|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-226 |
1.30e-126 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 357.05 E-value: 1.30e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARG 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVN 163
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-224 |
9.95e-119 |
|
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: 337.02 E-value: 9.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-224 |
1.24e-113 |
|
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: 323.67 E-value: 1.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-227 |
3.87e-103 |
|
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: 297.81 E-value: 3.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGL 84
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFVYQFHHLLPEFTALENVCMPL-LIGRtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVN 163
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLeLAGR---RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIAA 227
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-224 |
1.36e-100 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 291.33 E-value: 1.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETA 81
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL 161
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-225 |
5.01e-82 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 243.81 E-value: 5.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLL 85
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RnRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRsLQTSFLVVTHDLQLAGHMD-RILRLEEGRLI 225
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-226 |
3.81e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 235.37 E-value: 3.81e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MN-DKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNe 79
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 targllrnRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIAR 159
Cdd:COG1116 80 --------PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 160 ALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ----LAghmDRILRLEE--GRLIA 226
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfLA---DRVVVLSArpGRIVE 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-226 |
3.80e-74 |
|
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: 223.89 E-value: 3.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnetargllR 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEE--GRLIA 226
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLaDRVVVLSArpGRIVA 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-224 |
5.22e-73 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 221.19 E-value: 5.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-225 |
1.07e-69 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 213.38 E-value: 1.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGL 84
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRaLGFVYQFHHLLPEFTALENVCMPLLiGRTPI---------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVLAGRL-GRTSTwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA-GHMDRILRLEEGRLI 225
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRVV 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-226 |
1.82e-68 |
|
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: 218.23 E-value: 1.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDE-GPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET 80
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVA 156
Cdd:COG1123 336 SLRELR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRIVE 485
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-226 |
2.27e-68 |
|
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: 209.84 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETAR 82
Cdd:COG1127 2 SEPMIEVRNLTKSFG----DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRNRaLGFVYQFHHLLPEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL 161
Cdd:COG1127 78 YELRRR-IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIaDRVAVLADGKIIA 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-225 |
7.74e-68 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 212.27 E-value: 7.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NEt 80
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppEK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 argllrnRALGFVYQ----FHHLlpefTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVA 156
Cdd:COG3842 77 -------RNVGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHD----LQLAghmDRILRLEEGRLI 225
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLALA---DRIAVMNDGRIE 215
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-224 |
8.40e-68 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 207.56 E-value: 8.40e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RnRALGFVYQFHHLLPEFTALENVCMPL-LIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-226 |
1.30e-67 |
|
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: 206.99 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEtargllRNRA 89
Cdd:cd03259 4 KGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQ 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-225 |
6.26e-67 |
|
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: 205.82 E-value: 6.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRaLGFVYQ--FHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLG---HRLSHKPAELSGGERQRVAIARA 160
Cdd:cd03257 81 RKE-IQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-225 |
9.96e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 205.61 E-value: 9.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlNETARGLL 85
Cdd:COG1126 1 MIEIENLHKSFG----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRaLGFVYQFHHLLPEFTALENVCM-PLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMT-MVVVTHEMGFAREVaDRVVFMDGGRIV 215
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
10-225 |
1.09e-65 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 206.08 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRA 89
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR-RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL----QLAghmDRILRLEEGRLI 225
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMdvvrRIC---DRVAVLENGRIV 220
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-223 |
2.14e-65 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 201.32 E-value: 2.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRA 89
Cdd:TIGR02673 5 HNVSKAY---PGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHMD-RILRLEEGR 223
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-225 |
4.30e-65 |
|
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: 201.27 E-value: 4.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRA 89
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR-RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVV 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-226 |
1.29e-63 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 208.81 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGL 84
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHT-VIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-226 |
1.74e-62 |
|
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: 195.02 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSalneTARGLLR 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT----RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQ-----FHhllPEFTALENVCMPLLIGRtpIAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARA 160
Cdd:COG1124 78 RRRVQMVFQdpyasLH---PRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVE 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-225 |
5.57e-61 |
|
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: 191.24 E-value: 5.57e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLR 86
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQFHHLLPEFTALENVCMPLLiGRTPI---------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRL-GRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA-GHMDRILRLEEGRLI 225
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRIV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-227 |
6.58e-61 |
|
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: 190.79 E-value: 6.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLR 86
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQFHHLLPEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:cd03261 77 RR-MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAE 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-224 |
1.69e-60 |
|
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: 188.89 E-value: 1.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdeGPQsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlNETARGLLR 86
Cdd:cd03262 1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQFHHLLPEFTALENVCMPLLIGR-TPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLAPIKVKgMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMT-MVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-224 |
5.50e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 191.82 E-value: 5.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlr 86
Cdd:COG3839 4 LELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nralGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:COG3839 78 ----AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 167 LVLLDEPTGNLDQHT-AQGIQELMlELSRSLQTSFLVVTHD----LQLAghmDRILRLEEGRL 224
Cdd:COG3839 154 VFLLDEPLSNLDAKLrVEMRAEIK-RLHRRLGTTTIYVTHDqveaMTLA---DRIAVMNDGRI 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-226 |
6.37e-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: 185.23 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRAlGFVYQFhhllPE---F--TALENVCMPLL-IGRTPiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:COG1122 75 RKV-GLVFQN----PDdqlFapTVEEDVAFGPEnLGLPR-EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLA-GHMDRILRLEEGRLIA 226
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVaELADRVIVLDDGRIVA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-226 |
1.59e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.50 E-value: 1.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEFTALENVcmpLLIGR---TPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVN 163
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENL---RFFARlygLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLcDRVAIIDKGRIVA 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-219 |
4.94e-57 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 179.73 E-value: 4.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET-ARGLLRNRa 89
Cdd:TIGR03608 3 NISKKF----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkASKFRREK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHMDRILRL 219
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHDPEVAKQADRVIEL 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-227 |
7.48e-57 |
|
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: 181.01 E-value: 7.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGll 85
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVYQFHHLLPEFTALENVcmplLIGRTP--------IAEARQRAAELLERVGLGHrLSHKP-AELSGGERQRVA 156
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELV----ALGRYPhlglfgrpSAEDREAVEEALERTGLEH-LADRPvDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAG-HMDRILRLEEGRLIAA 227
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAArYADRLVLLKDGRIVAQ 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-224 |
1.13e-56 |
|
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: 179.74 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlr 86
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nralGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03300 75 ----NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMsDRIAVMNKGKI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-223 |
3.75e-56 |
|
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: 177.66 E-value: 3.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 8 SCRNLSKSYDEGPQsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllrn 87
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RALGFVYQFhhllPE---FT---------ALENVCMPlligrtpIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:cd03225 75 RKVGLVFQN----PDdqfFGptveeevafGLENLGLP-------EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQ-LAGHMDRILRLEEGR 223
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-226 |
1.17e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 180.73 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlNETARgllr 86
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT-NLPPR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQfHHLL-PEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:COG1118 74 ERRVGFVFQ-HYALfPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHD----LQLAghmDRILRLEEGRLIA 226
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeaLELA---DRVVVMNQGRIEQ 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-217 |
1.92e-55 |
|
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: 179.48 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTP---SAGSVWLAGEELSALNETAR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRNRALGFVYQ--FHHLLPEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGL---GHRLSHKPAELSGGERQRVA 156
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 157 IARALVNRPQLVLLDEPTGNLD---QhtAQgIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRIL 217
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDvtiQ--AQ-ILNLLKDLQRELGLAILFITHDLGVVAEIaDRVA 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
10-224 |
2.27e-55 |
|
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: 176.06 E-value: 2.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRA 89
Cdd:cd03292 4 INVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 170 LDEPTGNLDQHTAQGIQELMlELSRSLQTSFLVVTHDLQL-AGHMDRILRLEEGRL 224
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-226 |
2.28e-54 |
|
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: 181.64 E-value: 2.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGPqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSA---GSVWLAGEELSALNET 80
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGllrnRALGFVYQ--FHHLLPEfTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:COG1123 80 LRG----RRIGMVFQdpMTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVE 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
7-224 |
1.25e-53 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 171.44 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLR 86
Cdd:NF038007 2 LNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:NF038007 82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:NF038007 162 LLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-210 |
4.08e-53 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 171.58 E-value: 4.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsalneTARGL 84
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRnralGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:COG4525 77 DR----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA 210
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-224 |
5.83e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.65 E-value: 5.83e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnet 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 argllRNRALGFVYQFHHLLPEF--TALENVCMPLL----IGRTPIAEARQRAAELLERVGLGHrLSHKP-AELSGGERQ 153
Cdd:COG1121 73 -----ARRRIGYVPQRAEVDWDFpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLED-LADRPiGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDL-QLAGHMDRILRLEEGRL 224
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLgAVREYFDRVLLLNRGLV 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-224 |
7.72e-53 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 169.67 E-value: 7.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 12 LSKSYDEGPQSVQvlsGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRALG 91
Cdd:PRK10908 7 VSKAYLGGRQALQ---GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 92 FVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLD 171
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598183 172 EPTGNLDQHTAQGIQELMLELSRsLQTSFLVVTHDLQLAGHMD-RILRLEEGRL 224
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
1.60e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.46 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:COG4619 1 LELEGLSFRVGGKP----ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEfTALENVCMPLLIGRTPIAeaRQRAAELLERVGLGHRLSHKPA-ELSGGERQRVAIARALVNRP 165
Cdd:COG4619 74 -RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-226 |
1.84e-52 |
|
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: 169.83 E-value: 1.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNE---TA 81
Cdd:COG0411 3 PLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLLRnralgfVYQFHHLLPEFTALENVCMPLLIG---------------RTPIAEARQRAAELLERVGLGHRLSHKPAE 146
Cdd:COG0411 79 LGIAR------TFQNPRLFPELTVLENVLVAAHARlgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQL-AGHMDRILRLEEGRLI 225
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLvMGLADRIVVLDFGRVI 232
|
.
