsaEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETD 159
Cdd:PRK13633 102 iveedvafGPENLGIPPE-----------------EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-229 |
1.13e-23 |
|
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: 99.76 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEiTVFI-GSNGCGKSTLLRSLARLMkPKGGSVLLEGSSIAKLPTKE---VAKELAILPQGPSA---P--- 89
Cdd:COG4172 303 DGVSLTLRRGE-TLGLvGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFGslsPrmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 ------EGLTVLQLvkqgrypyqnwlkQWSAED-EEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:COG4172 381 vgqiiaEGLRVHGP-------------GLSAAErRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLAcRY-AHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVV-RAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-237 |
1.16e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.84 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA---KELAILPQGPSAPE 90
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GLTVLQLVkqgRYPyqnwLKQWSaedeeaVQKALKATRMEELAERtV----------DSLSGGQRQRAWIAMTLAQETDI 160
Cdd:COG1135 96 SRTVAENV---ALP----LEIAG------VPKAEIRKRVAELLEL-VglsdkadaypSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 161 ILLDEPTTYLD--MTHQieILDLLFELNEHEKRTIVMVLHDLNLACRYAHHlVAIKDK-KIYAEGRpesiincklVQDVF 237
Cdd:COG1135 162 LLCDEATSALDpeTTRS--ILDLLKDINRELGLTIVLITHEMDVVRRICDR-VAVLENgRIVEQGP---------VLDVF 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-218 |
1.60e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.92 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGE-ITVfIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPS---APe 90
Cdd:COG1101 18 EKRALDGLNLTIEEGDfVTV-IGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMmgtAP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GLTVLQ-----LVKQGRYPyqnwLKqwsaedeeavqKALKATRMEELAERT--------------VDSLSGGQRQrawiA 151
Cdd:COG1101 96 SMTIEEnlalaYRRGKRRG----LR-----------RGLTKKRRELFRELLatlglglenrldtkVGLLSGGQRQ----A 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 152 MTLAQET----DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:COG1101 157 LSLLMATltkpKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-229 |
1.61e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE-TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG---SSIAKLPtkEVAKEL 79
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQ--GIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAP-EGLTVLQLVKQGryPYQNWLKqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK13644 80 GIVFQNPETQfVGRTVEEDLAFG--PENLCLP--PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELneHEK-RTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKL--HEKgKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-227 |
2.40e-23 |
|
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: 96.79 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 35 IGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKELAILPQgpsapegLTVLQLVKQGrypyqnwL 109
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhinmVFQSYALFPH-------MTVEENVAFG-------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 110 KQW---SAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT----HQIEILDLL 182
Cdd:TIGR01187 68 KMRkvpRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521288620 183 FELNehekRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:TIGR01187 148 EQLG----ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-228 |
2.54e-23 |
|
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: 94.99 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGlTVLQLVKQGRypyqnwlkqwSAEDEEAVQKALKA-------TRMEE-----LAERTVdSLSGGQRQRAW 149
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGR----------PGATREEVEEAARAanahefiMELPEgydtvIGERGV-KLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 150 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-227 |
2.61e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.60 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTK---EVAKELAILPQG 85
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSAPEGLTVLQLVKqgrYPyqnwLKQWSAEDEE----AVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK11831 93 GALFTDMNVFDNVA---YP----LREHTQLPAPllhsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-211 |
2.99e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaklptkevakelailpQGP 86
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----------------EGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGLtVLQlvKQGRYPYQNWLKQWS----------AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:PRK11248 69 GAERGV-VFQ--NEGLLPWRNVQDNVAfglqlagvekMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLV 211
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-210 |
3.24e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.50 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 16 TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK----ELAILPQGPSAPEG 91
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQ-----LVKQGRYPyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:PRK11629 102 FTALEnvampLLIGKKKP---------AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 167 TTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHL 210
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-227 |
4.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPT----KEVAKELAILPQGPSAP- 89
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPEAQl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 -EGlTVLQLVKQGryPyqnwlKQWSAEDEEAVQKALKATRM----EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:PRK13641 99 fEN-TVLKDVEFG--P-----KNFGFSEDEAKEKALKWLKKvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 165 EPTTYLDMTHQIEILDlLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-227 |
7.71e-23 |
|
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: 95.95 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG----SSIAKLPTKEVAKELAILPQGPSAPEGLTVLQ 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRypyqnwlkqWSAEDEEAVQKALKATRM---EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 173
Cdd:TIGR02142 95 NLRYGM---------KRARPSERRISFERVIELlgiGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 174 HQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-227 |
8.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPT----KEVAKELAILPQGP-SAPEGLTVL 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPeSQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVKQGryPyQNWlkqwSAEDEEAVQKALKATRM----EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK13649 105 KDVAFG--P-QNF----GVSQEEAEALAREKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 172 MTHQIEILDLLFELneHEK-RTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13649 178 PKGRKELMTLFKKL--HQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-229 |
9.53e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.88 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-------------VAKEL 79
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQLVKQGryPYQnWLKQWSAEDEEAVQKALKATRMEELAERTVDS-LSGGQRQRAWIAMTLAQET 158
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEA--PIQ-VLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-222 |
1.14e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.15 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSaISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklptkevakela 80
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 iLPQGPSAPEGLTVLQLVKQGRYPYQNW----------------LKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQ 144
Cdd:COG4161 68 -FSQKPSEKAIRLLRQKVGMVFQQYNLWphltvmenlieapckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 145 RQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGI-TQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-229 |
1.26e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.52 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA-KELAILPQGPS 87
Cdd:PRK11300 11 LMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArMGVVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGLTVLQ--LVKQGRYPYQNWL------KQWSAEDEEAVQKA---LKATRMEELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:PRK11300 91 LFREMTVIEnlLVAQHQQLKTGLFsgllktPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-227 |
1.55e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.15 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSaISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE------ 74
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 75 -----------VAKELAIlpqgpsapeGLTVLQlvkqgRYPYQNwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGG 143
Cdd:PRK10851 80 fqhyalfrhmtVFDNIAF---------GLTVLP-----RRERPN-----AAAIKAKVTQLLEMVQLAHLADRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 144 QRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGR 223
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 521288620 224 PESI 227
Cdd:PRK10851 221 PDQV 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-225 |
1.83e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.79 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VAKELAILPQ--- 84
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPHmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 GPSAPEGLTVLQLVKqgrypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:PRK11432 96 GENVGYGLKMLGVPK--------------EERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPE 225
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-201 |
2.66e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.03 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA---KELAILPQGPSA---PEgLT 93
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYAslnPR-MT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQ-----LVKQGRYPyqnwlkqwSAEDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:COG4608 114 VGDiiaepLRIHGLAS--------KAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
170 180 190
....*....|....*....|....*....|....
gi 521288620 168 TYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLN 201
Cdd:COG4608 186 SALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-228 |
3.28e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 95.70 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVLQLV 98
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYG-TLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 KQGRyPYqnwlkqwsAEDEEaVQKALKATRMEELAERTVD-----------SLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:TIGR03375 560 ALGA-PY--------ADDEE-ILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 168 TYLDMTHQIEILDLLFELNEHekRTIVMVLHD---LNLACRyahhLVAIKDKKIYAEGRPESII 228
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRWLAG--KTLVLVTHRtslLDLVDR----IIVMDNGRIVADGPKDQVL 687
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-229 |
3.34e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 8 TLSLGYGETIIiDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPS 87
Cdd:TIGR01193 480 SYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGlTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRM---EELAERTvDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:TIGR01193 559 IFSG-SILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqTELSEEG-SSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEhekRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-200 |
3.35e-22 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 92.43 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 24 LTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPKGGS---------VLLE--GSSIAKLPTKEVAKEL--AILPQG---- 85
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILDEfrGSELQNYFTKLLEGDVkvIVKPQYvdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSAPEGlTVLQLVKQgrypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03236 100 PKAVKG-KVGELLKK-------------KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*
gi 521288620 166 PTTYLDMTHQIEILDLLFELNEHEKRTIVmVLHDL 200
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDL 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-205 |
3.57e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 91.73 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 8 TLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA------- 80
Cdd:COG4181 17 TVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRArhvgfvf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ----ILPqgpsapeGLTVLQLVK-----QGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIA 151
Cdd:COG4181 97 qsfqLLP-------TLTALENVMlplelAGR-----------RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 152 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACR 205
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-200 |
5.04e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 93.25 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG---GSVLLEGSSIAKLPTKEV----AKELAILPQGP 86
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELnklrAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAP--------EGLT-VLQLVKqGRYPYQNWlkqwsaedEEAVqKALKATRMEELAERTV---DSLSGGQRQRAWIAMTL 154
Cdd:PRK09473 107 MTSlnpymrvgEQLMeVLMLHK-GMSKAEAF--------EESV-RMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-218 |
5.34e-22 |
|
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: 90.93 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK---ELAILPQGPSAPE 90
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GLTV-----LQLVKQGRyPYQNWLKQwsaedeeaVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03292 92 DRNVyenvaFALEVTGV-PPREIRKR--------VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521288620 166 PTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-211 |
8.35e-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: 90.60 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlPTKE---VAKELAILPQgPSAPE--GLT 93
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDrmvVFQNYSLLPW-LTVREniALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQLVKQGRYPyqnwlkqwsaEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 173
Cdd:TIGR01184 79 VDRVLPDLSKS----------ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 521288620 174 HQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLV 211
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVV 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-201 |
1.59e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSApEGLT 93
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL-FGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQLVKqgrYPYQnwLKQwSAEDEEAVQKALKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 172
Cdd:PRK10247 97 VYDNLI---FPWQ--IRN-QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*....
gi 521288620 173 THQIEILDLLFELNEHEKRTIVMVLHDLN 201
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-229 |
2.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSI-AKLPTKE---VAKELAILPQGPSAP--EGl 92
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYirpVRKRIGMVFQFPESQlfED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVKQGryPyqnwlKQWSAEDEEAVQKALKATrMEELAERTVDSLS-----GGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:PRK13646 102 TVEREIIFG--P-----KNFKMNLDEVKNYAHRLL-MDLGFSRDVMSQSpfqmsGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 168 TYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-198 |
2.40e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 89.25 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 17 IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG---GSVLLEGSSIAKlptKEVAKELAILPQGPSAPEGLT 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 V---LQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRmeeLAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:cd03234 98 VretLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTR---IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*...
gi 521288620 171 DMTHQIEILDLLFELnEHEKRTIVMVLH 198
Cdd:cd03234 175 DSFTALNLVSTLSQL-ARRNRIVILTIH 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-239 |
2.83e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiAKLPTKEVA--KE 78
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARLarAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQGPSAPEGLTVLQ-LVKQGRYpyqnwLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQE 157
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKLVQDVF 237
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVI 269
|
..