gi 15598183 226 A 226
Cdd:COG0411 233 A 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
10-225 |
3.11e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 171.91 E-value: 3.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRA 89
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRIcDRVAVIDAGRLV 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-223 |
5.11e-52 |
|
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: 166.21 E-value: 5.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARglLRNRA 89
Cdd:cd03229 4 KNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELP--PLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLligrtpiaearqraaellervglghrlshkpaelSGGERQRVAIARALVNRPQLVL 169
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGR 223
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-227 |
1.16e-51 |
|
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: 175.34 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQFHHLlpeF--TALENvcmpLLIGRTPIAEARQRAAelLERVGLGHRLSHKP-----------AELSGGERQ 153
Cdd:COG4987 409 RR-IAVVPQRPHL---FdtTLREN----LRLARPDATDEELWAA--LERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGRLIAA 227
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-227 |
1.40e-50 |
|
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: 172.64 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArgl 84
Cdd:COG4988 335 PSIELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 lRNRALGFVYQFHHLLPEfTALENvcmpLLIGRTPIAEARQRAAelLERVGLGHRLSHKP-----------AELSGGERQ 153
Cdd:COG4988 409 -WRRQIAWVPQNPYLFAG-TIREN----LRLGRPDASDEELEAA--LEAAGLDEFVAALPdgldtplgeggRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsfLVVTHDLQLAGHMDRILRLEEGRLIAA 227
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-224 |
1.64e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.50 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgLLRNRA 89
Cdd:PRK09493 5 KNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 lGFVYQFHHLLPEFTALENVCM-PLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLV 168
Cdd:PRK09493 80 -GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 169 LLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMT-MVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-225 |
2.07e-50 |
|
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: 165.12 E-value: 2.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVL-------------SG-------VELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGS 66
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLlakgkskeeilkkTGqtvgvndVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 67 VWLAGEELSALNETARGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAE 146
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLV 240
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
10-225 |
3.03e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 165.65 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRA 89
Cdd:COG1125 5 ENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LR-RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCM-PLLIGrTPIAEARQRAAELLERVGL-----GHRlshKPAELSGGERQRVAIARALVN 163
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATvPRLLG-WDKERIRARVDELLELVGLdpeeyRDR---YPHELSGGQQQRVGVARALAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG1125 154 DPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLgDRIAVMREGRIV 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-223 |
1.11e-49 |
|
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: 159.86 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEfTALENVcmplligrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARALVNRPQ 166
Cdd:cd03228 76 -KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGR 223
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-226 |
1.30e-49 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 161.84 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETAR-G 83
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLppHEIARlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRnralgfVYQFHHLLPEFTALENVCMPLLIG----------RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQ 153
Cdd:cd03219 77 IGR------TFQIPRLFPELTVLENVMVAAQARtgsglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQL-AGHMDRILRLEEGRLIA 226
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVvMSLADRVTVLDQGRVIA 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
10-225 |
1.29e-48 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 158.88 E-value: 1.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGL-----DTPSAGSVWLAGEELSALNETaRGL 84
Cdd:cd03260 4 RDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD-VLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRnRALGFVYQFHHLLPeFTALENVCMPL-LIGRTPIAEARQRAAELLERVGLGHRLSHK--PAELSGGERQRVAIARAL 161
Cdd:cd03260 79 LR-RRVGMVFQKPNPFP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVaDRTAFLLNGRLV 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-226 |
1.44e-48 |
|
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: 159.25 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllrnRA 89
Cdd:COG4555 5 ENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-----RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVA 212
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-225 |
2.46e-48 |
|
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: 159.00 E-value: 2.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLL 85
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRaLGFVYQFHHLLPEFTALENVCMPLL---------IGRTPIAEaRQRAAELLERVGLGHRLSHKPAELSGGERQRVA 156
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLgykptwrslLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA-GHMDRILRLEEGRLI 225
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAkKYADRIVGLKAGEIV 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-225 |
1.50e-47 |
|
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: 156.69 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVQVLSgveLNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRA 89
Cdd:cd03295 4 ENVTKRYGGGKKAVNNLN---LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LR-RK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCM-PLLIGrTPIAEARQRAAELLERVGL--GHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALvPKLLK-WPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLaDRIAIMKNGEIV 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-227 |
1.66e-47 |
|
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: 156.34 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEtargllR 86
Cdd:cd03299 1 LKVENLSKDWKEF-----KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQV 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-223 |
1.76e-47 |
|
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: 156.06 E-value: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKS---YDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWL--AGEELSALNET 80
Cdd:COG4778 4 LLEVENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGL--LRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSH-KPAELSGGERQRVAI 157
Cdd:COG4778 84 PREIlaLRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDL----QLAghmDRILRLEEGR 223
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEevreAVA---DRVVDVTPFS 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-225 |
2.51e-47 |
|
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: 157.23 E-value: 2.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNR 88
Cdd:TIGR04521 4 KNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 89 aLGFVYQF-HHLLPEFTALENVCM-PLLIGRTPiAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARALVNRP 165
Cdd:TIGR04521 84 -VGLVFQFpEHQLFEETVYKDIAFgPKNLGLSE-EEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 166 QLVLLDEPTGNLDqhtAQGIQELM---LELSRSLQTSFLVVTHDL-QLAGHMDRILRLEEGRLI 225
Cdd:TIGR04521 162 EVLILDEPTAGLD---PKGRKEILdlfKRLHKEKGLTVILVTHSMeDVAEYADRVIVMHKGKIV 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-225 |
2.81e-47 |
|
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: 163.32 E-value: 2.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKS-TLLNMLGGLDTPSA---GSVWLAGEELSA 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 77 LNETARGLLRNRALGFVYQfhhllpE-FTALeNvcmPLL-IGRTpIAE------------ARQRAAELLERVGL---GHR 139
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQ------EpMTSL-N---PLHtIGKQ-IAEvlrlhrglsgaaARARALELLERVGIpdpERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 140 LSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILR 218
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFaDRVAV 229
|
....*..
gi 15598183 219 LEEGRLI 225
Cdd:COG4172 230 MRQGEIV 236
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
5.71e-47 |
|
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: 152.42 E-value: 5.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllrnRALGFVYQFHHLLPEFTA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR----KEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 106 LENVCMPLLIGRTPIAEARQRAAELLERVGLGH----RLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-216 |
7.52e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 157.59 E-value: 7.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYD-------EGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEE 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 74 LSALNETARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGLG----HRLSHkpaE 146
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRpehaDRYPH---E 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLD---QhtAQgIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRI 216
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDvsiQ--AQ-VLNLLEDLQDELGLTYLFISHDLSVVRHIsDRV 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-224 |
7.76e-47 |
|
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: 153.95 E-value: 7.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlrnra 89
Cdd:cd03301 4 ENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 lGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:cd03301 75 -AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMaDRIAVMNDGQI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-226 |
9.62e-47 |
|
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: 153.84 E-value: 9.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSalnetarglLRNRAL 90
Cdd:cd03235 4 DLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE---------KERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEF--TALENVCMPLL----IGRTPIAEARQRAAELLERVGLGHrLSHKP-AELSGGERQRVAIARALVN 163
Cdd:cd03235 71 GYVPQRRSIDRDFpiSVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDL-QLAGHMDRILRLeEGRLIA 226
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLgLVLEYFDRVLLL-NRTVVA 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-223 |
1.96e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 157.80 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEt 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 argllRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK09452 84 -----ENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGR 223
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMsDRIVVMRDGR 222
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
11-227 |
3.65e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 153.03 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetarglLRNRAL 90
Cdd:TIGR00968 5 NISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 171 DEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:TIGR00968 155 DEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVaDRIVVMSNGKIEQI 212
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-227 |
4.20e-46 |
|
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: 152.06 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 34 LPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelSALNETARGLL---RNRALGFVYQFHHLLPEFTALENVC 110
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKINlppQQRKIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 111 MPLLIGRTpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELML 190
Cdd:cd03297 98 FGLKRKRN--REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598183 191 ELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
10-225 |
4.48e-46 |
|
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: 152.88 E-value: 4.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetarglLRNRA 89
Cdd:cd03296 6 RNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLI----GRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHD----LQLAghmDRILRLEEGRLI 225
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqeeaLEVA---DRVVVMNKGRIE 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-226 |
1.97e-45 |
|
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: 160.38 E-value: 1.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLR 86
Cdd:COG2274 474 IELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEfTALENVCMplliGRTPIAEAR-QRAAE---LLERV-----GLGHRLSHKPAELSGGERQRVAI 157
Cdd:COG2274 549 -RQIGVVLQDVFLFSG-TIRENITL----GDPDATDEEiIEAARlagLHDFIealpmGYDTVVGEGGSNLSGGQRQRLAI 622
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-227 |
4.96e-45 |
|
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: 153.33 E-value: 4.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 29 VELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsALNETARGL---LRNRALGFVYQFHHLLPEFTA 105
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIflpPHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 106 LENvcmpLLIG--RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQ 183
Cdd:COG4148 95 RGN----LLYGrkRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598183 184 GIQELMLELSRSLQTSFLVVTHDL----QLAghmDRILRLEEGRLIAA 227
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLdevaRLA---DHVVLLEQGRVVAS 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
35-226 |
9.18e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.13 E-value: 9.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlrnralGFVYQFHHLLPEFTALENVCMPLL 114
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV------SMLFQENNLFPHLTVAQNIGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 115 IGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALV-NRPqLVLLDEPTGNLDQHTAQGIQELMLELS 193
Cdd:COG3840 98 PGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180 190
....*....|....*....|....*....|....
gi 15598183 194 RSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIaDRVLLVADGRIAA 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-225 |
1.17e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELS---ALNETARGLLRn 87
Cdd:COG4161 7 NINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RALGFVYQFHHLLPEFTALENVC-MPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 167 LVLLDEPTGNLDQH-TAQgIQELMLELSRSLQTSfLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG4161 162 VLLFDEPTAALDPEiTAQ-VVEIIRELSQTGITQ-VIVTHEVEFARKVaSQVVYMEKGRII 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-227 |
1.44e-44 |
|
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: 147.20 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 8 SCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArgllRN 87
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RALGFVYQfhhllpeftalenvcmplligrtpiaearqraaeLLERVGLGHrLSHKP-AELSGGERQRVAIARALVNRPQ 166
Cdd:cd03214 73 RKIAYVPQ----------------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQ 179
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-224 |
3.78e-44 |
|
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: 150.34 E-value: 3.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 41 IVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEtargllRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPI 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 121 AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSF 200
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*
gi 15598183 201 LVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:TIGR01187 155 VFVTHDQEEAMTMsDRIAIMRKGKI 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-225 |
5.91e-44 |
|
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: 154.07 E-value: 5.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYD-------EGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSAGSVWLAGEELSALN 78
Cdd:COG4172 275 LLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPLLIGRTPI--AEARQRAAELLERVGLGHRLSHK-PAELSGGERQ 153
Cdd:COG4172 354 RRALRPLR-RRMQVVFQdpFGSLSPRMTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDPAARHRyPHEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALaHRVMVMKDGKVV 505
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-223 |
7.85e-44 |
|
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: 146.08 E-value: 7.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVYQFHHLLPEFTALENVCMplLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:COG4133 75 --RRLAYLGHADGLKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHmDRILRLEEGR 223
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELAA-ARVLDLGDFK 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
4.15e-43 |
|
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: 142.92 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEFTALENVcmplligrtpiaearqraaellervglghrlshkpaELSGGERQRVAIARALVNRPQ 166
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-226 |
4.17e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.04 E-value: 4.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeeLSALNETARGLLR 86
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRAlGFVYQFhhllPE--FTA----------LENVCMPLligrtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQR 154
Cdd:TIGR04520 77 KKV-GMVFQN----PDnqFVGatveddvafgLENLGVPR-------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-225 |
4.18e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 4.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSA---LNETa 81
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLLRN--RALGFVYQFHHLLPEFTALENVCM-PLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK11264 77 KGLIRQlrQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVaDRAIFMDQGRIV 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-225 |
5.06e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 143.29 E-value: 5.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEG-----PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNE 79
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 TARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPL--LIGRTPiAEARQRAAELLERVGLGHRLSHK-PAELSGGERQR 154
Cdd:PRK10419 82 AQRKAFR-RDIQMVFQdsISAVNPRKTVREIIREPLrhLLSLDK-AERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQIV 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-227 |
7.13e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.56 E-value: 7.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALneTARGLLR 86
Cdd:COG4559 2 LEAENLSVRLG----GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW--SPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALgfVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALV---- 162
Cdd:COG4559 76 RRAV--LPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 163 ---NRPQLVLLDEPTGNLD---QHTaqgiqelMLELSRSL---QTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDlahQHA-------VLRLARQLarrGGGVVAVLHDLNLAAQYaDRILLLHQGRLVAQ 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
2.99e-41 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 141.22 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGE-----ELS 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 76 ALNETARGLLRNRALGFVYQfhH----LLPEFTALENVCMPLL-IGRTPIAEARQRAAELLERVGLG-HRLSHKPAELSG 149
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQ--HprdgLRMQVSAGGNIGERLMaVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 150 GERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLaHRLLVMKQGRVV 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-222 |
3.82e-41 |
|
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: 139.91 E-value: 3.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsalneTARGLLRNralgFVYQFHHLLPEFTA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-----TEPGPDRM----VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 106 LENVCMPL--LIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQ 183
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598183 184 GIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEG 222
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLsDRVVMLTNG 191
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
11-225 |
4.21e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 142.91 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGPqsvqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlrnral 90
Cdd:NF040840 6 NLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:NF040840 75 AYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 171 DEPTGNLDQHTAqgiQELMLELSR---SLQTSFLVVTHD----LQLAghmDRILRLEEGRLI 225
Cdd:NF040840 155 DEPLSALDVQTR---DELIREMKRwhrEFGFTAIHVTHNfeeaLSLA---DRVGIMLNGRLS 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-226 |
5.02e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.85 E-value: 5.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRA 89
Cdd:COG1132 343 ENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LR-RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLpEFTALENvcmpLLIGRTPI--AEARQ--RAAELLERV-----GLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:COG1132 416 IGVVPQDTFLF-SGTIREN----IRYGRPDAtdEEVEEaaKAAQAHEFIealpdGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFlVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTI-VIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-227 |
5.33e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.29 E-value: 5.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALneTARGLL 85
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW--SPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRALgfVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHrLSHKP-AELSGGERQRVAIARALV-- 162
Cdd:PRK13548 76 RRRAV--LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAH-LAGRDyPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 163 ----NRPQLVLLDEPTGNLD-QHtaqgiQELMLELSRSL----QTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDlAH-----QHHVLRLARQLaherGLAVIVVLHDLNLAARYaDRIVLLHQGRLVAD 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
36-227 |
8.72e-41 |
|
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: 138.39 E-value: 8.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 36 GERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllrnrALGFVYQFHHLLPEFTALENVCMPLLI 115
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR------PVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 116 GRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRS 195
Cdd:cd03298 98 GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAE 177
|
170 180 190
....*....|....*....|....*....|...