gi 521288620 238 EM 239
Cdd:PRK13536 270 EI 271
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-227 |
3.00e-21 |
|
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: 88.89 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPkGEITVFIGSNGCGKSTLLRSLARLMKPKGG------SVLLEGSSIAKLPTKE-----VAKELAILPQgpsap 89
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQrkiglVFQQYALFPH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 egLTVLQLVKQGrypyqnwLKQWS-AEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:cd03297 90 --LNVRENLAFG-------LKRKRnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 169 YLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDkkiyaeGRPESI 227
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED------GRLQYI 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-237 |
3.82e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.93 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-L 79
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTV-------LQLVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAM 152
Cdd:COG1137 81 GYLPQEASIFRKLTVednilavLELRKLSK-----------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 153 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEhekRTIVMVLHDLN----LA-CRYAHhlvAIKDKKIYAEGRPESI 227
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE---RGIGVLITDHNvretLGiCDRAY---IISEGKVLAEGTPEEI 223
|
250
....*....|
gi 521288620 228 INCKLVQDVF 237
Cdd:COG1137 224 LNNPLVRKVY 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-200 |
4.84e-21 |
|
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: 88.93 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP------ 86
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGLTVLQLVkqgrypYQnwlkqwsAEDEEAVQKALKATRM---EELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:cd03267 111 PVIDSFYLLAAI------YD-------LPPARFKKRLDELSELldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-227 |
7.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 7.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSV----LLEGSSIAKLPTKEVAKELAILPQGPSAPegLTVLQ 96
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVGVVFQFPESQ--LFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQI 176
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521288620 177 EILDlLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13643 182 EMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
1.03e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 85.58 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLeGSSIaklptkevakELAILP 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTV----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QgpsapegltvlqlvkqgrypyqnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 164 DEPTTYLDMTHQIEILDLLfelnEHEKRTIVMVLHDLNLACRYAHHLVAIKDKK 217
Cdd:cd03221 95 DEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-230 |
2.71e-20 |
|
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: 90.46 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaKLPTKEVAKELAILPQGPSAPEGLTVLQLV 98
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 KqgrypYQNWLKQWSAEDEEAVQKA-LKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 177
Cdd:TIGR01257 1025 L-----FYAQLKGRSWEEAQLEMEAmLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521288620 178 ILDLLfeLNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINC 230
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-227 |
2.98e-20 |
|
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: 88.62 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK------GGSVLLEGSSIAKLPTkevakE---LAILPQGPSAPEG 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlGGEVLQDSARGIFLPP-----HrrrIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQLVkqgRYPYQNWLKQWSAEDEEAVQKALKatrMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:COG4148 92 LSVRGNL---LYGRKRAPRAERRISFDEVVELLG---IGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 172 MTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-237 |
3.05e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.32 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK---------------------- 77
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrqigmifqhfnllssrtvfd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 78 ------ELAILPQGPSAPEGLTVLQLV----KQGRYPYQnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQR 147
Cdd:PRK11153 102 nvalplELAGTPKAEIKARVTELLELVglsdKADRYPAQ---------------------------------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 148 AWIAMTLAQETDIILLDEPTTYLD--MTHQieILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRpe 225
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDpaTTRS--ILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT-- 224
|
250
....*....|..
gi 521288620 226 siincklVQDVF 237
Cdd:PRK11153 225 -------VSEVF 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
3.56e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.73 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIaklptkEVAKELa 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI------DTARSL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ilpqgpSAPEGLtVLQLVKQGRYPYQNW------------------LKQWSAEDEEAVQKALKA----TRMEELAERtvd 138
Cdd:PRK11264 74 ------SQQKGL-IRQLRQHVGFVFQNFnlfphrtvleniiegpviVKGEPKEEATARARELLAkvglAGKETSYPR--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 139 SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
....
gi 521288620 219 YAEG 222
Cdd:PRK11264 223 VEQG 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-218 |
3.63e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 89.57 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSV-LLEGSSIAKLPtKEVAKELAi 81
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYA-QDHAYDFE- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 lpqgpsapEGLTVLqlvkqgrypyqNWLKQWSAE--DEEAVQKALKatRM---EELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:PRK15064 397 --------NDLTLF-----------DWMSQWRQEgdDEQAVRGTLG--RLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 157 ETDIILLDEPTTYLDMtHQIEILDLLFELNEHekrTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:PRK15064 456 KPNVLVMDEPTNHMDM-ESIESLNMALEKYEG---TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-218 |
3.88e-20 |
|
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: 84.40 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvAKELAIlpqgpsapegl 92
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 tvlqlvkqgrypyqnwlkqwsaedeeavqkalkatrmeelaeRTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDm 172
Cdd:cd03216 78 ------------------------------------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAALT- 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521288620 173 THQIEIL-DLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03216 115 PAEVERLfKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-198 |
3.98e-20 |
|
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: 84.96 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGET--IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQgpsapegltvlqlvkqgrypyqnwlkqwsaEDEeavqkALKATRMEELaertvdsLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03246 81 LPQ------------------------------DDE-----LFSGSIAENI-------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLH 198
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAH 154
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-201 |
4.82e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.92 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvAKEL--AILPQGPS-APEgLTVLQ 96
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiAIIHQELNlVPN-LSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRYPYQNWLKQWSAEDEEAvQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmTHQI 176
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-EREV 176
|
170 180
....*....|....*....|....*.
gi 521288620 177 EIL-DLLFELNEhEKRTIVMVLHDLN 201
Cdd:COG1129 177 ERLfRIIRRLKA-QGVAIIYISHRLD 201
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-237 |
9.49e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.52 E-value: 9.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKStlLRSLARL-MKPKG-----GSVLLEGSSIAklPTKEVAKELAILPQGP-SAPE 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgILPAGvrqtaGRVLLDGKPVA--PCALRGRKIATIMQNPrSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GL---------TVLQLVKQGrypyqnwlkqwsaeDEEAVQKALKATRMEElAERTVDS----LSGGQRQRAWIAMTLAQE 157
Cdd:PRK10418 94 PLhtmhthareTCLALGKPA--------------DDATLTAALEAVGLEN-AARVLKLypfeMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHlVAIKDkkiyaEGRpesIINCKLVQDVF 237
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADD-VAVMS-----HGR---IVEQGDVETLF 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-230 |
1.26e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.72 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETII----IDELNLTIPKGEITVFIGSNGCGKStlLRSLA---------RLMKPKggsVLLEGSSI 67
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKS--VSSLAimglidypgRVMAEK---LEFNGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 68 AKLPTKE----VAKELAILPQ------GPSAPEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEELAERtv 137
Cdd:PRK11022 76 QRISEKErrnlVGAEVAMIFQdpmtslNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQ-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 138 dsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKK 217
Cdd:PRK11022 154 --LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
250
....*....|...
gi 521288620 218 IYAEGRPESIINC 230
Cdd:PRK11022 232 VVETGKAHDIFRA 244
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-227 |
1.81e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.85 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSL-----GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTK-- 73
Cdd:COG4598 1 MTDTAPPALEVrdlhkSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 74 --EVAK---------ELAILPQGPSAPEGLTVLQLVKQGryPYQnWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSG 142
Cdd:COG4598 81 elVPADrrqlqrirtRLGMVFQSFNLWSHMTVLENVIEA--PVH-VLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
....*
gi 521288620 223 RPESI 227
Cdd:COG4598 237 PPAEV 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-229 |
2.21e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGgSVLLEGSSIAKLPTKE---VAKELAILPQGPSA-- 88
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 -PEgLTVLQLVKQGRYPYQNWLKqwSAEDEEAVQKALKATRME-ELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:PRK15134 376 nPR-LNVLQIIEEGLRVHQPTLS--AAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 167 TTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-229 |
4.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG----SSIAKLP-TKEVAKELAILPQGPSapeglt 93
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKeVKRLRKEIGLVFQFPE------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 vLQLvkqgrypYQNWLKQ--------WSAEDEEAVQKA---LKATRM-EELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK13645 101 -YQL-------FQETIEKdiafgpvnLGENKQEAYKKVpelLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-215 |
4.46e-19 |
|
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: 82.90 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklptkevakeLAILPQGPSAPEGlTVLQL 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 VKQGrYPYqnwlkqwsaeDEEAVQKALKATRME------------ELAERTVdSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03250 86 ILFG-KPF----------DEERYEKVIKACALEpdleilpdgdltEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 166 PTTYLDM---THQIE--ILDLLfelneHEKRTIVMVLHDLNLaCRYAHHLVAIKD 215
Cdd:cd03250 154 PLSAVDAhvgRHIFEncILGLL-----LNNKTRILVTHQLQL-LPHADQIVVLDN 202
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-201 |
7.46e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 7.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGY--GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:PRK11160 338 SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGP---SApeglTV---LQLVKQgrypyqnwlkqwSAEDEEAVQkALKATRMEELAERT--VDS--------LSGGQ 144
Cdd:PRK11160 418 VVSQRVhlfSA----TLrdnLLLAAP------------NASDEALIE-VLQQVGLEKLLEDDkgLNAwlgeggrqLSGGE 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 145 RQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDLN 201
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLT 535
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-210 |
7.53e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 8 TLSLGYGETIIiDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--------RLMKPKGGSVLLegssiaklptkevakel 79
Cdd:COG4178 369 TLRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF----------------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 aiLPQGPSAPEGlTVLQLVkqgRYPYQNwlkqwSAEDEEAVQKALKATRMEELAER--TVDS----LSGGQRQRAWIAMT 153
Cdd:COG4178 431 --LPQRPYLPLG-TLREAL---LYPATA-----EAFSDAELREALEAVGLGHLAERldEEADwdqvLSLGEQQRLAFARL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 154 LAQETDIILLDEPTTYLDMTHQIEILDLLfeLNEHEKRTIVMVLHDLNLACRYAHHL 210
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-222 |
8.01e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 8.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPsapegltvlql 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEP----------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 VKQGRYPYQNWLKQWSAEDEEAVQKALKA-------TRMEELAERTVDS----LSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:TIGR00958 565 VLFSGSVRENIAYGLTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 167 TTYLDmthqIEILDLLFELNEHEKRTIVMVLHDLNLaCRYAHHLVAIKDKKIYAEG 222
Cdd:TIGR00958 645 TSALD----AECEQLLQESRSRASRTVLLIAHRLST-VERADQILVLKKGSVVEMG 695
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-225 |
1.06e-18 |
|
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: 81.80 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK--GGSVLLEGSSIAKLPTKEVAKE-LAILPQGPSAPEGLTV 94
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIPGVKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVkqgrypyqnwlkqwsaedeeavqkalkatrmeelaeRTVD-SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 173
Cdd:cd03217 95 ADFL------------------------------------RYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 174 HQIEILDLLFELNEhEKRTIVMVLHDLNLA----CRYAHHLVaikDKKIYAEGRPE 225
Cdd:cd03217 139 ALRLVAEVINKLRE-EGKSVLIITHYQRLLdyikPDRVHVLY---DGRIVKSGDKE 190
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-243 |
1.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELN---LTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGP------SAPEGLTVLQLVKQGrYPYQNWLKQwsaedeeaVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTL 154
Cdd:PRK13642 85 MVFQNPdnqfvgATVEDDVAFGMENQG-IPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPESIINCKlvQ 234
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS--E 232
|
....*....
gi 521288620 235 DVFEMDCEV 243
Cdd:PRK13642 233 DMVEIGLDV 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-207 |
2.01e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-L 79
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVLQLVKQGRYpyqnwlkqwSAEDEEAVQKALKA----TRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGF---------FAERDQFQERIKWVyelfPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYA 207
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLA 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-198 |
2.23e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.65 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPKGGSVLLEGSSIAKLPTKEVAKE---LAIlpQGPSA 88
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAgifLAF--QYPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQL-------VKQGRYPYQNWLKQwsaedeeaVQKALKATRM-EELAERTVD-SLSGGQRQRAWIAMTLAQETD 159
Cdd:COG0396 89 IPGVSVSNFlrtalnaRRGEELSAREFLKL--------LKEKMKELGLdEDFLDRYVNeGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521288620 160 IILLDEPTTYLDmthqIEILDLLFE-LNE--HEKRTIVMVLH 198
Cdd:COG0396 161 LAILDETDSGLD----IDALRIVAEgVNKlrSPDRGILIITH 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-171 |
2.73e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.61 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 6 TETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlPTKEVAKELAILPQG 85
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSAPEGLTVLqlvkqgrypyQNwLKQWSAE-DEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:cd03231 82 PGIKTTLSVL----------EN-LRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*..