gi 15598183 196 LQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03298 178 TKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQ 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-224 |
1.22e-40 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 139.43 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwLAGEE-LSALNETARgll 85
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTApLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnralgFVYQFHHLLPEFTALENVCMPLLigrtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:PRK11247 85 ------LMFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
2.74e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 2.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYdeGPqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETAR 82
Cdd:COG1129 1 AEPLLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 gllrnRALG--FVYQFHHLLPEFTALENVCMPLLIGRTPI---AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:COG1129 77 -----QAAGiaIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDL----QLAghmDRI--LRleEGRLIA 226
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLdevfEIA---DRVtvLR--DGRLVG 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-222 |
3.21e-40 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 140.99 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEtargllRNRAL 90
Cdd:PRK10851 7 NIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEFTALENVCMPLLI----GRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 167 LVLLDEPTGNLDqhtAQGIQEL---MLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEG 222
Cdd:PRK10851 157 ILLLDEPFGALD---AQVRKELrrwLRQLHEELKFTSVFVTHDQEEAMEVaDRVVVMSQG 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-225 |
4.21e-40 |
|
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: 138.40 E-value: 4.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEG-----PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNE 79
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 TARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPLL-IGRTPIAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRV 155
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKlPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFcQRVAVMDKGQIV 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-223 |
6.69e-40 |
|
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: 134.29 E-value: 6.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 8 SCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLRN 87
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RaLGFVYQfhhllpeftalenvcmplligrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARALVNRPQL 167
Cdd:cd00267 74 R-IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 168 VLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGH-MDRILRLEEGR 223
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELaADRVIVLKDGK 157
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-225 |
6.99e-40 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 140.74 E-value: 6.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDeGPQSVQvlsGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETargll 85
Cdd:PRK11607 19 LLEIRNLTKSFD-GQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:PRK11607 90 -QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMaGRIAIMNRGKFV 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-221 |
1.70e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 134.92 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQsvqvLSGVELNLLPGERVAIVGSSGSGKSTLLN-MLGGLDTP--SAGSVWLAGEELSALNETARG 83
Cdd:COG4136 2 LSLENLTITLGGRPL----LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LlrnralGFVYQFHHLLPEFTALENVC--MPLLIGRtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL 161
Cdd:COG4136 78 I------GILFQDDLLFPHLSVGENLAfaLPPTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEE 221
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-213 |
1.83e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 136.37 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnetaRGLLR 86
Cdd:PRK11248 2 LQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nralGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:PRK11248 73 ----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM 213
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFM 195
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-212 |
1.95e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.17 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYD------EGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNE 79
Cdd:PRK11308 5 LLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 TARGLLRnRALGFVYQ--FHHLLPEFTALENVCMPLLIGRT-PIAEARQRAAELLERVGLghRLSHK---PAELSGGERQ 153
Cdd:PRK11308 85 EAQKLLR-QKIQIVFQnpYGSLNPRKKVGQILEEPLLINTSlSAAERREKALAMMAKVGL--RPEHYdryPHMFSGGQRQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGH 212
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEH 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-227 |
4.35e-39 |
|
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: 134.42 E-value: 4.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeeLSALNETARglLRnRAL 90
Cdd:cd03265 5 NLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPRE--VR-RRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 171 DEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAE 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-227 |
1.45e-38 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 133.67 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAG-SVWLAGEELSALN--Eta 81
Cdd:COG1119 2 PLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvwE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 rglLRNRaLGFVYQ-FHHLLPEFTALENVcmpLL------IG--RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGER 152
Cdd:COG1119 76 ---LRKR-IGLVSPaLQLRFPRDETVLDV---VLsgffdsIGlyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRLIAA 227
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAA 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-225 |
2.20e-38 |
|
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: 132.73 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRNRa 89
Cdd:cd03254 6 ENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSM- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEfTALENVCM-PLLIGRTPIAEARQ--RAAELLERV--GLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLgRPNATDEEVIEAAKeaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKII 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-225 |
2.44e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEE--LSALNETARGL 84
Cdd:PRK11124 3 IQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFVYQFHHLLPEFTALENV----CMPLLIGRtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLieapCRVLGLSK---DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 161 LVNRPQLVLLDEPTGNLD-QHTAQgIQELMLELSRSLQTSfLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDpEITAQ-IVSIIRELAETGITQ-VIVTHEVEVARKTaSRVVYMENGHIV 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-224 |
3.34e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 135.93 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLlrnra 89
Cdd:PRK11000 7 RNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 lGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQR---AAELLErvgLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:PRK11000 78 -GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRvnqVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 167 LVLLDEPTGNLDqhTAQGIQeLMLELSR---SLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK11000 154 VFLLDEPLSNLD--AALRVQ-MRIEISRlhkRLGRTMIYVTHDQVEAMTLaDKIVVLDAGRV 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-223 |
1.13e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 134.20 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALnETArgllr 86
Cdd:PRK11650 4 LKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQR---AAELLErvgLGHRLSHKPAELSGGERQRVAIARALVN 163
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERvaeAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 164 RPQLVLLDEPTGNLD-QHTAQGIQELMlELSRSLQTSFLVVTHD----LQLAghmDRILRLEEGR 223
Cdd:PRK11650 152 EPAVFLFDEPLSNLDaKLRVQMRLEIQ-RLHRRLKTTSLYVTHDqveaMTLA---DRVVVMNGGV 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-219 |
1.45e-37 |
|
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: 137.03 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETAR 82
Cdd:TIGR02857 318 PASSLEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GllrnRALGFVYQfHHLLPEFTALENVcmplLIGR-----TPIAEARQRA--AELLERVGLGH--RLSHKPAELSGGERQ 153
Cdd:TIGR02857 395 R----DQIAWVPQ-HPFLFAGTIAENI----RLARpdasdAEIREALERAglDEFVAALPQGLdtPIGEGGAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRL 219
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-226 |
1.03e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 134.95 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NrALGFVYQFHHLLPEfTALENvcmpLLIGRTPIAEARQRAAelLERVGLGHRLSHKPA----------ELSGGERQRVA 156
Cdd:PRK11160 414 Q-AISVVSQRVHLFSA-TLRDN----LLLAAPNASDEALIEV--LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-227 |
1.35e-36 |
|
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: 131.39 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 34 LPG-ERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsALNETARGLL---RNRALGFVYQFHHLLPEFTALENv 109
Cdd:TIGR02142 20 LPGqGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIFlppEKRRIGYVFQEARLFPHLSVRGN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 cmpLLIG--RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQE 187
Cdd:TIGR02142 96 ---LRYGmkRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598183 188 LMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAA 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-225 |
4.46e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 126.15 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGeRVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03264 72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQ-LAGHMDRILRLEEGRLI 225
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEdVESLCNQVAVLNKGKLV 208
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-226 |
4.80e-36 |
|
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: 125.12 E-value: 4.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALS---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLpeftalenvcmplligrtpiaearqrAAELLERVGlghrlshkpAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03247 75 -SLISVLNQRPYLF--------------------------DTTLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-224 |
9.90e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 126.62 E-value: 9.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET------ 80
Cdd:PRK10619 6 LNVIDLHKRYGEH----EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ----ARGLLRNRaLGFVYQFHHLLPEFTALENVC-MPLLIGRTPIAEARQRAAELLERVGLGHRLSHK-PAELSGGERQR 154
Cdd:PRK10619 82 adknQLRLLRTR-LTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVsSHVIFLHQGKI 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-225 |
1.25e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 125.81 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRA 89
Cdd:cd03253 4 ENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQ----FHHllpefTALENVCMplliGR---TP--IAEARqRAAELLERV-----GLGHRLSHKPAELSGGERQRV 155
Cdd:cd03253 77 IGVVPQdtvlFND-----TIGYNIRY----GRpdaTDeeVIEAA-KAAQIHDKImrfpdGYDTIVGERGLKLSGGEKQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTT-IVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-226 |
1.58e-35 |
|
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: 124.92 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdeGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLsHKPA-ELSGGERQRVAIARALVNRP 165
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRArTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALcDRIAIMSDGKLRC 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-227 |
3.59e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.29 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLaGEELSALNETARGL--LRNRaLGFVYQF-HHLLPE 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLkpLRKK-VGIVFQFpEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 FTALENVCM-PLLIGrTPIAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQH 180
Cdd:PRK13634 101 ETVEKDICFgPMNFG-VSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598183 181 TAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRLIAA 227
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQ 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
10-225 |
5.15e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.71 E-value: 5.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlNETARGL--LR 86
Cdd:PRK13641 6 ENVDYIYSPGtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP-ETGNKNLkkLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQFHHL-LPEFTALENVCM-PLLIGRTPiAEARQRAAELLERVGLGHRL-SHKPAELSGGERQRVAIARALVN 163
Cdd:PRK13641 85 KK-VSLVFQFPEAqLFENTVLKDVEFgPKNFGFSE-DEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLvVTHDL-QLAGHMDRILRLEEGRLI 225
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMdDVAEYADDVLVLEHGKLI 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-224 |
5.25e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.13 E-value: 5.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGL---DTPSAGSVWLAGEELSALNET 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRNRA-LGFVYQFHHLLPEFTALENVCMPLLiGRTPI---------AEARQRAAELLERVGLGHRLSHKPAELSGG 150
Cdd:PRK09984 78 ARDIRKSRAnTGYIFQQFNLVNRLSVLENVLIGAL-GSTPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA-GHMDRILRLEEGRL 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHV 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-226 |
9.32e-35 |
|
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: 123.31 E-value: 9.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllr 86
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRA-LGFVYQFHHLLPEFTALENvcmpLLIGRTPIAEARQRAAelLERV-----GLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:cd03224 73 ARAgIGYVPEGRRIFPELTVEEN----LLLGAYARRRAKRKAR--LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIaDRAYVLERGRVVL 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-225 |
1.24e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 9 CRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAG--------------EEL 74
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqeppldDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 75 SALNETARGLLRNRALgfVYQFHHLLPEFTALENVCMPL--LIGRTPIA---EARQRAAELLERVGLGHRLSHKP-AELS 148
Cdd:COG0488 77 TVLDTVLDGDAELRAL--EAELEELEAKLAEPDEDLERLaeLQEEFEALggwEAEARAEEILSGLGFPEEDLDRPvSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 149 GGERQRVAIARALVNRPQLVLLDEPTGNLDqhtAQGIQ--ELMLelsRSLQTSFLVVTHD---L-QLAGHmdrILRLEEG 222
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEwlEEFL---KNYPGTVLVVSHDryfLdRVATR---ILELDRG 225
|
...