gi 521288620 165 EPTTYLD 171
Cdd:cd03231 151 EPTTALD 157
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-230 |
3.22e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 3.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSI--AKLPTKEVAKELAI 81
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSapEGLTVLQLVKQGRYPYQNwLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK13638 82 VFQDPE--QQIFYTDIDSDIAFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 162 LLDEPTTYLD---MTHQIEILDLLFELNEHekrtIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINC 230
Cdd:PRK13638 159 LLDEPTAGLDpagRTQMIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
3.38e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM-KPKG----GSVLLEGSSIAKL-PTKEVA 76
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSaPEGLTVLQLVKQGRYPYQNWLKQwsaEDEEAVQKALKATRM-EELAERTVDS---LSGGQRQRAWIAM 152
Cdd:PRK14271 101 RRVGMLFQRPN-PFPMSIMDNVLAGVRAHKLVPRK---EFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 153 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-198 |
3.95e-18 |
|
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: 79.90 E-value: 3.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 10 SLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA-RLMKPK-GGSVLLEGSSIAKlptKEVAKELAILPQGPS 87
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPLDK---RSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGLTVlqlvkqgrypyqnwlkqwsaedEEAVQKALKatrmeelaertVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:cd03213 93 LHPTLTV----------------------RETLMFAAK-----------LRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190
....*....|....*....|....*....|.
gi 521288620 168 TYLDMTHQIEILDLLFELnEHEKRTIVMVLH 198
Cdd:cd03213 140 SGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-224 |
5.04e-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: 83.30 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 25 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEgssiAKLPTKevakelailPQGPSAPEGLTVLQLVKQGRYP 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYK---------PQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 105 Y--QNWLKqwsaedEEAVQKalkaTRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLL 182
Cdd:COG1245 429 DfgSSYYK------TEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521288620 183 FELNEHEKRTIVMVLHDLnlacrYAHHLVAikDKKIYAEGRP 224
Cdd:COG1245 499 RRFAENRGKTAMVVDHDI-----YLIDYIS--DRLMVFEGEP 533
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-205 |
5.67e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG-----GSVLLEGSSI--AKLPTK 73
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 74 EVAKELAILPQGPSapegltVLQLVKQGRYPYQNWLKQW--SAEDEEAVQKALKATRM-EELAERTVDS---LSGGQRQR 147
Cdd:PRK14258 85 RLRRQVSMVHPKPN------LFPMSVYDNVAYGVKIVGWrpKLEIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 148 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACR 205
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-218 |
5.88e-18 |
|
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: 80.21 E-value: 5.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTV 94
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVKQGrypyqnwLKQWSAED-EEAVQKALKATRMEELA--------ERTvDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03248 105 QDNIAYG-------LQSCSFECvKEAAQKAHAHSFISELAsgydtevgEKG-SQLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521288620 166 PTTYLDMTHQIEILDLLFElnEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKI 218
Cdd:cd03248 177 ATSALDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-204 |
6.05e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAilPQGPSAPEgLT 93
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPA-LT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLqlvkqgrypyQNwLKQWSA---EDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:PRK13539 90 VA----------EN-LEFWAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 521288620 171 DMTHQIEILDLLFelnEHEKR--TIVMVLH-DLNLAC 204
Cdd:PRK13539 159 DAAAVALFAELIR---AHLAQggIVIAATHiPLGLPG 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-200 |
7.56e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 25 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEgssiAKLPTKevakelailPQGPSAPEGLTVLQLVKQGRYP 104
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYK---------PQYIKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 105 Y-QNWLKqwsaedEEAVQKalkaTRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLF 183
Cdd:PRK13409 428 LgSSYYK------SEIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170
....*....|....*..
gi 521288620 184 ELNEHEKRTIVMVLHDL 200
Cdd:PRK13409 498 RIAEEREATALVVDHDI 514
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-224 |
9.04e-18 |
|
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: 79.38 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGLTVLQLVKQGRYpyqnwlkqwsaeDEEAVQKALKATrmeelaeRTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEY------------SDEEIYGALRVS-------EGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFElnEHEKRTIVMVLHDLNLACRYAHHLVaIKDKKIYAEGRP 224
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILV-MDAGEVKEYDHP 207
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-229 |
1.99e-17 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 81.54 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGET--IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA 80
Cdd:TIGR03797 451 AIEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 IlpqgpsapegltVLQlvkQGRYP----YQNWLKQWSAEDEEAVQkalkATRMEELAE---------RTVDS-----LSG 142
Cdd:TIGR03797 531 V------------VLQ---NGRLMsgsiFENIAGGAPLTLDEAWE----AARMAGLAEdirampmgmHTVISegggtLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ---IEILDLLfelneheKRTIVMVLHDLNlACRYAHHLVAIKDKKIY 219
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQaivSESLERL-------KVTRIVIAHRLS-TIRNADRIYVLDAGRVV 663
|
250
....*....|
gi 521288620 220 AEGRPESIIN 229
Cdd:TIGR03797 664 QQGTYDELMA 673
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-228 |
2.27e-17 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 81.71 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVLQL 97
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 VKQGRyPyqnwlkqwSAEDEEAVQKA-----------LKATRMEELAERTVdSLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:TIGR01846 551 IALCN-P--------GAPFEHVIHAAklagahdfiseLPQGYNTEVGEKGA-NLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 167 TTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:TIGR01846 621 TSALDYESEALIMRNMREIC--RGRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-171 |
2.34e-17 |
|
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: 78.17 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLpTKEVAKELAILP 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVLQLVKqgrypyqnWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:TIGR01189 80 HLPGLKPELSALENLH--------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
....*...
gi 521288620 164 DEPTTYLD 171
Cdd:TIGR01189 152 DEPTTALD 159
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-215 |
3.30e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK-ELAIL 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGRYPYQNWLK----QWSAEDEEAVQKALKATRMEELAERtVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCGvniiDWREMRVRAAMMLLRVGLKVDLDEK-VANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 159 DIILLDEPTTYLdMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKD 215
Cdd:PRK09700 165 KVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKD 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-227 |
4.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.01 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAP-EGLT 93
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 V-----LQLVKQGrYPYQnwlkqwsaEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:PRK13650 99 VeddvaFGLENKG-IPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 169 YLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNlacryahhLVAIKDKKI-YAEGRPESI 227
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLD--------EVALSDRVLvMKNGQVEST 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-237 |
8.10e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-L 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTV---LQLVKQGRypyqnwlKQWSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVydnLMAVLQIR-------DDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLfelnEHEKRTIVMVL---HDLNLACRYAHHLVAIKDKKIYAEGRPESIINCKL 232
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRII----EHLRDSGLGVLitdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
....*
gi 521288620 233 VQDVF 237
Cdd:PRK10895 230 VKRVY 234
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-215 |
8.17e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.99 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiaKLPTKEVAKELAILPQGPSApegltvlqlv 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----KNESEPSFEATRSRNRYSVA---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 kqgrYPYQN-WLKQWSAEDEEAVQKALKATRME---------------------ELAERTVDsLSGGQRQRAWIAMTLAQ 156
Cdd:cd03290 83 ----YAAQKpWLLNATVEENITFGSPFNKQRYKavtdacslqpdidllpfgdqtEIGERGIN-LSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 157 ETDIILLDEPTTYLDM-----THQIEILDLLfelnEHEKRTIVMVLHDLNLaCRYAHHLVAIKD 215
Cdd:cd03290 158 NTNIVFLDDPFSALDIhlsdhLMQEGILKFL----QDDKRTLVLVTHKLQY-LPHADWIIAMKD 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-201 |
1.06e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.21 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLpTKEVAKELAI-----------LPqgps 87
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGVvfgqrsqlwwdLP---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGLTVLQLVkqgrypYQnwlkqwsaedeeaVQKALKATRMEELAE---------RTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:COG4586 113 AIDSFRLLKAI------YR-------------IPDAEYKKRLDELVElldlgelldTPVRQLSLGQRMRCELAAALLHRP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLN 201
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
9-215 |
1.22e-16 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 79.22 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYG--ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP 86
Cdd:TIGR03796 483 ITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 SAPEGlTVlqlvkqgrypyQNWLKQW--SAEDEEAVQKALKATRMEELAERT--VDS--------LSGGQRQRAWIAMTL 154
Cdd:TIGR03796 563 FLFEG-TV-----------RDNLTLWdpTIPDADLVRACKDAAIHDVITSRPggYDAelaegganLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLfelnehEKR--TIVMVlhdlnlacryAHHLVAIKD 215
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNL------RRRgcTCIIV----------AHRLSTIRD 677
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-227 |
1.58e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMK------PKGGSVLLEGSSIAKLPTKEVAKELAIL 82
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKqgrYPYQNWLKQWSAEDEEAVQKALKATRM-EELAER---TVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRlnsPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELK--NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-200 |
1.70e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTK---EVAKELAILPQGPSA---PEgL 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLAslnPR-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVKQGRYPYQNWLKQwsAEDEEAVQK-ALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK15079 116 TIGEIIAEPLRTYHPKLSR--QEVKDRVKAmMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*....
gi 521288620 172 MTHQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-200 |
2.86e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 25 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlPTKEVAKELAilpqgpsapeglTVLQLVKQGRYP 104
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQKLLR------------QKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 105 YQNWLKQWSAEDEE---------AVQKALKATRM-------EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:PRK11308 104 SLNPRKKVGQILEEpllintslsAAERREKALAMmakvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|..
gi 521288620 169 YLDMTHQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-212 |
2.89e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.05 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLeGSSIaKL-----------PT 72
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-KLayvdqsrdaldPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 73 KEVAKELAilpqgpsapEGLTVLQLVKQ--------GRYPYqnwlkqwSAEDEeavQKalkatrmeelaerTVDSLSGGQ 144
Cdd:TIGR03719 401 KTVWEEIS---------GGLDIIKLGKReipsrayvGRFNF-------KGSDQ---QK-------------KVGQLSGGE 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 145 RQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVA 212
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-225 |
3.42e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAK----ELAILPQGPS 87
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 APEGLTVLQLVKqgrYP--YQNWLKqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:PRK10535 97 LLSHLTAAQNVE---VPavYAGLER---KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 166 PTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRyAHHLVAIKDKKIYAEGRPE 225
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-200 |
5.30e-16 |
|
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: 77.52 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 23 NLTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPKGGSV--------LLE---GSSIAKLPTKEVAKEL--AILPQG--- 85
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKKLANGEIkvAHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 -PSAPEGlTVLQLVKQgrypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:COG1245 172 iPKVFKG-TVRELLEK-------------VDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*.