gi 15598183 223 RLI 225
Cdd:COG0488 226 KLT 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-226 |
1.25e-34 |
|
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: 122.70 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLRnRA 89
Cdd:cd03245 6 RNVSFSYPNQEIPA--LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLlpeF--TALENVCMplliGRTPIAEAR-QRAAEL--------LERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:cd03245 80 IGYVPQDVTL---FygTLRDNITL----GAPLADDERiLRAAELagvtdfvnKHPNGLDLQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAqgiQELMLELSRSL-QTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQLLgDKTLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-227 |
1.88e-34 |
|
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: 123.40 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYdeGPQsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGE-----ELSALN 78
Cdd:TIGR02323 1 KPLLQVSGLSKSY--GGG--KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETARGLLRNRALGFVYQ--FHHLLPEFTALENVCMPLL-IGRTPIAEARQRAAELLERVGLGH-RLSHKPAELSGGERQR 154
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQnpRDGLRMRVSAGANIGERLMaIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVVES 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
7-225 |
1.91e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.41 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDE-----GPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETA 81
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RG-LLR------NRALGFVYQFHHLLPEftalenvcmPLLIGRTPIAEAR-QRAAELLERVGL-GHRLSHKPAELSGGER 152
Cdd:COG4167 85 RCkHIRmifqdpNTSLNPRLNIGQILEE---------PLRLNTDLTAEEReERIFATLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHIsDKVLVMHQGEVV 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-226 |
4.20e-34 |
|
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: 122.01 E-value: 4.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETAR 82
Cdd:COG0410 2 PMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLppHRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 gllrnRALGFVYQFHHLLPEFTALENvcmpLLIG------RTPIAEARQRAAELLERvgLGHRLSHKPAELSGGERQRVA 156
Cdd:COG0410 78 -----LGIGYVPEGRRIFPSLTVEEN----LLLGayarrdRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIaDRAYVLERGRIVL 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-222 |
7.62e-34 |
|
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: 120.44 E-value: 7.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetargllRNRAL 90
Cdd:cd03226 4 NISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQ--FHHLLPEFTALEnvcmpLLIGRTPIAEARQRAAELLERVGL-GHRLSHkPAELSGGERQRVAIARALVNRPQL 167
Cdd:cd03226 74 GYVMQdvDYQLFTDSVREE-----LLLGLKELDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 168 VLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEG 222
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-225 |
8.83e-34 |
|
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: 126.46 E-value: 8.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSY---DEGpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVW-LAGEELsaLNE 79
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvDRG--VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEW--VDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 TARG-LLRNRA---LGFVYQFHHLLPEFTALENVCMPLLIgRTPIAEARQRAAELLERVGLGHR-----LSHKPAELSGG 150
Cdd:TIGR03269 353 TKPGpDGRGRAkryIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVcDRAALMRDGKIV 507
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
9.02e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 9.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETa 81
Cdd:PRK13632 3 NKSVMIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 rgLLRNRaLGFVYQ-----FHHLLPE----FtALENVCMPLligrtpiAEARQRAAELLERVGLGHRLSHKPAELSGGER 152
Cdd:PRK13632 80 --EIRKK-IGIIFQnpdnqFIGATVEddiaF-GLENKKVPP-------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIA 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-225 |
1.44e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.35 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGll 85
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVYQfHHLL---PEFTALENVCM--------PLLIGRTpiAEARQRAAELLERVGLG--HRLSHKPAELSGGER 152
Cdd:COG1101 80 --KYIGRVFQ-DPMMgtaPSMTIEENLALayrrgkrrGLRRGLT--KKRRELFRELLATLGLGleNRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-226 |
2.16e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.48 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 28 GVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETARgllrnraLGFVYQFHH--LLPEF 103
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpgHQIAR-------MGVVRTFQHvrLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALEN--------VCMPLLIG--RTPI-----AEARQRAAELLERVGLGhRLSHKPA-ELSGGERQRVAIARALVNRPQL 167
Cdd:PRK11300 96 TVIENllvaqhqqLKTGLFSGllKTPAfrraeSEALDRAATWLERVGLL-EHANRQAgNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 168 VLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLA-GHMDRILRLEEGRLIA 226
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLA 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-226 |
2.26e-33 |
|
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: 119.39 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllrnRA 89
Cdd:cd03266 5 DALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-----RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVC-MPLLIGRTPiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLV 168
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGLYGLKG-DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 169 LLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLcDRVVVLHRGRVVY 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-226 |
3.34e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 3.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEgpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSalnETARG 83
Cdd:PRK13635 3 EEIIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRnRALGFVYQFhhllP--EFT----------ALENVCMPlligRTPIAEarqRAAELLERVGLGHRLSHKPAELSGGE 151
Cdd:PRK13635 78 DVR-RQVGMVFQN----PdnQFVgatvqddvafGLENIGVP----REEMVE---RVDQALRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-219 |
3.88e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 22 SVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelsalnetargllrNRALGFVYQFHHLLP 101
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EF--TALENVCM----PLLIGRTPIAEARQRAAELLERVGLgHRLSHKP-AELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:NF040873 69 SLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598183 175 GNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHMDRILRL 219
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-224 |
4.29e-33 |
|
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: 118.81 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 30 ELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETargllrNRALGFVYQFHHLLPEFTALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 CMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELM 189
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598183 190 LELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRL 224
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-225 |
4.51e-33 |
|
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: 118.47 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETargllr 86
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENvcmpLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQ 166
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 167 LVLLDEPTGNLDqhtAQGIQElMLELSRSLQ---TSFLVVTHDL----QLAghmDRILRLEEGRLI 225
Cdd:cd03268 147 LLILDEPTNGLD---PDGIKE-LRELILSLRdqgITVLISSHLLseiqKVA---DRIGIINKGKLI 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-226 |
5.23e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.37 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELS------ALne 79
Cdd:COG3845 5 ALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 tARGllrnraLGFVYQfhH--LLPEFTALENVCM---PLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQR 154
Cdd:COG3845 79 -ALG------IGMVHQ--HfmLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLdqhTAQGIQELMLELsRSL---QTSFLVVTHDL----QLAghmDRI--LRLeeGRLI 225
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVL---TPQEADELFEIL-RRLaaeGKSIIFITHKLrevmAIA---DRVtvLRR--GKVV 220
|
.
gi 15598183 226 A 226
Cdd:COG3845 221 G 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-227 |
7.69e-33 |
|
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: 118.41 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETARgl 84
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 lrnRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHrLSHKPA-ELSGGERQRVAIARALVN 163
Cdd:cd03218 75 ---LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKAsSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHD----LQLAghmDRILRLEEGRLIAA 227
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNvretLSIT---DRAYIIYEGKVLAE 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-192 |
9.09e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETAR 82
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 gllrnRALGFVYQ----FHHLlpefTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:COG1137 78 -----LGIGYLPQeasiFRKL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190
....*....|....*....|....*....|....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLEL 192
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHL 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-226 |
1.08e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.91 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgl 84
Cdd:PRK13537 6 APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHAR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 lrnRALGFVYQFHHLLPEFTALENVcmpLLIGR---TPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL 161
Cdd:PRK13537 80 ---QRVGVVPQFDNLDPDFTVRENL---LVFGRyfgLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTaqgiQELMLELSRSLQTS---FLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQA----RHLMWERLRSLLARgktILLTTHFMEEAERLcDRLCVIEEGRKIA 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-225 |
1.24e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 123.80 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSAGSVWLAGEELSALNETA-RgllrnRALGFVYQFHH 98
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESwR-----KHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 LlPEFTALENVcmplLIGRTPIAEA-------RQRAAELLERV--GLGHRLSHKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:PRK11174 434 L-PHGTLRDNV----LLGNPDASDEqlqqaleNAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLELSRSLQTsfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-206 |
1.40e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.59 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsalneT 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFG----SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLlRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK11432 72 HRSI-QQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHD 206
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-224 |
2.40e-32 |
|
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: 115.39 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllr 86
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 nRALGFVYQFHHLLPEfTALENVcmplligrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARALVNRPQ 166
Cdd:cd03246 76 -DHVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSfLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALKAAGATR-IVIAHRPETLASADRILVLEDGRV 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-225 |
2.79e-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: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGL--DTPSA---GSVWLAGEELSA 76
Cdd:COG1117 7 TLEPKIEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 77 ----LNEtarglLRnRALGFVYQFHHLLPeFTALENVCMPL-LIGRTPIAEARQRAAELLERVGL----GHRLsHKPA-E 146
Cdd:COG1117 83 pdvdVVE-----LR-RRVGMVFQKPNPFP-KSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRL-KKSAlG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARVsDYTAFFYLGELV 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-224 |
4.17e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.61 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 31 LNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsalNETARGLLRnRALGFVYQFHHLLPEFTALENVC 110
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTPPSR-RPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 111 MPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELML 190
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*
gi 15598183 191 ELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIaPRSLVVADGRI 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
4.47e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.03 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSvqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsALNETARGLL 85
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNR-ALGFVYQF-HHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHrLSHKPAE-LSGGERQRVAIARALV 162
Cdd:PRK13636 79 KLReSVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 163 NRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQL-AGHMDRILRLEEGRLI 225
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVI 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-207 |
8.75e-32 |
|
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: 121.31 E-value: 8.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETAr 82
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 gllRNRALGFVYQFHHLLpEFTALENvcmpLLIGRTPIAEARQRAAelLERVGLGHRLSHKP-----------AELSGGE 151
Cdd:TIGR02868 407 ---VRRRVSVCAQDAHLF-DTTVREN----LRLARPDATDEELWAA--LERVGLADWLRALPdgldtvlgeggARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsfLVVTHDL 207
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHHL 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-225 |
2.49e-31 |
|
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: 119.91 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDT--PSAGSV-----------WL---- 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgYVerps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 70 --------AGEELSA-------LNETARGLLRNR-ALGFVYQFHhLLPEFTALENVCMPLLIGRTPIAEARQRAAELLER 133
Cdd:TIGR03269 77 kvgepcpvCGGTLEPeevdfwnLSDKLRRRIRKRiAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 134 VGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGH 212
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIEDL 235
|
250
....*....|...
gi 15598183 213 MDRILRLEEGRLI 225
Cdd:TIGR03269 236 SDKAIWLENGEIK 248
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-226 |
5.66e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.47 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllrnRAL 90
Cdd:PRK13536 46 GVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR-----ARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 91 GFVYQFHHLLPEFTALENVcmpLLIGRTPIAEARQRAA---ELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQL 167
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENL---LVFGRYFGMSTREIEAvipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 168 VLLDEPTGNLDQHTaqgiQELMLELSRSLQT---SFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:PRK13536 194 LILDEPTTGLDPHA----RHLIWERLRSLLArgkTILLTTHFMEEAERLcDRLCVLEAGRKIA 252
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-225 |
6.90e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.18 E-value: 6.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-WL---------AGEELSALN 78
Cdd:PRK13651 6 KNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkdeknkkkTKEKEKVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETARGLLRNRAL----------GFVYQF-HHLLPEFTALENVCM-PLLIGrTPIAEARQRAAELLERVGLGHR-LSHKPA 145
Cdd:PRK13651 86 KLVIQKTRFKKIkkikeirrrvGVVFQFaEYQLFEQTIEKDIIFgPVSMG-VSKEEAKKRAAKYIELVGLDESyLQRSPF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 146 ELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLA-GHMDRILRLEEGRL 224
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVlEWTKRTIFFKDGKI 243
|
.
gi 15598183 225 I 225
Cdd:PRK13651 244 I 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-227 |
1.22e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.95 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWL----AGEELSALNET 80
Cdd:PRK13631 21 ILRVKNLYCVFDEKqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRN--------RALGFVYQFhhllPEF----TALENVCM--PLLIGRTPIaEARQRAAELLERVGLGHR-LSHKPA 145
Cdd:PRK13631 101 TNPYSKKiknfkelrRRVSMVFQF----PEYqlfkDTIEKDIMfgPVALGVKKS-EAKKLAKFYLNKMGLDDSyLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 146 ELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFlVVTHD----LQLAghmDRILRLEE 221
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF-VITHTmehvLEVA---DEVIVMDK 251
|
....*.
gi 15598183 222 GRLIAA 227
Cdd:PRK13631 252 GKILKT 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-226 |
1.25e-30 |
|
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: 110.60 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllR 86
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQfhhllpeftalenvcmplligrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARALVNRPQ 166
Cdd:cd03216 74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 167 LVLLDEPTGNLDQHTAqgiqELMLELSRSLQ---TSFLVVTHDL----QLAghmDRILRLEEGRLIA 226
Cdd:cd03216 103 LLILDEPTAALTPAEV----ERLFKVIRRLRaqgVAVIFISHRLdevfEIA---DRVTVLRDGRVVG 162
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-226 |
1.38e-30 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 112.75 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALN--ETARg 83
Cdd:TIGR04406 1 TLVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 llrnRALGFVYQFHHLLPEFTALENVCMPL-LIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALV 162
Cdd:TIGR04406 76 ----LGIGYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 163 NRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRLIA 226
Cdd:TIGR04406 152 TNPKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVReTLDICDRAYIISDGKVLA 215
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
10-227 |
1.63e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSvqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRNRa 89
Cdd:PRK13647 8 EDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQ------FhhllpEFTALENVCM-PLLIGRTPiAEARQRAAELLERVGLgHRLSHK-PAELSGGERQRVAIARAL 161
Cdd:PRK13647 81 VGLVFQdpddqvF-----SSTVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRM-WDFRDKpPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGH-MDRILRLEEGRLIAA 227
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEwADQVIVLKEGRVLAE 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-225 |
1.63e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLaGEELSalnetarg 83
Cdd:COG0488 313 KKVLELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 llrnraLGFVYQFHHLL-PEFTALENVCmPLLIGRTPIaEARQraaeLLERVGLGHRLSHKPAE-LSGGERQRVAIARAL 161
Cdd:COG0488 380 ------IGYFDQHQEELdPDKTVLDELR-DGAPGGTEQ-EVRG----YLGRFLFSGDDAFKPVGvLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTaqgiQELMLELsrsLQT---SFLVVTHDLQ-LAGHMDRILRLEEGRLI 225
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIET----LEALEEA---LDDfpgTVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-226 |
1.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.63 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLL 85
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK---KSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNR-ALGFVYQFhhllPE---F--TALENVCM-PLLIGrTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK13639 75 EVRkTVGIVFQN----PDdqlFapTVEEDVAFgPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAG-HMDRILRLEEGRLIA 226
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPvYADKVYVMSDGKIIK 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-226 |
1.83e-30 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.54 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 21 QSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllrnRALGFVYQFHHLL 100
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 101 PEfTALENvcmpllIGRTP------IAEARQRAA--ELLERVGLGH--RLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:COG4618 419 DG-TIAEN------IARFGdadpekVVAAAKLAGvhEMILRLPDGYdtRIGEGGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 171 DEPTGNLDqhtAQGIQELM--LELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:COG4618 492 DEPNSNLD---DEGEAALAaaIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
10-225 |
2.24e-30 |
|
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: 112.25 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetARGLLRNra 89
Cdd:cd03249 4 KNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN--LRWLRSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLpEFTALENVCMplliGRTPI----AEARQRAAELLERV-----GLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:cd03249 79 IGLVSQEPVLF-DGTIAENIRY----GKPDAtdeeVEEAAKKANIHDFImslpdGYDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-227 |
2.82e-30 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 115.71 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 22 SVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllrnRALGFVYQFHHLLP 101
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EFTALENVCMplliGRTP-------IAEARQRAAE-LLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEP 173
Cdd:PRK09536 91 EFDVRQVVEM----GRTPhrsrfdtWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 174 TGNLDQHTAQGIQELMLELSRSLQTSfLVVTHDLQLAG-HMDRILRLEEGRLIAA 227
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGKTA-VAAIHDLDLAArYCDELVLLADGRVRAA 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-225 |
4.98e-30 |
|
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: 111.42 E-value: 4.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 19 GPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRALGFVYQ--- 95
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW---LR-RQVGVVLQenv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 96 -FHHLLPEFTALENVCMPL--LIGRTPIAEARQRAAELLErvGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDE 172
Cdd:cd03252 87 lFNRSIRDNIALADPGMSMerVIEAAKLAGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598183 173 PTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
6.51e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.54 E-value: 6.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGL-----DTPSAGSVWLAGEELSALN 78
Cdd:PRK14247 1 MNKIEIRDLKVSFG----QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETargLLRNRaLGFVYQFHHLLPEFTALENVCMPLLIGR--TPIAEARQRAAELLERVGL----GHRLSHKPAELSGGER 152
Cdd:PRK14247 77 VI---ELRRR-VQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLqtSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARIsDYVAFLYKGQIV 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-225 |
7.42e-30 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 115.97 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdeGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALnetargLLR 86
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY------TLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 N--RALGFVYQFHHLLPEfTALENVCM--PLLIGRTPIAEARQrAAELLERV-----GLGHRLSHKPAELSGGERQRVAI 157
Cdd:TIGR02203 403 SlrRQVALVSQDVVLFND-TIANNIAYgrTEQADRAEIERALA-AAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-227 |
1.36e-29 |
|
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: 109.29 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETA----- 81
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 --RGLLRNRALG--FVYqfhhllpeFTALENVcmplligrtPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:cd03269 77 eeRGLYPKMKVIdqLVY--------LAQLKGL---------KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELcDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
10-225 |
1.76e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.99 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNR 88
Cdd:PRK13649 6 QNVSYTYQAGtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 89 ALGFVYQF-HHLLPEFTALENVCM-PLLIGRTPIaEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARALVNRP 165
Cdd:PRK13649 86 KVGLVFQFpESQLFEETVLKDVAFgPQNFGVSQE-EAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 166 QLVLLDEPTGNLDqhtAQGIQELMlELSRSLQTS---FLVVTHDL-QLAGHMDRILRLEEGRLI 225
Cdd:PRK13649 165 KILVLDEPTAGLD---PKGRKELM-TLFKKLHQSgmtIVLVTHLMdDVANYADFVYVLEKGKLV 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-226 |
2.47e-29 |
|
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: 109.34 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYD-----EGP------------QSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGE 72
Cdd:cd03267 4 SNLSKSYRvyskePGLigslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 73 ELSalnETARGLLRNraLGFVY-QFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLsHKPA-ELSGG 150
Cdd:cd03267 84 VPW---KRRKKFLRR--IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELL-DTPVrQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRLIA 226
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLY 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-227 |
2.65e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.79 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAL--NETARGL--L 85
Cdd:COG4604 5 KNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsRELAKRLaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RnralgfvyQFHHLLPEFTALENVCMplliGRTP------IAEARQRAAELLERVGLGHrLSHKPA-ELSGGERQRVAIA 158
Cdd:COG4604 81 R--------QENHINSRLTVRELVAF----GRFPyskgrlTAEDREIIDEAIAYLDLED-LADRYLdELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYaDHIVAMKDGRVVAQ 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-225 |
2.70e-29 |
|
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: 109.12 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYdeGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALnetarGL--LRN 87
Cdd:cd03244 6 KNVSLRY--RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-----GLhdLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RaLGFVYQFHHLLP-----------EFT------ALENVCMPLLIGRTPIaearqraaellervGLGHRLSHKPAELSGG 150
Cdd:cd03244 79 R-ISIIPQDPVLFSgtirsnldpfgEYSdeelwqALERVGLKEFVESLPG--------------GLDTVVEEGGENLSVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELmlelsrsLQTSF-----LVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT-------IREAFkdctvLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-225 |
3.47e-29 |
|
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: 108.02 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGPQSV--QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSA--GSVWLAGEELSALNe 79
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 targlLRNRaLGFVYQFHHLLPEFTalenvcmplligrtpIAEARQRAAELleRVglghrlshkpaeLSGGERQRVAIAR 159
Cdd:cd03213 80 -----FRKI-IGYVPQDDILHPTLT---------------VRETLMFAAKL--RG------------LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 160 ALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSrSLQTSFLVVTHDL--QLAGHMDRILRLEEGRLI 225
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPssEIFELFDKLLLLSQGRVI 191
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-227 |
8.50e-29 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 108.00 E-value: 8.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllr 86
Cdd:TIGR03410 1 LEVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENvcmpLLIGRTPIAEA-RQRAAELLERVGLGHRLSHKPA-ELSGGERQRVAIARALVNR 164
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEEN----LLTGLAALPRRsRKIPDEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVVAS 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-225 |
1.18e-28 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 107.70 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALneTARGLLRNraLGFVYQFHHLLPEfT 104
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY--TLASLRRQ--IGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVcmplLIGRTPIAEARQRAA-------ELLERV--GLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTG 175
Cdd:cd03251 92 VAENI----AYGRPGATREEVEEAaraanahEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598183 176 NLDQHTAQGIQELMLELSRSlQTSFlVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03251 168 ALDTESERLVQAALERLMKN-RTTF-VIAHRLSTIENADRIVVLEDGKIV 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-226 |
2.04e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.58 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 34 LPGERV-AIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelSALNETARGLL---RNRALGFVYQFHHLLPEFTALENv 109
Cdd:PRK11144 21 LPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGIClppEKRRIGYVFQDARLFPHYKVRGN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 cmpLLIGRTPIAEAR-QRAAELLervGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAqgiQEL 188
Cdd:PRK11144 97 ---LRYGMAKSMVAQfDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK---REL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598183 189 M--LE-LSRSLQTSFLVVTHDLQ----LAghmDRILRLEEGRLIA 226
Cdd:PRK11144 168 LpyLErLAREINIPILYVSHSLDeilrLA---DRVVVLEQGKVKA 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-223 |
2.59e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.34 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKS-TLLNMLGGLDTPSA----GSVWLAGEE-LSALNET 80
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESlLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRNR-ALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAE-ARQRAAELLERVGLGH---RLSHKPAELSGGERQRV 155
Cdd:PRK15134 86 LRGVRGNKiAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREaARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL----QLAghmDRILRLEEGR 223