gi 521288620 165 EPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDL 200
Cdd:COG1245 238 EPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDL 272
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-202 |
1.38e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiaKLPTKEVAKELAILP 83
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPsapegLTVLQLVKqgrypyqnwLKQWSAEDEeaVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:PRK09544 81 TLP-----LTVNRFLR---------LRPGTKKED--ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNL 202
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-200 |
1.46e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.00 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 23 NLTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLE-----------GSSIAKLPTKEVAKEL--AILPQG--- 85
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswdevlkrfrGTELQNYFKKLYNGEIkvVHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 -PSAPEGlTVLQLVKQgrypyqnwlkqwsaEDEEAVQKAL-KATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:PRK13409 172 iPKVFKG-KVRELLKK--------------VDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 521288620 164 DEPTTYLDMTHQIEILDLLFELNehEKRTIVMVLHDL 200
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHDL 271
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-228 |
1.56e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 75.85 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlT 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQ-LVKQGRYPyqnwlkqwsaeDEEAVQKALKATRMEELAERTVD-----------SLSGGQRQRAWIAMTLAQETDII 161
Cdd:TIGR01842 408 VAEnIARFGENA-----------DPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLN-LACryAHHLVAIKDKKIYAEGRPESII 228
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSlLGC--VDKILVLQDGRIARFGERDEVL 541
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-222 |
1.83e-15 |
|
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: 75.91 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVLQLV 98
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 KQGRypyqnwLKQWsaeDEEAVQKALKATRMEELAERTVDS-----------LSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:TIGR02203 427 AYGR------TEQA---DRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 168 TYLDMTHQIEILDLLFELneHEKRTIVMVLHDLNlACRYAHHLVAIKDKKIYAEG 222
Cdd:TIGR02203 498 SALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-228 |
2.78e-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: 73.29 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYG--ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 lpqgpsapegltVLQlvkqgrypyQNWLKQWSAEDEEA-------VQKALKATRMEE---------------LAERTVdS 139
Cdd:cd03252 81 ------------VLQ---------ENVLFNRSIRDNIAladpgmsMERVIEAAKLAGahdfiselpegydtiVGEQGA-G 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 140 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDllfelNEHE---KRTIVMVLHDLNlACRYAHHLVAIKDK 216
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMR-----NMHDicaGRTVIIIAHRLS-TVKNADRIIVMEKG 212
|
250
....*....|..
gi 521288620 217 KIYAEGRPESII 228
Cdd:cd03252 213 RIVEQGSHDELL 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-227 |
3.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTV 94
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVKQgrYPYQNWLKQWSAED------------EEAVQKALKATRM----EELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK13631 118 VSMVFQ--FPEYQLFKDTIEKDimfgpvalgvkkSEAKKLAKFYLNKmgldDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFElNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-229 |
3.99e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 72.94 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSS-----IAKLPTKE----VAKEL 79
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAErrrlMRTEW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AILPQGPSAPEGLTVL-------QLVKQGRYPYQNwLKQWSAEDEEAVQkaLKATRMEELAErtvdSLSGGQRQRAWIAM 152
Cdd:TIGR02323 89 GFVHQNPRDGLRMRVSaganigeRLMAIGARHYGN-IRATAQDWLEEVE--IDPTRIDDLPR----AFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 153 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-234 |
4.52e-15 |
|
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: 74.78 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVlql 97
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-TI--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 vKQ--GRYPyqnwlkqwsAEDEEAVQKALKATRMEELAER------TV-----DSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:COG4618 423 -AEniARFG---------DADPEKVVAAAKLAGVHEMILRlpdgydTRigeggARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 165 EPTTYLDmtHQIE--ILDLLFELNEHeKRTIVMVLHDLNLAcRYAHHLVAIKDKKIYAEGRPESIINcKLVQ 234
Cdd:COG4618 493 EPNSNLD--DEGEaaLAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVLA-RLAR 559
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-214 |
6.57e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK-----GGSVLLEGSSIAKLPTKEV----AKELAILPQGPSA 88
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 peGLTVLQLVKQGRY---PYQNWLKQWSAEDEeaVQKALKATRMEELAERTVD---SLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:PRK15134 104 --SLNPLHTLEKQLYevlSLHRGMRREAARGE--ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIK 214
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-205 |
9.82e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 10 SLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELA------- 80
Cdd:PRK10584 15 SVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkhvgfvf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ---ILPQGPSAPEGLTVLQLVKqgrypyqnwlkqwSAEDEEAVQKALKATRMEELAERTVD---SLSGGQRQRAWIAMTL 154
Cdd:PRK10584 95 qsfMLIPTLNALENVELPALLR-------------GESSRQSRNGAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACR 205
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-201 |
1.42e-14 |
|
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: 70.99 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGlTVlqlvkqgRY---PYQNWlkqwsaeDEEAVQKALKATRMEELAERTVDSL-----------SGGQRQR 147
Cdd:cd03244 83 IPQDPVLFSG-TI-------RSnldPFGEY-------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521288620 148 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFElnEHEKRTIVMVLHDLN 201
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-201 |
1.93e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiaklptKEV-------AKELAI--LPQGPSAPE 90
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--------KPVrirsprdAIALGIgmVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 GLTVLQLVKQGRYPYQNWLKQWSAEdeeavqkalkATRMEELAER---------TVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:COG3845 94 NLTVAENIVLGLEPTKGGRLDRKAA----------RARIRELSERygldvdpdaKVEDLSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521288620 162 LLDEPTTYLdmT-HQIEIL-DLLFELNEhEKRTIVMVLHDLN 201
Cdd:COG3845 164 ILDEPTAVL--TpQEADELfEILRRLAA-EGKSIIFITHKLR 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-171 |
3.50e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLeGSSIaKL-----------PT 72
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-KLayvdqsrdaldPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 73 KEVAKELAilpqgpsapEGLTVLQLVKQ--------GRY----PYQnwlkqwsaedeeavQKAlkatrmeelaertVDSL 140
Cdd:PRK11819 403 KTVWEEIS---------GGLDIIKVGNReipsrayvGRFnfkgGDQ--------------QKK-------------VGVL 446
|
170 180 190
....*....|....*....|....*....|.
gi 521288620 141 SGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-200 |
4.37e-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: 69.77 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLL--EGSSI--AKLPTKE-----------VAKELAILP 83
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPREilalrrrtigyVSQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QgpsapegLTVLQLVKQGrypyqnwLKQWSAEDEEAVQKALKATRMEELAERTVDS----LSGGQRQRAWIAMTLAQETD 159
Cdd:COG4778 107 R-------VSALDVVAEP-------LLERGVDREEARARARELLARLNLPERLWDLppatFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFELneheKR---TIVMVLHDL 200
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEA----KArgtAIIGIFHDE 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-200 |
5.56e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVLQlvkqg 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLRD----- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 rypyqNWLKQWSAEDEEAVQKALKATRMEELAERT---VDS--------LSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:PRK11174 442 -----NVLLGNPDASDEQLQQALENAWVSEFLPLLpqgLDTpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190
....*....|....*....|....*....|
gi 521288620 171 DMTHQIEILDLLFELNEHekRTIVMVLHDL 200
Cdd:PRK11174 517 DAHSEQLVMQALNAASRR--QTTLMVTHQL 544
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-228 |
6.27e-14 |
|
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: 71.37 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLL----EGSSIAKLPTKE---VAKELAILPQGPSAPEG 91
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQlvkqgrypyqNWLKQWSAE--DEEAVQKALKATRM--------EELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:TIGR03269 380 RTVLD----------NLTEAIGLElpDELARMKAVITLKMvgfdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESII 228
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-228 |
6.31e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.52 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 17 IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQ 96
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRYPYQN-WlkqWSAE--DEEAVQKALKATRMEELAERTvDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMt 173
Cdd:TIGR00957 1380 LDPFSQYSDEEvW---WALElaHLKTFVSALPDKLDHECAEGG-ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL- 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 174 hqiEILDLLFEL--NEHEKRTIVMVLHDLNLACRYAHhlVAIKDKKIYAE-GRPESII 228
Cdd:TIGR00957 1455 ---ETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTR--VIVLDKGEVAEfGAPSNLL 1507
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-167 |
6.42e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklptkevAKELAI- 81
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-------AGDIATr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 -----LPQGPSAPEGLTVLQ-LVKQGRypyqnwLKQWSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTL 154
Cdd:NF033858 339 rrvgyMSQAFSLYGELTVRQnLELHAR------LFHLPAAEiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170
....*....|...
gi 521288620 155 AQETDIILLDEPT 167
Cdd:NF033858 413 IHKPELLILDEPT 425
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-222 |
1.01e-13 |
|
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: 68.33 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 11 LGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLptkEVAkeLAILPQgpsape 90
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---GLG--GGFNPE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 gLTVLQLVK-QGRypyqnwLKQWSAEDEEAvqkalkatRMEELAE---------RTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:cd03220 99 -LTGRENIYlNGR------LLGLSRKEIDE--------KIDEIIEfselgdfidLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 161 ILLDEPTTYLDMTHQIEILDLLFELNEHeKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-199 |
1.03e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE----- 74
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 75 VAKELAILPQgpsapegLTVlqlvkqgrypYQNW---LKQW---SAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRa 148
Cdd:PRK11650 81 VFQNYALYPH-------MSV----------RENMaygLKIRgmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 149 wIAMTLA--QETDIILLDEPTTYLD------MthQIEILDLLFELNEhekrTIVMVLHD 199
Cdd:PRK11650 143 -VAMGRAivREPAVFLFDEPLSNLDaklrvqM--RLEIQRLHRRLKT----TSLYVTHD 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-229 |
1.24e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.57 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 12 GYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklptkeVAkelAILpqGPSA--- 88
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VS---ALL--ELGAgfh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEgLTVLQLVK-QGRYpyqnwLKQWSAEDEEAVQKalkatrMEELAE------RTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:COG1134 101 PE-LTGRENIYlNGRL-----LGLSRKEIDEKFDE------IVEFAElgdfidQPVKTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIIN 229
Cdd:COG1134 169 LVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-222 |
1.62e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 5 STETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG-----SSIAKLPTKE----V 75
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAErrrlL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKELAILPQGPSapEGL--TVL-------QLVKQGRYPYQNwLKQWSAEDEEAVQkaLKATRMEELAeRTvdsLSGGQRQ 146
Cdd:PRK11701 88 RTEWGFVHQHPR--DGLrmQVSaggnigeRLMAVGARHYGD-IRATAGDWLERVE--IDAARIDDLP-TT---FSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 147 RAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEG 222
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-203 |
2.05e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEItVFI-GSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTkEVAKELAILPQGPSAPEGL 92
Cdd:PRK13538 12 DERILFSGLSFTLNAGEL-VQIeGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TvlqlvkqgryPYQN--WLKQWSAE-DEEAVQKALKAT---RMEELAERTvdsLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:PRK13538 90 T----------ALENlrFYQRLHGPgDDEALWEALAQVglaGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521288620 167 TTYLDmTHQIEILDLLFElnEHEKR--TIVMVLH-DLNLA 203
Cdd:PRK13538 157 FTAID-KQGVARLEALLA--QHAEQggMVILTTHqDLPVA 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-208 |
2.83e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 29 GEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE---VAKELAILPQGPSApeGLTVLQLVKqgrYPY 105
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqaLRRDIQFIFQDPYA--SLDPRQTVG---DSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 106 QNWLKQWSAEDEEAVQKAL-----KATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILD 180
Cdd:PRK10261 425 MEPLRVHGLLPGKAAAARVawlleRVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIIN 504
|
170 180
....*....|....*....|....*...
gi 521288620 181 LLFELNEHEKRTIVMVLHDLNLACRYAH 208
Cdd:PRK10261 505 LLLDLQRDFGIAYLFISHDMAVVERISH 532
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-225 |
3.04e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.21 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 29 GEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVA---KELAILPQGPSAPEGLTV-----LQLVKQ 100
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQDHHLLMDRTVydnvaIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 101 GRypyqnwlkqwSAED-EEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEIL 179
Cdd:PRK10908 108 GA----------SGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521288620 180 DLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPE 225
Cdd:PRK10908 178 RLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-171 |
7.85e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKggsvllEGSSIAKLPTKEVAKELAI---LPQG 85
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT------PVAGCVDVPDNQFGREASLidaIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSAPEGLTVLQLVKQGRYPyqNWLkqwsaedeeavqkalkatrmeelaeRTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:COG2401 110 GDFKDAVELLNAVGLSDAV--LWL-------------------------RRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
....*.