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLsivrKLA---DRVAVMQNGR 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-225 |
3.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYDEGPQSVQ--VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET 80
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARglLRNRAlGFVYQ------FHHLLPEFTAL--ENVCMPLLigrtpiaEARQRAAELLERVGLGHRLSHKPAELSGGER 152
Cdd:PRK13633 81 WD--IRNKA-GMVFQnpdnqiVATIVEEDVAFgpENLGIPPE-------EIRERVDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
25-219 |
3.82e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.95 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALN-ETARgllrnRALGFVYQFHHLLPEf 103
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYR-----QQVSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCMPLLIGRtpIAEARQRAAELLERVGLGHRLSHKP-AELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTA 182
Cdd:PRK10247 96 TVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598183 183 QGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRL 219
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-226 |
1.02e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALneTARGLlr 86
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--SSRQL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQfHHLLPEFTAlenVCMPLLIGRTPI--------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK11231 75 ARRLALLPQ-HHLTPEGIT---VRELVAYGRSPWlslwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 159 RALVNRPQLVLLDEPTGNLD-QHTAqgiqELMlELSRSLQT---SFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDiNHQV----ELM-RLMRELNTqgkTVVTVLHDLnQASRYCDHLVVLANGHVMA 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-225 |
1.02e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.05 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVqvlSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLRnRA 89
Cdd:PRK13657 338 DDVSFSYDNSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQfHHLLPEFTALENvcmpLLIGRT-----PIAEARQRAA--ELLER--VGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK13657 411 IAVVFQ-DAGLFNRSIEDN----IRVGRPdatdeEMRAAAERAQahDFIERkpDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFlVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKG-RTTF-IIAHRLSTVRNADRILVFDNGRVV 548
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-225 |
1.15e-27 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 109.91 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRALGFVyqfhhllPEF 103
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LR-AAIGIV-------PQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TAL------ENVCMplliGRtpiAEARQ-------RAAELLE-----------RVGlghrlshkpaE----LSGGERQRV 155
Cdd:COG5265 441 TVLfndtiaYNIAY----GR---PDASEeeveaaaRAAQIHDfieslpdgydtRVG----------ErglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTT-LVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-217 |
1.38e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.10 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYD---------EGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-WLaG 71
Cdd:PRK15079 4 GKKVLLEVADLKVHFDikdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWL-G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 72 EELSALNETARGLLRNRaLGFVYQ--FHHLLPEFTALENVCMPLLI--GRTPIAEARQRAAELLERVGLGHRLSHK-PAE 146
Cdd:PRK15079 83 KDLLGMKDDEWRAVRSD-IQMIFQdpLASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRIL 217
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIsDRVL 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
7-225 |
2.76e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSV-----------QVLSGVELNL---------LPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGS 66
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAfkyieqglskeQILEKTGLSLgvkdaslaiEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 67 VWLAGEELSALNETARGLLRNRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAE 146
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-225 |
3.27e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.25 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLagEELSALNETARGLLR--N 87
Cdd:PRK13646 7 NVSYTYQKGtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDKYIRpvR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RALGFVYQFhhllPEFTALE-NVCMPLLIG----RTPIAEARQRAAELLERVGLGHR-LSHKPAELSGGERQRVAIARAL 161
Cdd:PRK13646 85 KRIGMVFQF----PESQLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL-QLAGHMDRILRLEEGRLI 225
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMnEVARYADEVIVMKEGSIV 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-227 |
3.29e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.19 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSA--------L 77
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigyL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 78 NETaRGLLRNRALG--FVYqfhhllpeFTALENvcMPLligrtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:COG4152 77 PEE-RGLYPKMKVGeqLVY--------LARLKG--LSK-------AEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELcDRIVIINKGRKVLS 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-208 |
3.43e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.25 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKST----LLNMLggldtPSAGSVWLAGEELSALNETARGLLRNRaLGFVYQ--FH 97
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 98 HLLPEFTALENVCMPLLIGRTPI--AEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQPTLsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190
....*....|....*....|....*....|....
gi 15598183 175 GNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ 208
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-224 |
4.23e-27 |
|
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: 103.32 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnetargllrnra 89
Cdd:cd03248 15 QNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 lgfvYQFHHLLPEFTALENvcMPLLIGRT---------------PIAEARQRAA-----ELLERvGLGHRLSHKPAELSG 149
Cdd:cd03248 81 ----YEHKYLHSKVSLVGQ--EPVLFARSlqdniayglqscsfeCVKEAAQKAHahsfiSELAS-GYDTEVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 150 GERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-222 |
5.15e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.97 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdtpsagsvWLAGEELSALNETARGLlrnralgFV----Yq 95
Cdd:COG4178 373 PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--------WPYGSGRIARPAGARVL-------FLpqrpY- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 96 fhhlLPEFTALENVCMPlligRTPIAEARQRAAELLERVGLGH---RLS---HKPAELSGGERQRVAIARALVNRPQLVL 169
Cdd:COG4178 437 ----LPLGTLREALLYP----ATAEAFSDAELREALEAVGLGHlaeRLDeeaDWDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598183 170 LDEPTGNLDQHTAQGIQELMLElsRSLQTSFLVVTHDLQLAGHMDRILRLEEG 222
Cdd:COG4178 509 LDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-222 |
8.16e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.18 E-value: 8.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdeGPqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETargLLR 86
Cdd:PRK09700 6 ISMAGIGKSF--GP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK---LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENvcmpLLIGRTPI-----------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLEN----LYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDL-QLAGHMDRILRLEEG 222
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
25-224 |
1.85e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 106.28 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGllrnRALGFVYQFHHLLPEfT 104
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVCMpllIGRTPIAEARQRAA------ELLERVGLGHRLSHKP--AELSGGERQRVAIARALVNRPQLVLLDEPTGN 176
Cdd:TIGR01842 408 VAENIAR---FGENADPEKIIEAAklagvhELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598183 177 LDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:TIGR01842 485 LDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-225 |
2.80e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEG-PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNRA 89
Cdd:PRK13637 7 NLTHIYMEGtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENVCMPLLIGRTPiAEARQRAAELLERVGLGHR--LSHKPAELSGGERQRVAIARALVNRPQL 167
Cdd:PRK13637 87 LVFQYPEYQLFEETIEKDIAFGPINLGLSE-EEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 168 VLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRLI 225
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCE 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-195 |
3.86e-26 |
|
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: 100.81 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 22 SVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSA---GSVWLAGEELSalnetaRGLLRNRaLGFVYQFHH 98
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK------PDQFQKC-VAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 LLPEFTALENV--CMPLLIGR-TPIAEARQRAA-ELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:cd03234 92 LLPGLTVRETLtyTAILRLPRkSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|.
gi 15598183 175 GNLDQHTAQGIQELMLELSRS 195
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARR 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4-225 |
6.43e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.13 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGPQSvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPS---AGSVWLAGEELSALNET 80
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERPRK-HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGllrnralGFVYQFHHLLPEFTALEN------VCMPlliGRTPIAEARQRAAELLERVGL--------GHRLSHKpaE 146
Cdd:TIGR00955 99 AIS-------AYVQQDDLFIPTLTVREHlmfqahLRMP---RRVTKKEKRERVDEVLQALGLrkcantriGVPGRVK--G 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVtHD--LQLAGHMDRILRLEEGRL 224
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI-HQpsSELFELFDKIILMAEGRV 245
|
.
gi 15598183 225 I 225
Cdd:TIGR00955 246 A 246
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-225 |
7.44e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.09 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSY-----DEGP------------QSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVW 68
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 69 LAGEELSAlNETArgLLRNraLGFVY-QFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLsHKPA-E 146
Cdd:COG4586 81 VLGYVPFK-RRKE--FARR--IGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL----QLAghmDRILRLEEG 222
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMddieALC---DRVIVIDHG 231
|
...
gi 15598183 223 RLI 225
Cdd:COG4586 232 RII 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-225 |
8.29e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglL 85
Cdd:PRK13642 4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN---L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RnRALGFVYQF-HHLLPEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNR 164
Cdd:PRK13642 80 R-RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 165 PQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEII 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-226 |
1.28e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNRALGFVYQF-HH 98
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 LLPEFTALENVCM-PLLIGRTPiAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIARALVNRPQLVLLDEPTGN 176
Cdd:PRK13643 96 QLFEETVLKDVAFgPQNFGIPK-EKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598183 177 LDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
31-226 |
1.51e-25 |
|
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: 99.15 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 31 LNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelsalnetARGLLRNRALGFVYQFHHLLPEF-TALENV 109
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG---------ASPGKGWRHIGYVPQRHEFAWDFpISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 CM---PLLIG--RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQG 184
Cdd:TIGR03771 72 VMsgrTGHIGwlRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598183 185 IQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILrLEEGRLIA 226
Cdd:TIGR03771 152 LTELFIELAGA-GTAILMTTHDLAQAMATcDRVV-LLNGRVIA 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-226 |
1.97e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSY------------------DEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGS 66
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 67 VWLAGeELSALNETARGllrnralgfvyqFHhllPEFTALENVcmpLLIGRT---PIAEARQRAAELLERVGLGHRLsHK 143
Cdd:COG1134 83 VEVNG-RVSALLELGAG------------FH---PELTGRENI---YLNGRLlglSRKEIDEKFDEIVEFAELGDFI-DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 144 PAE-LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEE 221
Cdd:COG1134 143 PVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLcDRAIWLEK 221
|
....*
gi 15598183 222 GRLIA 226
Cdd:COG1134 222 GRLVM 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
2.88e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.50 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegpqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:cd03215 4 VLEVRGLSVKG--------AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVY-----QFHHLLPEFTALENVCMPLLigrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARA 160
Cdd:cd03215 73 --IRAGIAYvpedrKREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQ-LAGHMDRILRLEEGRL 224
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-225 |
3.36e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 98.59 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 27 SGVELNLLPGERVAIVGSSGSGKST----LLNMLGGLDTPSAGSVWLAGEELSALNetarglLRNRALGFVYQ--FHHLL 100
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQnpRTAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 101 PEFTALENVCMPLLIGRTPIAEARQRAAELLERVGLGH--RLSHK-PAELSGGERQRVAIARALVNRPQLVLLDEPTGNL 177
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDpeEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 178 DQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIV 205
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-223 |
4.03e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.57 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPS---AGSVWLAGEELSALN 78
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETARGLLRNRALGFVYQ--FHHLLPEF---TALENVCMplLIGRTPIAEARQRAAELLERVGLGH---RLSHKPAELSGG 150
Cdd:PRK09473 88 EKELNKLRAEQISMIFQdpMTSLNPYMrvgEQLMEVLM--LHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGR 223
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGR 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-207 |
4.50e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 23 VQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRnRALGFVYQ--FHHLL 100
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 101 PEFTALENVCMPLLI-GRTPIAEARQRAAELLERVGLghRLSHK---PAELSGGERQRVAIARALVNRPQLVLLDEPTGN 176
Cdd:PRK10261 416 PRQTVGDSIMEPLRVhGLLPGKAAAARVAWLLERVGL--LPEHAwryPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190
....*....|....*....|....*....|.