gi 521288620 166 PTTYLD 171
Cdd:COG2401 163 FCSHLD 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-206 |
8.88e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLT-IPKGEITVfIGSNGCGKSTLLRSLARLMKPKGGSVLL-EGSSIAklptkevakelaILPQGPSAPEGLTVL 95
Cdd:TIGR03719 20 ILKDISLSfFPGAKIGV-LGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKVG------------YLPQEPQLDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVKQGRYPYQNWLK-------QWSAEDEEAVQKALKATRMEEL--------AERTVD----------------SLSGGQ 144
Cdd:TIGR03719 87 ENVEEGVAEIKDALDrfneisaKYAEPDADFDKLAAEQAELQEIidaadawdLDSQLEiamdalrcppwdadvtKLSGGE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 145 RQRAWIAMTLAQETDIILLDEPTTYLDMthqiEILDLLFELNEHEKRTIVMVLHDlnlacRY 206
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD-----RY 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-243 |
1.92e-12 |
|
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: 66.75 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLaRLMK---PKGGSVLLE----------------- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDqyePTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 64 ------GSSIAKLP----------TKEVAKELAILPQGPSAPEG-LTVLQLVKQGrypyqnwLKQWSAEDEEAVQKALKA 126
Cdd:TIGR03269 80 epcpvcGGTLEPEEvdfwnlsdklRRRIRKRIAIMLQRTFALYGdDTVLDNVLEA-------LEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 127 TRMEELAERTVD---SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD-MTHQIeILDLLFELNEHEKRTIVMVLHDLNL 202
Cdd:TIGR03269 153 IEMVQLSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKL-VHNALEEAVKASGISMVLTSHWPEV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 521288620 203 ACRYAHHLVAIKDKKIYAEGRPESIINcKLVQDV--FEMDCEV 243
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKEEGTPDEVVA-VFMEGVseVEKECEV 273
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-200 |
2.21e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAilpqgpsapegltv 94
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA-------------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 lqLVKQGRYPYQNWL---------KQWSAEDEEAVQKALKATRMEELAERTVD--------SLSGGQRQRAWIAMTLAQE 157
Cdd:PRK11176 421 --LVSQNVHLFNDTIanniayartEQYSREQIEEAARMAYAMDFINKMDNGLDtvigengvLLSGGQRQRIAIARALLRD 498
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521288620 158 TDIILLDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDL 200
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRL 539
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-199 |
2.54e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MSAISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLArlmkpkgGSVLLEGSSIaklptkEVAKELA 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRI------IYEQDLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 I--LPQGPSAPEGLTVLQLVKQG---------RY----------PYQNWLKQ-------------WSAEDEeaVQKALKA 126
Cdd:PRK11147 68 VarLQQDPPRNVEGTVYDFVAEGieeqaeylkRYhdishlvetdPSEKNLNElaklqeqldhhnlWQLENR--INEVLAQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521288620 127 TRMEelAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLLFELNEHEKRTIVMVLHD 199
Cdd:PRK11147 146 LGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-206 |
2.54e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLT-IPKGEITVfIGSNGCGKSTLLRSLARLMKPKGG-SVLLEGSSIAklptkevakelaILPQGPSAPEGLTVL 95
Cdd:PRK11819 22 ILKDISLSfFPGAKIGV-LGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKVG------------YLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVKQGRYPYQNWLKQWsaeDEEAVQKALKATRMEELAER----------------------------------TVDSLS 141
Cdd:PRK11819 89 ENVEEGVAEVKAALDRF---NEIYAAYAEPDADFDALAAEqgelqeiidaadawdldsqleiamdalrcppwdaKVTKLS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 142 GGQRQRAWIAMTLAQETDIILLDEPTTYLDMthqieildllfE----LNEHEKR---TIVMVLHDlnlacRY 206
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDA-----------EsvawLEQFLHDypgTVVAVTHD-----RY 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-198 |
2.55e-12 |
|
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: 63.33 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 16 TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegssiaKLPTKEvakELAILPQGPSAPEGLTVL 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE---DLLFLPQRPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVkqgrYPyqnwlkqWSaedeeavqkalkatrmeelaertvDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMthq 175
Cdd:cd03223 83 QLI----YP-------WD------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE--- 124
|
170 180
....*....|....*....|...
gi 521288620 176 iEILDLLFELNEHEKRTIVMVLH 198
Cdd:cd03223 125 -ESEDRLYQLLKELGITVISVGH 146
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-210 |
3.24e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK----------GGSVLLegssiaKLPTKE----VAKEL 79
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLL------KLSPRErrkiIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AIL---PQG---PSAPEGLTVLQLVKQGRYPyqNWLKQWSAEDEEAVQKALKATRMEElAERTVDS----LSGGQRQRAW 149
Cdd:COG4170 92 AMIfqePSScldPSAKIGDQLIEAIPSWTFK--GKWWQRFKWRKKRAIELLHRVGIKD-HKDIMNSypheLTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 150 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHHL 210
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-224 |
3.57e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 63.36 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 26 IPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEvakelailpqgpsapegltvlqlvkqgrypy 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 106 qnwlkqwsaedeeavqkalkatrmeelaertvdSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFEL 185
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|....*....
gi 521288620 186 NEHEKRTIVMVLHDLNLacryahhLVAIKDKKIYAEGRP 224
Cdd:cd03222 118 SEEGKKTALVVEHDLAV-------LDYLSDRIHVFEGEP 149
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-200 |
3.73e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEG-------SSIAKLPTKEVAK-------ELAILPQ 84
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 85 GP--SAPEGLTVLQLVKQGRYPYQNwlkqwsAEDEEAVQKA---LKATRM---EELAERTVDSLSGGQRQRAWIAMTLAQ 156
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESIRLHQG------ASREEAMVEAkrmLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 157 ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDL 200
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-199 |
3.76e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklptkevAKELAILPQGPSApegltvlqlVKQG 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-------AEQPEDYRKLFSA---------VFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 RYPYQNWL-KQWSAEDEEAVQKALKATRMEELAE----RTVD-SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD-MTH 174
Cdd:PRK10522 406 FHLFDQLLgPEGKPANPALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDpHFR 485
|
170 180
....*....|....*....|....*
gi 521288620 175 QIEILDLLFELNEHEKrTIVMVLHD 199
Cdd:PRK10522 486 REFYQVLLPLLQEMGK-TIFAISHD 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-198 |
4.15e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-----VA---KELAILPQgpsapeg 91
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagVAiiyQELHLVPE------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQLVKQGRYPYQ-NWLKqwsaedeeavQKALKATRMEELAERTVD--------SLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:PRK11288 94 MTVAENLYLGQLPHKgGIVN----------RRLLNYEAREQLEHLGVDidpdtplkYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 521288620 163 LDEPTTYLDmTHQIEILDLLFELNEHEKRTIVMVLH 198
Cdd:PRK11288 164 FDEPTSSLS-AREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-218 |
5.08e-12 |
|
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: 62.83 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-VAKELAILPQGPSApEGLtVLQL 97
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKR-EGL-VLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 vkqgrypyqnwlkqwsaedeeavqkalkatrmeELAERTV--DSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ 175
Cdd:cd03215 94 ---------------------------------SVAENIAlsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521288620 176 IEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:cd03215 141 AEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-200 |
1.29e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.21 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP-----SAPEGLT 93
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAglfnrSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VlqlvkqGRYpyqnwlkqwSAEDEEaVQKALKATRMEELAERTVD-----------SLSGGQRQRAWIAMTLAQETDIIL 162
Cdd:PRK13657 431 V------GRP---------DATDEE-MRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHekRTIVMVLHDL 200
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKG--RTTFIIAHRL 530
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-218 |
1.37e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklptkevakeLAILPQgpsapegltvlqlvkq 100
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-------------IAYVPQ---------------- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 101 grypyQNWLKQ---------WSAEDEEAVQKALKATRME------------ELAERTVDsLSGGQRQRAWIAMTLAQETD 159
Cdd:PTZ00243 729 -----QAWIMNatvrgnilfFDEEDAARLADAVRVSQLEadlaqlgggletEIGEKGVN-LSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 160 IILLDEPTTYLDMTHQIEILDLLFeLNEHEKRTIVMVLHDLNLACRyAHHLVAIKDKKI 218
Cdd:PTZ00243 803 VYLLDDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-217 |
2.76e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGS-SIAKLPTKEVAKELAILPQGP---------- 86
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPllfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 -----SAPEGLTVL--QLVKQGRYPYQNWLKQWSA------------------------------EDEEAVQKALKA--- 126
Cdd:PTZ00265 480 ikyslYSLKDLEALsnYYNEDGNDSQENKNKRNSCrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 127 -------TRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHD 199
Cdd:PTZ00265 560 dfvsalpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250
....*....|....*...
gi 521288620 200 LNlACRYAHHLVAIKDKK 217
Cdd:PTZ00265 640 LS-TIRYANTIFVLSNRE 656
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-199 |
4.62e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegssiaKLPTK-EVAkelailpqg 85
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKlEVA--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 psapegltvlqlvkqgrypyqnWLKQWSAE-DEEAvqkalkaTRMEELAE----------------------------RT 136
Cdd:PRK11147 386 ----------------------YFDQHRAElDPEK-------TVMDNLAEgkqevmvngrprhvlgylqdflfhpkraMT 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 137 -VDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLLFELNEHEKRTIVMVLHD 199
Cdd:PRK11147 437 pVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-198 |
7.44e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 15 ETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG--GSVLLEGSSiaklPTKEVAKELAILPQGPSAPEGL 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK----PTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TV---LQLVKQGRYPyQNWLKQWSAEDEEAVQKALKATRMEE--LAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:PLN03211 156 TVretLVFCSLLRLP-KSLTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|.
gi 521288620 168 TYLDMTHQIEILDLLFELnEHEKRTIVMVLH 198
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-171 |
9.09e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.89 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDeLNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPT---KEVAKELA 80
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpycTYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQgpsapegLTVlqlvkqgrypYQNwLKQWSA--EDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQET 158
Cdd:PRK13541 81 LKLE-------MTV----------FEN-LKFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170
....*....|...
gi 521288620 159 DIILLDEPTTYLD 171
Cdd:PRK13541 143 DLWLLDEVETNLS 155
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-200 |
1.03e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 23 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA-KLPTKEVAKELAILPQGPSApEGLTVLQLVKQG 101
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRKA-EGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 ------RY--PYQNWLKQ-WSAEDEEAVQKALK-ATRMeelAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK11288 352 inisarRHhlRAGCLINNrWEAENADRFIRSLNiKTPS---REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180
....*....|....*....|....*....
gi 521288620 172 MTHQIEILDLLFELNEhEKRTIVMVLHDL 200
Cdd:PRK11288 429 VGAKHEIYNVIYELAA-QGVAVLFVSSDL 456
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-168 |
1.56e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLrSL---ARlmKPKGGSVLLEGSSIA-KLPTKEVAKE 78
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagAR--KIQQGRVEVLGGDMAdARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQG------PSapegLTV---LQ----LVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVDSLSGGQR 145
Cdd:NF033858 78 IAYMPQGlgknlyPT----LSVfenLDffgrLFGQDA-----------AERRRRIDELLRATGLAPFADRPAGKLSGGMK 142
|
170 180
....*....|....*....|...
gi 521288620 146 QRAWIAMTLAQETDIILLDEPTT 168
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTT 165
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-202 |
2.08e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegsSIAKlptkevAKELAILPQGP 86
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAK------GIKLGYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 sapegltvLQLVKQGRYPYQNWLKQWSAEDEEAVQKAL-----KATRMEELAERtvdsLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK10636 385 --------LEFLRADESPLQHLARLAPQELEQKLRDYLggfgfQGDKVTEETRR----FSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521288620 162 LLDEPTTYLDMTHQIEILDLLFELneheKRTIVMVLHDLNL 202
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHL 489
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-200 |
2.14e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 3 AISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGlTVLQLVKQGRypyqnwlkqwsAEDEEAVQKALKATRMEELAERTVD-----------SLSGGQRQRAWI 150
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGR-----------DISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLAL 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521288620 151 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEkrTIVMVLHDL 200
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRL 535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-209 |
3.05e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKG---GSVLLEG-----SSIAKLPTKEVA---KELAILPQgps 87
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGeelqaSNIRDTERAGIAiihQELALVKE--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 apegLTVLQLVKQGRYPYQNWLKQWSAEDEEAvQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:PRK13549 97 ----LSVLENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521288620 168 TyldmthqieildllfELNEHEKRTIVMVLHDL---NLACRYAHH 209
Cdd:PRK13549 172 A---------------SLTESETAVLLDIIRDLkahGIACIYISH 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-201 |
3.72e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 35 IGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVlqlvkqgRYPyqnwLKQWSA 114
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TV-------RFN----IDPFSE 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 115 EDEEAVQKALKATRMEELAERTV-----------DSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLF 183
Cdd:PLN03232 1336 HNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR 1415
|
170
....*....|....*...
gi 521288620 184 ElnEHEKRTIVMVLHDLN 201
Cdd:PLN03232 1416 E--EFKSCTMLVIAHRLN 1431
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-171 |
4.29e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 7 ETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARlmKPK----GGSVLLEGSSIAKLPTKEVAKE---L 79
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLgifL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 80 AIlpQGPSAPEGLT---VLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEE-LAERTV-DSLSGGQRQRAWIAMTL 154
Cdd:CHL00131 89 AF--QYPIEIPGVSnadFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPsFLSRNVnEGFSGGEKKRNEILQMA 166
|
170
....*....|....*..
gi 521288620 155 AQETDIILLDEPTTYLD 171
Cdd:CHL00131 167 LLDSELAILDETDSGLD 183
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
23-196 |
5.31e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 23 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA-KLPTKEVAKELAILP-----QG--PSAP--EGL 92
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVPedrkgEGlvLDLSirENI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVKQGRypyqNWLKQWSAEDEEAVQ--KAL--KATRMEELaertVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 168
Cdd:COG1129 352 TLASLDRLSR----GGLLDRRRERALAEEyiKRLriKTPSPEQP----VGNLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190
....*....|....*....|....*....|..
gi 521288620 169 YLDmthqI----EILDLLFELNEhEKRTIVMV 196
Cdd:COG1129 424 GID----VgakaEIYRLIRELAA-EGKAVIVI 450
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-171 |
8.44e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSsiaklptkevakeLAILP 83
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QgpsapegltvlqlvkqgrypyQNWLKQWSAEDEEAVQKALKATRME---------------------ELAERTVDsLSG 142
Cdd:TIGR00957 706 Q---------------------QAWIQNDSLRENILFGKALNEKYYQqvleacallpdleilpsgdrtEIGEKGVN-LSG 763
|
170 180
....*....|....*....|....*....
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-198 |
1.03e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.52 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 29 GEITVFIGSNGCGKSTLLRSLA-RLMK--PKGGSVLLEGSSIAKlptKEVAKELAILPQG----PS--APEGLTVLQLVK 99
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfRSPKgvKGSGSVLLNGMPIDA---KEMRAISAYVQQDdlfiPTltVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 100 QGRYPYQNwlkqwsaEDEEAVQKALKATRMEELA------ERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 173
Cdd:TIGR00955 128 MPRRVTKK-------EKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....*
gi 521288620 174 HQIEILDLLFELNEhEKRTIVMVLH 198
Cdd:TIGR00955 201 MAYSVVQVLKGLAQ-KGKTIICTIH 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-165 |
1.14e-09 |
|
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: 58.27 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEItVFI-GSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklptkevAKELAILPQGPSApegltvlqlVKQ 100
Cdd:COG4615 351 IDLTIRRGEL-VFIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-------ADNREAYRQLFSA---------VFS 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 101 GRYPYQNWLKQWSAEDEEAVQKALKatRMeELAER---------TVDsLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:COG4615 414 DFHLFDRLLGLDGEADPARARELLE--RL-ELDHKvsvedgrfsTTD-LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-243 |
1.62e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRS-LARLMKPKGGSVLLEGSsiaklptkevakeLAILPQGP-----SAPEGL 92
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS-------------VAYVPQVSwifnaTVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVKQGRYpyqnwlkqWSAEDEEAVQKALK---ATRMEELAERTVDsLSGGQRQRAWIAMTLAQETDIILLDEPTTY 169
Cdd:PLN03232 700 LFGSDFESERY--------WRAIDVTALQHDLDllpGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 170 LDMTHQIEILDLLFElNEHEKRTIVMV---LHDLNLACRYAhhLVA---IKDKKIYAEGRPESIINCKLVQDVFEMDCEV 243
Cdd:PLN03232 771 LDAHVAHQVFDSCMK-DELKGKTRVLVtnqLHFLPLMDRII--LVSegmIKEEGTFAELSKSGSLFKKLMENAGKMDATQ 847
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-219 |
1.94e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 28 KGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLegssIaklptkevakelailpqgpsapegltvlqlvkqgrypyqn 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----I---------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 108 wlkqwsaeDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDL-----L 182
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 521288620 183 FELNEHEKRTIVMVLHDLNLACRyaHHLVAIKDKKIY 219
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP--ALLRRRFDRRIV 143
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-209 |
2.22e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 13 YGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPKG---GSVLLEGSSIAKLPTKEV-AKELAILPQGPSA 88
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRMEEL-AERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:TIGR02633 90 VPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521288620 168 TYLDMTHQIEILDLLFELNEHekrtivmvlhdlNLACRYAHH 209
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAH------------GVACVYISH 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-198 |
2.73e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LP-QGPSAPEGL-------TVLQLVKQgrYPYQNWLKQWSAEDeeAVQKALKATRM-EELAERTVD-SLSGGQRQRAWIA 151
Cdd:PRK09580 82 MAfQYPVEIPGVsnqfflqTALNAVRS--YRGQEPLDRFDFQD--LMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521288620 152 MTLAQETDIILLDEPTTYLDmthqIEILDLLFE-LN--EHEKRTIVMVLH 198
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLD----IDALKIVADgVNslRDGKRSFIIVTH 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-228 |
2.77e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIA-KLPTKEVAKELAILPQGP---------SA 88
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESRrdngffpnfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVKQGRYPYQNWLKQWSAEDEEA-VQKALKATRMEELaERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 167
Cdd:PRK09700 359 AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAeNQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521288620 168 TYLDMTHQIEILDLLFELNEhEKRTIVMVLHDLNlacryahHLVAIKDK-KIYAEGRPESII 228
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELP-------EIITVCDRiAVFCEGRLTQIL 491
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-191 |
2.87e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.73 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAK-LPTKEvaKELAILPQgps 87
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQ--KQLCFVGH--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 88 apegltvlqlvKQGRYPYQNwLKQWSAEDEEAVQKALKAT------RMEELAERTVDSLSGGQRQRAWIAMTLAQETDII 161
Cdd:PRK13540 82 -----------RSGINPYLT-LRENCLYDIHFSPGAVGITelcrlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|
gi 521288620 162 LLDEPTTYLDmthQIEILDLLFELNEHEKR 191
Cdd:PRK13540 150 LLDEPLVALD---ELSLLTIITKIQEHRAK 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
3.04e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.61 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKgGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGLTVLQL 97
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 vkqgrYPYQNWLKQ--WSAEDEEAVqKALKATRMEELAERTVDS---LSGGQRQRAWIAMTLAQETDIILLDEPTTYLD- 171
Cdd:TIGR01271 1313 -----DPYEQWSDEeiWKVAEEVGL-KSVIEQFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLDp 1386
|
....*
gi 521288620 172 MTHQI 176
Cdd:TIGR01271 1387 VTLQI 1391
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
130-227 |
3.45e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 130 EELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYAHH 209
Cdd:PRK11144 119 EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADR 198
|
90
....*....|....*...
gi 521288620 210 LVAIKDKKIYAEGRPESI 227
Cdd:PRK11144 199 VVVLEQGKVKAFGPLEEV 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-172 |
3.87e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 9 LSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAklpTKEVAKELAILPQGPSA 88
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 89 PEGLTVLQLVK-----QGRYPYQnwlkqwsaedeeAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:PRK13543 94 KADLSTLENLHflcglHGRRAKQ------------MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
....*....
gi 521288620 164 DEPTTYLDM 172
Cdd:PRK13543 162 DEPYANLDL 170
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-208 |
4.15e-09 |
|
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: 54.29 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLmkpkggsVLLEGSSIAKlptkevakELAILPQGPSAPEGLT 93
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA-------LGGAQSATRR--------RSGVKAGCIVAAVSAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQLVKQgrypyqnwlkqwsaedeeavqkalkatrmeelaertvdsLSGGQRQRAWIAMTLA----QETDIILLDEPTTY 169
Cdd:cd03227 71 LIFTRLQ---------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRG 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 521288620 170 LDMTHQIEILDLLFELNEHEKRTIVmVLHDLNLACRYAH 208
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADK 149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-170 |
5.26e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE--------VAKELAILPQgpsape 90
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEalengismVHQELNLVLQ------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 gLTVLQLVKQGRYPYQNWLKqwsaeDEEAVQKALKATrMEEL-----AERTVDSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:PRK10982 88 -RSVMDNMWLGRYPTKGMFV-----DQDKMYRDTKAI-FDELdididPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
....*
gi 521288620 166 PTTYL 170
Cdd:PRK10982 161 PTSSL 165
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-234 |
6.70e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 1 MS--AISTETLSLGYGETIIIDELnlTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE 78
Cdd:PRK10938 1 MSslQISQGTFRLSDTKTLQLPSL--TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQ-----GPSAPE---GLTVLQLVkqgrypyqnwlkQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWI 150
Cdd:PRK10938 79 VSDEWQrnntdMLSPGEddtGRTTAEII------------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 151 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNeHEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAEGRPESIINC 230
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
....