gi 15598183 177 LDQHTAQGIQELMLELSRSLQTSFLVVTHDL 207
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-207 |
4.66e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 99.07 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLRNRaLGFVYQFHHLLPEF 103
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCMPLLiGRTPIAEARQRAAEL--LERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHT 181
Cdd:PRK11831 100 NVFDNVAYPLR-EHTQLPAPLLHSTVMmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPIT 178
|
170 180
....*....|....*....|....*.
gi 15598183 182 AQGIQELMLELSRSLQTSFLVVTHDL 207
Cdd:PRK11831 179 MGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-224 |
5.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 5.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARg 83
Cdd:PRK13650 2 SNIIEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 llrNRALGFVYQFhhllP--EF---TALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK13650 80 ---RHKIGMVFQN----PdnQFvgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDqhtAQGIQELM---LELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLD---PEGRLELIktiKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-225 |
8.33e-25 |
|
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: 101.74 E-value: 8.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLRnralgfvyQFHHLLPE-- 102
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR--------QFINYLPQep 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 --F--TALENvcmpLLIGRTPIAEARQ--RAAELLE--------RVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLV 168
Cdd:TIGR01193 558 yiFsgSILEN----LLLGAKENVSQDEiwAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 169 LLDEPTGNLDQHTAQGIQELMLELSrslQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-225 |
1.08e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLL---NMLGGL--DTPSAGSVWLAGEEL-SAL 77
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 78 NETARglLRnRALGFVYQFHHLLPeFTALENVCMPLLIGRT-------PIAEARQRAAELLERVGlgHRLSHKPAELSGG 150
Cdd:PRK14239 79 TDTVD--LR-KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkdkqvldEAVEKSLKGASIWDEVK--DRLHDSALGLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRIsDRTGFFLDGDLI 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-225 |
1.35e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.61 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGL-----DTPSAGSVWLAGEELsaLNETARGLLRNRALGFVYQFHH 98
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 LLPEFTALENVCM-----PLLIGRTPIAEARQRA---AELLERVGlgHRLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:PRK14267 96 PFPHLTIYDNVAIgvklnGLVKSKKELDERVEWAlkkAALWDEVK--DRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 171 DEPTGNLDQHTAQGIQELMLELSRSLqtSFLVVTHD-LQLAGHMDRILRLEEGRLI 225
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-224 |
1.62e-24 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDEGPqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETa 81
Cdd:TIGR00958 474 NLEGLIEFQDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 rgLLRnRALGFVYQfHHLLPEFTALENVCMPLliGRTPIAEARQRAAELLER-------VGLGHRLSHKPAELSGGERQR 154
Cdd:TIGR00958 552 --YLH-RQVALVGQ-EPVLFSGSVRENIAYGL--TDTPDEEIMAAAKAANAHdfimefpNGYDTEVGEKGSQLSGGQKQR 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLqtsfLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTV----LLIAHRLSTVERADQILVLKKGSV 691
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-226 |
2.09e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdegPqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsALNETARGLlr 86
Cdd:PRK11288 5 LSFDGIGKTF---P-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAAL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENvcmpLLIGRTP-------IAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIAR 159
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAEN----LYLGQLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 160 ALVNRPQLVLLDEPTGNLdqhTAQGIQELMlELSRSLQ---TSFLVVTHdlqlagHMDRILRL-------EEGRLIA 226
Cdd:PRK11288 154 ALARNARVIAFDEPTSSL---SAREIEQLF-RVIRELRaegRVILYVSH------RMEEIFALcdaitvfKDGRYVA 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-226 |
2.17e-24 |
|
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: 96.06 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSY--DEGPQS----------------VQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVW 68
Cdd:cd03220 1 IELENVSKSYptYKGGSSslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 69 LAGeELSALnetargllrnraLGFVYQFHhllPEFTALENVCMPLLI-GRTPiAEARQRAAELLERVGLGHRLSHKPAEL 147
Cdd:cd03220 81 VRG-RVSSL------------LGLGGGFN---PELTGRENIYLNGRLlGLSR-KEIDEKIDEIIEFSELGDFIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 148 SGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPsSIKRLCDRALVLEKGKIRF 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-223 |
8.43e-24 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 92.51 E-value: 8.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWlageelsalnetargllR 86
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-----------------W 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYqFHHllpeftalenvcmplligrtpiaearqraaellervglghrlshkpaeLSGGERQRVAIARALVNRPQ 166
Cdd:cd03221 60 GSTVKIGY-FEQ------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 167 LVLLDEPTGNLDQHTAQGIQELMLELSRSLqtsfLVVTHDLQLAGHM-DRILRLEEGR 223
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPGTV----ILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-226 |
1.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetarglL 85
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN------I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RN--RALGFVYQ------FHHLLPEFTALENVCMPLligrtPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:PRK13652 74 REvrKFVGLVFQnpddqiFSPTVEQDIAFGPINLGL-----DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDqhtAQGIQELMLELSRSLQTSFLVV---THDLQLAGHM-DRILRLEEGRLIA 226
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLD---PQGVKELIDFLNDLPETYGMTVifsTHQLDLVPEMaDYIYVMDKGRIVA 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-209 |
1.52e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.80 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlageelsalnetarglLRNRAL--GFVYQFHHLLP 101
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------------KRNGKLriGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EftalenvcMPLLIGRTPIAEARQRAAEL---LERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLD 178
Cdd:PRK09544 81 T--------LPLTVNRFLRLRPGTKKEDIlpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|.
gi 15598183 179 QHTAQGIQELMLELSRSLQTSFLVVTHDLQL 209
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-225 |
6.18e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.33 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRNrA 89
Cdd:PRK10790 344 DNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LRQ-G 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEfTALENVCMplliGRtPIAEarQRAAELLERV-----------GLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTL----GR-DISE--EQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQElMLELSRSlQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQ-ALAAVRE-HTTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-226 |
7.05e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDkSVLSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET 80
Cdd:PRK13640 1 MKD-NIVEFKHVSFTYPDSKKPA--LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRNRaLGFVYQFhhllP--EF---TALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:PRK13640 78 TVWDIREK-VGIVFQN----PdnQFvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
11-225 |
8.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 8.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAG---EELSALNETargllrN 87
Cdd:PRK13644 6 NVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtGDFSKLQGI------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 RALGFVYQ------FHHLLPEFTAL--ENVCMPlligrtPIaEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIAR 159
Cdd:PRK13644 77 KLVGIVFQnpetqfVGRTVEEDLAFgpENLCLP------PI-EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 160 ALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-226 |
9.00e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSydegpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA--- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVY-----QFHHLLPEFTALENVCMPLL--IGRTPI---AEARQRAAELLERVGL-GHRLSHKPAELSGGERQR 154
Cdd:COG1129 325 --IRAGIAYvpedrKGEGLVLDLSIRENITLASLdrLSRGGLldrRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQ-LAGHMDRILRLEEGRLIA 226
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPeLLGLSDRILVMREGRIVG 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-219 |
9.37e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 91.27 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNEtarglLR 86
Cdd:TIGR01189 1 LAARNLACSRGERM----LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-----EP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLLPEFTALENVCMPLLIGRTpiaeARQRAAELLERVGLGHrLSHKPA-ELSGGERQRVAIARALVNRP 165
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHFWAAIHGG----AQRTIEDALAAVGLTG-FEDLPAaQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 166 QLVLLDEPTGNLDqhtAQGIQELMLELSRSLQTSFLVVthdlqLAGHMD------RILRL 219
Cdd:TIGR01189 147 PLWILDEPTTALD---KAGVALLAGLLRAHLARGGIVL-----LTTHQDlglveaRELRL 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-223 |
1.32e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 90.99 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQ-SVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelsalnetargllrnr 88
Cdd:cd03250 4 EDASFTWDSGEQeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 89 ALGFVYQFHHLLPEfTALENVCMplliGRtPIAEARQRAA----------ELLE-----RVGlghrlsHKPAELSGGERQ 153
Cdd:cd03250 67 SIAYVSQEPWIQNG-TIRENILF----GK-PFDEERYEKVikacalepdlEILPdgdltEIG------EKGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGI-QELMLELSRSLQTSFLvVTHDLQLAGHMDRILRLEEGR 223
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRIL-VTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-225 |
1.46e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKS--YDEG---PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALN 78
Cdd:PRK15112 2 ETLLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETarglLRNRALGFVYQ--FHHLLPEFTALENVCMPLLIGRTPIAEAR-QRAAELLERVGL-GHRLSHKPAELSGGERQR 154
Cdd:PRK15112 82 YS----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQReKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIsDQVLVMHQGEVV 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
36-209 |
1.71e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.27 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 36 GERVAIVGSSGSGKS-TLLNMLGGLDTP---SAGSVWLAGEELSALNETARGLLRNRALGFVYQ--FHHLLPEFTALENV 109
Cdd:PRK11022 33 GEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQdpMTSLNPCYTVGFQI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 CMPLLIGRT-PIAEARQRAAELLERVGL---GHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGI 185
Cdd:PRK11022 113 MEAIKVHQGgNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQI 192
|
170 180
....*....|....*....|....
gi 15598183 186 QELMLELSRSLQTSFLVVTHDLQL 209
Cdd:PRK11022 193 IELLLELQQKENMALVLITHDLAL 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-227 |
2.08e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSAGSVWLAGEELSALneTARGLLRNRA-------LGF---VYQ 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDW--SAAELARHRAylsqqqsPPFampVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 96 FHHL-LPEFTALENVCmplligrtpiaearQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL------VN-RPQL 167
Cdd:COG4138 89 YLALhQPAGASSEAVE--------------QLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 168 VLLDEPTGNLDqhTAQgiQELMLELSRSL---QTSFLVVTHDLQLA-GHMDRILRLEEGRLIAA 227
Cdd:COG4138 155 LLLDEPMNSLD--VAQ--QAALDRLLRELcqqGITVVMSSHDLNHTlRHADRVWLLKQGKLVAS 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-222 |
2.30e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.74 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRALGFVYQFhhllPE--F 103
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK---LR-KHIGIVFQN----PDnqF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 ---TALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQH 180
Cdd:PRK13648 97 vgsIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598183 181 TAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEG 222
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-191 |
2.56e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:PRK13539 2 MLEGEDLACVRGG----RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnralgFVYQFHH--LLPEFTALENvcmpLLIGRTPIAEARQRAAELLERVGLGHrLSHKPA-ELSGGERQRVAIARALV 162
Cdd:PRK13539 75 ------CHYLGHRnaMKPALTVAEN----LEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFgYLSAGQKRRVALARLLV 143
|
170 180 190
....*....|....*....|....*....|
gi 15598183 163 -NRPqLVLLDEPTGNLDQHTAQGIQELMLE 191
Cdd:PRK13539 144 sNRP-IWILDEPTAALDAAAVALFAELIRA 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-225 |
3.01e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.09 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALnETARg 83
Cdd:PRK11614 3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW-QTAK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 lLRNRALGFVYQFHHLLPEFTALENVCMP-LLIGRTPIAEARQRAAELLERvgLGHRLSHKPAELSGGERQRVAIARALV 162
Cdd:PRK11614 77 -IMREAVAIVPEGRRVFSRMTVEENLAMGgFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 163 NRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-226 |
4.22e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.72 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGL 84
Cdd:PRK10895 2 ATLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 lrnRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAEARQ-RAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVN 163
Cdd:PRK10895 78 ---RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLIA 226
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVcERAYIVSQGHLIA 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-207 |
7.14e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSaGSVWLAGE-ELSALNETARGLLRNR 88
Cdd:PRK14258 11 NNLSFYYD----TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRvEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 89 ---ALGFVYQFHHLLPeFTALENVCMPL-LIGRTP------IAEARQRAAELLERVGlgHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK14258 86 lrrQVSMVHPKPNLFP-MSVYDNVAYGVkIVGWRPkleiddIVESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL 207
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-226 |
1.22e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.36 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLD--TPSAGSVWLAGEELSAL--NETAR 82
Cdd:COG0396 1 LEIKNLHVSVEGKE----ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELspDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 -GLlrnrALGFVYQfhhllPEF----------TALENVCMPLLigrtPIAEARQRAAELLERVGLGHRLSHKP--AELSG 149
Cdd:COG0396 77 aGI----FLAFQYP-----VEIpgvsvsnflrTALNARRGEEL----SAREFLKLLKEKMKELGLDEDFLDRYvnEGFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 150 GERQRVAIARALVNRPQLVLLDEPTGNLD----QHTAQGIQELmlelsRSLQTSFLVVTHDLQLAGHM--DRILRLEEGR 223
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDidalRIVAEGVNKL-----RSPDRGILIITHYQRILDYIkpDFVHVLVDGR 218
|
...