gi 521288620 231 KLVQ 234
Cdd:PRK10938 226 ALVA 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-198 |
8.05e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 58 GSVLLEGSSIAKLPTKEVAKELAILPQGPSApEGLTVLQLVKQGRypyqnwlkqwsaED--EEAVQKALKATRMEELAER 135
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK------------EDatREDVKRACKFAAIDEFIES 1343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 136 TVD-----------SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLH 198
Cdd:PTZ00265 1344 LPNkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-187 |
1.30e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSApeGLTVLQLV 98
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST--SLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 KQG-RYPyqnwLKQWSAEDEEAVQKALKAT-RMEEL----AERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 172
Cdd:PRK15112 107 SQIlDFP----LRLNTDLEPEQREKQIIETlRQVGLlpdhASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170
....*....|....*
gi 521288620 173 THQIEILDLLFELNE 187
Cdd:PRK15112 183 SMRSQLINLMLELQE 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-197 |
1.79e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 6 TETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKG---GSVLLEGssiakLPTKEVAK----E 78
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG-----IPYKEFAEkypgE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 79 LAILPQGPSAPEGLTVLQLVKqgrypyqnwlkqWSAEdeeavqkaLKATRMeelaertVDSLSGGQRQRAWIAMTLAQET 158
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLD------------FALR--------CKGNEF-------VRGISGGERKRVSIAEALVSRA 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 521288620 159 DIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVL 197
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL 176
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-199 |
3.19e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 8 TLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGS-SIAklptkEVAKELAILPQgp 86
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLA-----WVNQETPALPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 87 sapeglTVLQLVKQGRYPYQNWLKQWSAEDE--------------EAVQ----KALKATRMEELA------ERTVDSLSG 142
Cdd:PRK10636 79 ------PALEYVIDGDREYRQLEAQLHDANErndghaiatihgklDAIDawtiRSRAASLLHGLGfsneqlERPVSDFSG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 143 GQRQRAWIAMTLAQETDIILLDEPTTYLDmthqieiLDLLFELNEHEKR---TIVMVLHD 199
Cdd:PRK10636 153 GWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqgTLILISHD 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-180 |
3.71e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 16 TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiaklptkevakELAILPQGPSAPEGL--- 92
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTikd 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATrmeELAERTVdSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 172
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKT---VLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*...
gi 521288620 173 THQIEILD 180
Cdd:TIGR01271 582 VTEKEIFE 589
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-182 |
3.85e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 21 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE-VAKELAILPQGPS-------APEGL 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQssglyldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 93 TVLQLVkQGRYPYqnWLKqwSAEDEEAVQKALKATRME-ELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 171
Cdd:PRK15439 361 NVCALT-HNRRGF--WIK--PARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170
....*....|.
gi 521288620 172 MTHQIEILDLL 182
Cdd:PRK15439 436 VSARNDIYQLI 446
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-205 |
4.06e-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: 51.94 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLrslarlmkpkggsvlLEGssIAKLPTKEVAKELailpqgPSAPEGLTVL--Q 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEG--LYASGKARLISFL------PKFSRNKLIFidQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LvkqgrypyqnwlkqwsaedeeavqKALKATRMEELA-ERTVDSLSGGQRQRAWIAMTLAQETD--IILLDEPTTYLdmt 173
Cdd:cd03238 68 L------------------------QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL--- 120
|
170 180 190
....*....|....*....|....*....|....
gi 521288620 174 HQIEILDLLFELNE--HEKRTIVMVLHDLNLACR 205
Cdd:cd03238 121 HQQDINQLLEVIKGliDLGNTVILIEHNLDVLSS 154
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-170 |
4.45e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKL-PTKevAKELAI--LPQGPSAPEGLTVLQ-- 96
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAK--AHQLGIylVPQEPLLFPNLSVKEni 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521288620 97 LVKQGRypyqnwlkqwSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:PRK15439 108 LFGLPK----------RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-201 |
4.50e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVlqlvkqg 101
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TV------- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 102 RYPYQNWLKQWSAEDEEAVQKA-LK-ATRMEEL---AERTV--DSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTH 174
Cdd:PLN03130 1330 RFNLDPFNEHNDADLWESLERAhLKdVIRRNSLgldAEVSEagENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
170 180
....*....|....*....|....*..
gi 521288620 175 QIEILDLLFElnEHEKRTIVMVLHDLN 201
Cdd:PLN03130 1410 DALIQKTIRE--EFKSCTMLIIAHRLN 1434
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-194 |
4.76e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.08 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGeITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLE----GSSIAKLPTKEVAKELA-----ILPQGPSAP 89
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEedfyLGDDPDLPEIEIELTFGsllsrLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 90 EGLTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKATRME-ELAERTVDSLSG-----------------GQRQRAWIA 151
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNELLSEYLKELLDGLDLElELSLDELEDLLKslslriedgkelpldrlGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521288620 152 MTLAQ---------ETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIV 194
Cdd:COG3593 173 LALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-207 |
4.92e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK----GGSVLLEGSSIAKLPTKE----VAKELAIL---PQG-- 85
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRErrklVGHNVSMIfqePQScl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 -PSAPEGLTVLQLVK----QGRYpYQ--NWLKQWSAEDEEAV----QKALKATRMEELAErtvdslsgGQRQRAWIAMTL 154
Cdd:PRK15093 103 dPSERVGRQLMQNIPgwtyKGRW-WQrfGWRKRRAIELLHRVgikdHKDAMRSFPYELTE--------GECQKVMIAIAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACRYA 207
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-176 |
5.04e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 52.93 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGE--TIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKgGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGltvlqLVKQGRYPYQNWLKQ--WSAEDEEAVQKALKATRmEELAERTVDS---LSGGQRQRAWIAMTLAQ 156
Cdd:cd03289 82 IPQKVFIFSG-----TFRKNLDPYGKWSDEeiWKVAEEVGLKSVIEQFP-GQLDFVLVDGgcvLSHGHKQLMCLARSVLS 155
|
170 180
....*....|....*....|.
gi 521288620 157 ETDIILLDEPTTYLD-MTHQI 176
Cdd:cd03289 156 KAKILLLDEPSAHLDpITYQV 176
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-214 |
7.62e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.45 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 31 ITVFIGSNGCGKSTLLR----SLARLMKP--KGG----SVLLEGSSIA------KLPTK---EVAKELAIL------PQG 85
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPnsKGGahdpKLIREGEVRAqvklafENANGkkyTITRSLAILenvifcHQG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 PSapegltvlqlvkqgrypyqNWLkqwsaedeeavqkalkatrmeelAERTVDSLSGGQRQ------RAWIAMTLAQETD 159
Cdd:cd03240 104 ES-------------------NWP-----------------------LLDMRGRCSGGEKVlasliiRLALAETFGSNCG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 160 IILLDEPTTYLDMTH-QIEILDLLFELNEHEKRTIVMVLHDLNLAcRYAHHLVAIK 214
Cdd:cd03240 142 ILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDEELV-DAADHIYRVE 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-200 |
7.67e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKE--------VAKELAILPQgpsape 90
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 91 gLTVLQLVKQGRYPYQNWLK-QWSAEDEEAvQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 169
Cdd:PRK10762 94 -LTIAENIFLGREFVNRFGRiDWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|.
gi 521288620 170 LDMTHQIEILDLLFELNEhEKRTIVMVLHDL 200
Cdd:PRK10762 172 LTDTETESLFRVIRELKS-QGRGIVYISHRL 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-200 |
1.11e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGP---SApeglTV 94
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPflfSD----TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 95 LQLVKQGRyPYQNwlkqwSAEDEEAVQKA--------LKATRMEELAERTVdSLSGGQRQRAWIAMTLAQETDIILLDEP 166
Cdd:PRK10789 406 ANNIALGR-PDAT-----QQEIEHVARLAsvhddilrLPQGYDTEVGERGV-MLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190
....*....|....*....|....*....|....
gi 521288620 167 TTYLDMTHQIEILDLLFELNEHekRTIVMVLHDL 200
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEG--RTVIISAHRL 510
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-198 |
1.31e-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: 50.70 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPKGGSVLLEGssiaKLPTKEVAKELAILPQGPSAPEGLTVL 95
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILING----RPLDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 96 QLVkqgrypyqnwlkQWSAedeeavqkALKAtrmeelaertvdsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ 175
Cdd:cd03232 98 EAL------------RFSA--------LLRG-------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|...
gi 521288620 176 IEILDLLFELNEHeKRTIVMVLH 198
Cdd:cd03232 145 YNIVRFLKKLADS-GQAILCTIH 166
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-198 |
1.65e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.06 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 17 IIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVllegssiaklpTKEVAKELAILPQGPSapegLTVLQ 96
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----------TKPAKGKLFYVPQRPY----MTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRYP---YQNWLKQWSAEDEEAVqkaLKATRMEELAERTV---------DSLSGGQRQRAWIAMTLAQETDIILLD 164
Cdd:TIGR00954 531 LRDQIIYPdssEDMKRRGLSDKDLEQI---LDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 521288620 165 EPTTYLdmthQIEILDLLFELNEHEKRTIVMVLH 198
Cdd:TIGR00954 608 ECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-200 |
1.76e-07 |
|
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: 52.32 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKlPTKEVAKELAILPQGPSAPEGLTvlqlv 98
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLT----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 99 kqGR---YPYQNWLKQWSAEDEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ 175
Cdd:TIGR01257 2029 --GRehlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180
....*....|....*....|....*
gi 521288620 176 IEILDLLFELNEhEKRTIVMVLHDL 200
Cdd:TIGR01257 2107 RMLWNTIVSIIR-EGRAVVLTSHSM 2130
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-198 |
3.33e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETI--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAI 81
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 82 LPQGPSAPEGLTVLQLVKQGRYPYQnwlKQWSAEDEEAVQKALKATR--MEELAERTVDSLSGGQRQRAWIAMTLAQETD 159
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPggLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 521288620 160 IILLDEPTTYLDMTHQiEILDLLFeLNEHEKRTIVMVLH 198
Cdd:cd03288 177 ILIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAH 213
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
35-204 |
4.02e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 35 IGSNGCGKSTLLRSLARLMKPKGGSVLLEgssiaklPTKEVAKelaiLPQGPSAPEGLTVLQLVKQGRypyqnwLKQWSA 114
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGK----LRQDQFAFEEFTVLDTVIMGH------TELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 115 EDE--------EAVQK-ALKATRME-ELAE--------RTVDSLSG-----------------GQRQRAWIAMTLAQETD 159
Cdd:PRK15064 96 KQErdriyalpEMSEEdGMKVADLEvKFAEmdgytaeaRAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521288620 160 IILLDEPTTYLDMtHQIEILDLlfELNEHeKRTIVMVLHD---LNLAC 204
Cdd:PRK15064 176 ILLLDEPTNNLDI-NTIRWLED--VLNER-NSTMIIISHDrhfLNSVC 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-167 |
4.27e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKE-LAILPQGPSApEGL----T 93
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLG-RGLvpdmS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 94 VLQ---LVKQGRYPYQNW-LKQWSAEDEEAVQKalkatrMEELAERT------VDSLSGGQRQRAWIAMTLAQETDIILL 163
Cdd:COG3845 353 VAEnliLGRYRRPPFSRGgFLDRKAIRAFAEEL------IEEFDVRTpgpdtpARSLSGGNQQKVILARELSRDPKLLIA 426
|
....
gi 521288620 164 DEPT 167
Cdd:COG3845 427 AQPT 430
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-235 |
4.90e-07 |
|
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: 50.59 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPK-GGSVLLEGSSIA-KLPTKEVAKELAILPQGPSAPEGLTVLQ 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 97 LVKQGRYPYQNWLKQWSAEDEEAVQKALKATrMEELAERT------VDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 170
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDAAAELQIIGSA-IQRLKVKTaspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 171 DMTHQIEILDLLFELNEhEKRTIVMVLHDLNLACRYAHHLVAIKDKKIYAegrpeSIINCKLVQD 235
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG-----DFVNHALTQE 493
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-238 |
5.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTLLRS-LARLMKPKGGSVLLEGSsiaklptkevakeLAILPQgPSAPEGLTVLQLVKQ 100
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGT-------------VAYVPQ-VSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 101 GRyPYQNwLKQWSAEDEEAVQKALK---ATRMEELAERTVDsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 177
Cdd:PLN03130 702 GS-PFDP-ERYERAIDVTALQHDLDllpGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521288620 178 ILDLLFElNEHEKRTIVMV---LHDLNlacrYAHHLVAIKDKKIYAEGRPESII-NCKLVQDVFE 238
Cdd:PLN03130 779 VFDKCIK-DELRGKTRVLVtnqLHFLS----QVDRIILVHEGMIKEEGTYEELSnNGPLFQKLME 838
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-180 |
6.65e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 49.47 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGssiaklptkevakELAILPQGPSAPEGLTVLQL 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 98 VKQGRYpyqnwlkqwsaeDEEAVQKALKATRMEE------------LAERTVdSLSGGQRQRAWIAMTLAQETDIILLDE 165
Cdd:cd03291 119 IFGVSY------------DEYRYKSVVKACQLEEditkfpekdntvLGEGGI-TLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|....*
gi 521288620 166 PTTYLDMTHQIEILD 180
Cdd:cd03291 186 PFGYLDVFTEKEIFE 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-201 |
1.76e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 20 DELNLTIPKGEITVFIGSNGCGKSTllrslarLMK------PKG---GSVLLEGssiaklptkEVAK------------- 77
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKST-------LMKvlsgvyPHGsyeGEILFDG---------EVCRfkdirdsealgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 78 ----ELAILPQgpsapegLTVLQLVKQGRYPYQNWLKQWSAEDEEAvQKALKATRMEELAERTVDSLSGGQRQRAWIAMT 153
Cdd:NF040905 82 iihqELALIPY-------LSIAENIFLGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521288620 154 LAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHeKRTIVMVLHDLN 201
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLN 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-218 |
2.96e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGY-GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEgssiAKLptkevakELAIL 82
Cdd:PLN03073 509 ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS----AKV-------RMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEGLTVLQLVKQGR-YPyqnwlkqwsAEDEEAVQKALKATRME-ELAERTVDSLSGGQRQRAWIAMTLAQETDI 160
Cdd:PLN03073 578 SQHHVDGLDLSSNPLLYMMRcFP---------GVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521288620 161 ILLDEPTTYLDMThQIEILD---LLFElnehekRTIVMVLHDLNLACRYAHHLVAIKDKKI 218
Cdd:PLN03073 649 LLLDEPSNHLDLD-AVEALIqglVLFQ------GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-182 |
4.37e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.91 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGE-ITVFIGSNGCGKSTLLRSLA--------RLMKPKGGSVLL-------EGSSIA------KLPTKEVA 76
Cdd:COG3950 14 FEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIAlalsgllsRLDDVKFRKLLIrngefgdSAKLILyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 77 KELAILPQGPSAPEGLT-----------VLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKA------------------T 127
Cdd:COG3950 94 KLERLKEEYFSRLDGYDslldedsnlreFLEWLREYLEDLENKLSDELDEKLEAVREALNKllpdfkdiridrdpgrlvI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 128 RMEELAERTVDSLSGGQRQR----AWIAMTLAQ---------ETD-IILLDEPTTYLDMTHQIEILDLL 182
Cdd:COG3950 174 LDKNGEELPLNQLSDGERSLlalvGDLARRLAElnpalenplEGEgIVLIDEIDLHLHPKWQRRILPDL 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-198 |
6.16e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 14 GETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLArlmKPKGGSVLLEGSSIAKLPTKEVAKELAI--LPQGPSAPEG 91
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA---ERVTTGVITGGDRLVNGRPLDSSFQRSIgyVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 92 LTVLQLVKqgrypYQNWLKQWS----AEDEEAVQKALKATRMEELAERTV----DSLSGGQRQRAWIAMTLAQETDIIL- 162
Cdd:TIGR00956 851 STVRESLR-----FSAYLRQPKsvskSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*.
gi 521288620 163 LDEPTTYLDMTHQIEILDLLFELNEHeKRTIVMVLH 198
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-201 |
6.69e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPKGGSVLLEGSS--IA-------KLP--------------TKEV 75
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAalIAissglngQLTgienielkglmmglTKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 76 AKElaILPQgpsapegltVLQLVKQGRYPYQnwlkqwsaedeeavqkalkatrmeelaerTVDSLSGGQRQRAWIAMTLA 155
Cdd:PRK13545 120 IKE--IIPE---------IIEFADIGKFIYQ-----------------------------PVKTYSSGMKSRLGFAISVH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKrTIVMVLHDLN 201
Cdd:PRK13545 160 INPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLS 204
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
19-59 |
2.58e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 44.37 E-value: 2.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 521288620 19 IDELNLTIPkgeITVFIGSNGCGKSTLLRSLARLM--KPKGGS 59
Cdd:COG3910 30 LEGLEFHPP---VTFFVGENGSGKSTLLEAIAVAAgfNPEGGS 69
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
23-52 |
3.08e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 3.08e-05
10 20 30
....*....|....*....|....*....|
gi 521288620 23 NLTIPKGEITVFIGSNGCGKSTLLRSLARL 52
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
124-227 |
3.73e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 124 LKATRMEELAERTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELnEHEKRTIVMVLHDLNLA 203
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEA 207
|
90 100
....*....|....*....|....
gi 521288620 204 CRYAHHLVAIKDKKIYAEGRPESI 227
Cdd:NF000106 208 EQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-172 |
4.18e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 4 ISTETLSLGYGETIIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLArlMKPKGGsvLLEGSSIAKLPTKEVAKELAILP 83
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG--IPKNCQILHVEQEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 84 QGPSAPEGLTVL-----QLVKQGR-YPYQNWLKQWSAEDEEAVQKALKATRMEEL-----------AE------------ 134
Cdd:PLN03073 254 CVLNTDIERTQLleeeaQLVAQQReLEFETETGKGKGANKDGVDKDAVSQRLEEIykrlelidaytAEaraasilaglsf 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521288620 135 ------RTVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 172
Cdd:PLN03073 334 tpemqvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-177 |
4.53e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 35 IGSNGCGKSTLLRSLARLMKPKGGSVLLEGSSIAKLPTKEVAKELAILPQGPSAPEGlTVLQLVKqgryPYqnwLKQWSA 114
Cdd:PTZ00243 1342 VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD----PF---LEASSA 1413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521288620 115 EdeeaVQKALKATRM-EELAERT--VDS--LSG------GQRQRAWIAMTLAQE-TDIILLDEPTTYLD--MTHQIE 177
Cdd:PTZ00243 1414 E----VWAALELVGLrERVASESegIDSrvLEGgsnysvGQRQLMCMARALLKKgSGFILMDEATANIDpaLDRQIQ 1486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
136-195 |
6.27e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 6.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 136 TVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVM 195
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
26-127 |
1.22e-04 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 41.98 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 26 IPKGEITVFIGSNGCGKSTLLRSLA-----------RLMKPKGGSVLL---EGssiaklPTKEVAKELAILPQGPSAPEG 91
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVLYvsaEG------PADELRRRLRAAGADLDLPAR 103
|
90 100 110
....*....|....*....|....*....|....*.
gi 521288620 92 LTVLQLVKQGRYPYQNWLKQWSAEDEEAVQKALKAT 127
Cdd:pfam13481 104 LLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEV 139
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
19-219 |
2.92e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.49 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 19 IDELNLTIpkGEITVFIGSNGCGKSTLLRSLARLMKPK--------------GGSVLLEGSSIAKL--PTKEVAKELAIL 82
Cdd:COG4938 12 FKEAELEL--KPLTLLIGPNGSGKSTLIQALLLLLQSNfiylpaersgparlYPSLVRELSDLGSRgeYTADFLAELENL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 83 PQGPSAPEgltvlQLVKQgrypYQNWLKQWSAE----DEEAVQKALKATRMEELAERTVDSLSGGQRQRAWIAMTL---A 155
Cdd:COG4938 90 EILDDKSK-----ELLEQ----VEEWLEKIFPGkvevDASSDLVRLVFRPSGNGKRIPLSNVGSGVSELLPILLALlsaA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521288620 156 QETDIILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIV-----MVLHDLNLACrYAHHLVAIKDKKIY 219
Cdd:COG4938 161 KPGSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIethsdYILNGLRNLI-KEGKLLDPDDVAVY 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-196 |
3.62e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 18 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSL-----ARlmkpKGGSVLLEGSSIA-KLPTKEVAKELAILP-----QG- 85
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR----WEGEIFIDGKPVKiRNPQQAIAQGIAMVPedrkrDGi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 86 -PSAPEG----LTVLQlvkqgRYpyqnwlKQWSAEDEEAVQKALKaTRMEELAERT------VDSLSGGQRQRAWIAMTL 154
Cdd:PRK13549 353 vPVMGVGknitLAALD-----RF------TGGSRIDDAAELKTIL-ESIQRLKVKTaspelaIARLSGGNQQKAVLAKCL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521288620 155 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEhEKRTIVMV 196
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVI 461
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-213 |
3.89e-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: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 22 LNLTIPKGEITVFIGSNGCGKSTL----------------LRSLAR-----LMKPKGGSVllEGSSIAklptkeVAKELA 80
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqflgqMDKPDVDSI--EGLSPA------IAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 81 ILPQGPSAPEGlTVLQLvkqgrYPYQNWLkqWSAEDEEAVQKALKATRMEELA-ERTVDSLSGGQRQRAWIAMTL-AQET 158
Cdd:cd03270 86 TTSRNPRSTVG-TVTEI-----YDYLRLL--FARVGIRERLGFLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIgSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 159 DII-LLDEPTTYLDMTHQIEILDLLFELNEHeKRTIVMVLHDLNLAcRYAHHLVAI 213
Cdd:cd03270 158 GVLyVLDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHDEDTI-RAADHVIDI 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-215 |
2.43e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 135 RTVDSLSGGQRQRAWIAMTL---AQETDIILLDEPTTYLDmTHQIEIL-DLLFELNeHEKRTIVMVLHDLnlacryahHL 210
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH-THDIKALiYVLQSLT-HQGHTVVIIEHNM--------HV 874
|
....*
gi 521288620 211 VAIKD 215
Cdd:PRK00635 875 VKVAD 879
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
28-50 |
7.17e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 7.17e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-215 |
7.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 37.71 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521288620 138 DSLSGGQRQ------RAWIAMTLAQETD------IILLDEPTTYLDMTHQIEILDLLFELNEHEKRTIVMVLHDLNLACR 205
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDELVGA 859
|
90
....*....|.
gi 521288620 206 yAHHLVAI-KD 215
Cdd:PRK02224 860 -ADDLVRVeKD 869
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-52 |
7.26e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 7.26e-03
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
29-80 |
8.30e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 36.53 E-value: 8.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 521288620 29 GEITVFIGSNGCGKSTLLRSLARLMKPKGGSVL----LEGSSIAKLPTKEVAKELA 80
Cdd:pfam01637 20 NLIYVIYGPEGCGKTALLRESIENLLDLGYYVIyydpLRRYFISKLDRFEEVRRLA 75
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
18-61 |
8.62e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 37.19 E-value: 8.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 521288620 18 IIDELnltIPKGEITVFIGSNGCGKSTLLRSLARL---------MKPKGGSVL 61
Cdd:COG3598 5 LVPGL---LPEGGVTLLAGPPGTGKSFLALQLAAAvaaggpwlgRRVPPGKVL 54
|
|
| |