gi 15598183 224 LIA 226
Cdd:COG0396 219 IVK 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-225 |
2.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.68 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSY-DEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSA----LNETARglL 85
Cdd:PRK13645 11 NVSYTYaKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkIKEVKR--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RnRALGFVYQFhhllPEFTALENVCM------PLLIGRTPiAEARQRAAELLERVGLGHRLSHK-PAELSGGERQRVAIA 158
Cdd:PRK13645 89 R-KEIGLVFQF----PEYQLFQETIEkdiafgPVNLGENK-QEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL-QLAGHMDRILRLEEGRLI 225
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVI 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-220 |
3.37e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET-ARGL 84
Cdd:PRK13538 1 MLEARNLACERDERI----LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyHQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LrnralgfvYQFHH--LLPEFTALENVCMPLLIGRTPIAEARQRAaelLERVGLGHRLsHKPAE-LSGGERQRVAIARAL 161
Cdd:PRK13538 77 L--------YLGHQpgIKTELTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFE-DVPVRqLSAGQQRRVALARLW 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 162 VNRPQLVLLDEPTGNLDqhtAQGIQELMLELSRSLQTSFLVV--TH-DLQLAGHMDRILRLE 220
Cdd:PRK13538 145 LTRAPLWILDEPFTAID---KQGVARLEALLAQHAEQGGMVIltTHqDLPVASDKVRKLRLG 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
43-216 |
5.02e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.95 E-value: 5.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 43 GSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllrnRALGFVYQFHHLLPEFTALENVcmpLLIGR---TP 119
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-----RRVGYMSQAFSLYGELTVRQNL---ELHARlfhLP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 120 IAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTS 199
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVT 450
|
170
....*....|....*..
gi 15598183 200 FLVVTHDLQLAGHMDRI 216
Cdd:NF033858 451 IFISTHFMNEAERCDRI 467
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-205 |
6.34e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 86.94 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 3 DKSVLSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGG--LDTPSAGSVWLAGEELSalnet 80
Cdd:COG2401 25 ERVAIVLEAFGVELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 argllrnralgfvyqfhhllPEFTALENVCMplligRTPIAEArqraAELLERVGLGHR--LSHKPAELSGGERQRVAIA 158
Cdd:COG2401 98 --------------------REASLIDAIGR-----KGDFKDA----VELLNAVGLSDAvlWLRRFKELSTGQKFRFRLA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTH 205
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-224 |
6.46e-21 |
|
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: 90.84 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsalnETARGLLRnRA 89
Cdd:TIGR01257 932 KNLVKIFE--PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQ----FHHLlpefTALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:TIGR01257 1005 LGMCPQhnilFHHL----TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTsFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRT-IIMSTHHMDEADLLgDRIAIISQGRL 1138
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-197 |
6.46e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 6.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSA---GSVWLAGEELSALN--ET 80
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNirDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARgllrnRALGFVYQFHHLLPEFTALENVCM---PLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:PRK13549 80 ER-----AGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598183 158 ARALVNRPQLVLLDEPTGNLdqhTAQGIQELmLELSRSLQ 197
Cdd:PRK13549 155 AKALNKQARLLILDEPTASL---TESETAVL-LDIIRDLK 190
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-225 |
1.29e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 40 AIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETAR--GLLRNRALGFVYQFHHLLPEFTALENVCMPLLI-G 116
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKShG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 117 RTPIAEARQRAAELLERVGLGH----RLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLEL 192
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170 180 190
....*....|....*....|....*....|....
gi 15598183 193 SRSLqtSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK14246 200 KNEI--AIVIVSHNPQQVARVaDYVAFLYNGELV 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-225 |
1.48e-20 |
|
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: 89.61 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAgeelsalnetargll 85
Cdd:TIGR03719 4 IYTMNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRALGFVYQFHHLLPEFTALENVCMPL-----LIGR---------TPIAE-----ARQraAELLERV--GLGHRLSHK- 143
Cdd:TIGR03719 66 PGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdALDRfneisakyaEPDADfdklaAEQ--AELQEIIdaADAWDLDSQl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 144 ---------P------AELSGGERQRVAIARALVNRPQLVLLDEPTGNLDqhtaqgiQELMLELSRSLQT---SFLVVTH 205
Cdd:TIGR03719 144 eiamdalrcPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-------AESVAWLERHLQEypgTVVAVTH 216
|
250 260
....*....|....*....|....
gi 15598183 206 DL----QLAGHmdrILRLEEGRLI 225
Cdd:TIGR03719 217 DRyfldNVAGW---ILELDRGRGI 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-226 |
1.54e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArgllrnralgFVYQFHHLLPEFT 104
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA----------FARKVAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVCMPLL--IGRTPI--------AEARQRAAELLERVGL---GHRLSHkpaELSGGERQRVAIARALVNRPQLVLLD 171
Cdd:PRK10575 96 AAEGMTVRELvaIGRYPWhgalgrfgAADREKVEEAISLVGLkplAHRLVD---SLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 172 EPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAG-HMDRILRLEEGRLIA 226
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIA 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-225 |
2.05e-20 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 89.02 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYdegPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAgeelsalnET 80
Cdd:PRK11819 1 MMAQYIYTMNRVSKVV---PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA--------PG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARgllrnraLGFVYQFHHLLPEFTALENVCMplliGRTPIAEARQR-----AA---------ELLERVGL---------G 137
Cdd:PRK11819 70 IK-------VGYLPQEPQLDPEKTVRENVEE----GVAEVKAALDRfneiyAAyaepdadfdALAAEQGElqeiidaadA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 138 HRLSHK-----------PAE-----LSGGERQRVAIARALVNRPQLVLLDEPTGNLDqhtaqgiQELMLELSRSLQT--- 198
Cdd:PRK11819 139 WDLDSQleiamdalrcpPWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-------AESVAWLEQFLHDypg 211
|
250 260 270
....*....|....*....|....*....|.
gi 15598183 199 SFLVVTHD---L-QLAGHmdrILRLEEGRLI 225
Cdd:PRK11819 212 TVVAVTHDryfLdNVAGW---ILELDRGRGI 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-226 |
3.39e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 86.19 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELS--ALNETARgllrnrALGFVYQFHHLLPE 102
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVAR------RIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 FTALENVCMplliGRTP--------IAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:PRK10253 96 ITVQELVAR----GRYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598183 175 GNLDQHTAQGIQELMLELSRSLQTSFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKIVA 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
10-225 |
3.98e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 3.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYD--EGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELsalNETARGLLRN 87
Cdd:PRK11176 345 RNVTFTYPgkEVP----ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 R-ALgfVYQFHHLLPEfTALENvcmplligrtpIAEARQ---------RAAEL---------LERvGLGHRLSHKPAELS 148
Cdd:PRK11176 418 QvAL--VSQNVHLFND-TIANN-----------IAYARTeqysreqieEAARMayamdfinkMDN-GLDTVIGENGVLLS 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 149 GGERQRVAIARALV-NRPQLVlLDEPTGNLDQHTAQGIQELMLELSRSlQTSfLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK11176 483 GGQRQRIAIARALLrDSPILI-LDEATSALDTESERAIQAALDELQKN-RTS-LVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-226 |
4.45e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:COG3845 257 VLEVENLSVRDDRG---VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 RNRALGFVYQ--FHH-LLPEFTALENVCMpLLIGRTPIA--------EARQRAAELLERVGL-GHRLSHKPAELSGGERQ 153
Cdd:COG3845 331 RRLGVAYIPEdrLGRgLVPDMSVAENLIL-GRYRRPPFSrggfldrkAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDL----QLAghmDRILRLEEGRLIA 226
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLdeilALS---DRIAVMYEGRIVG 482
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-225 |
9.49e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 9.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLD--TPSAGSVWLAGEELSAL--NETAR 82
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLppEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 -GLLrnraLGFVYQfhhllPEFTALENvcmplligrtpiaearqraAELLERVGLGhrlshkpaeLSGGERQRVAIARAL 161
Cdd:cd03217 77 lGIF----LAFQYP-----PEIPGVKN-------------------ADFLRYVNEG---------FSGGEKKRNEILQLL 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 162 VNRPQLVLLDEPTGNLD----QHTAQGIQELmlelsRSLQTSFLVVTHDLQLAGHM--DRILRLEEGRLI 225
Cdd:cd03217 120 LLEPDLAILDEPDSGLDidalRLVAEVINKL-----REEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIV 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-226 |
1.23e-19 |
|
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: 86.80 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSA--GSVWLAGEELSALN--ETA 81
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNirDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RgllrnRALGFVYQFHHLLPEFTALENVCMPLLI----GRTPIAEARQRAAELLERVGLGHRLSHKP-AELSGGERQRVA 156
Cdd:TIGR02633 77 R-----AGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 157 IARALVNRPQLVLLDEPTGNLdqhTAQGIqELMLELSRSLQ---TSFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSL---TEKET-EILLDIIRDLKahgVACVYISHKLnEVKAVCDTICVIRDGQHVA 221
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
20-225 |
1.27e-19 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 86.87 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRGLLRnRALGFVYQFHHL 99
Cdd:TIGR01192 345 ANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVT---RESLR-KSIATVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 100 LPEfTALENVCmpllIGRT-----PIAEARQRAAE---LLERV-GLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLL 170
Cdd:TIGR01192 421 FNR-SIRENIR----LGREgatdeEVYEAAKAAAAhdfILKRSnGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 171 DEPTGNLDQHTAQGIQELMLELSRSlQTSFlVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:TIGR01192 496 DEATSALDVETEARVKNAIDALRKN-RTTF-IIAHRLSTVRNADLVLFLDQGRLI 548
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-177 |
1.46e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNET 80
Cdd:PRK15439 6 TTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 argllRNRALG--FVYQFHHLLPEFTALENVcmplLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIA 158
Cdd:PRK15439 82 -----KAHQLGiyLVPQEPLLFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170
....*....|....*....
gi 15598183 159 RALVNRPQLVLLDEPTGNL 177
Cdd:PRK15439 153 RGLMRDSRILILDEPTASL 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-227 |
3.25e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.52 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 21 QSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsALNETARGLLRNRA-LGFVYQFHHL 99
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQqVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 100 LPEFTALE-NVCMPLLIGRTPIAEARQRAAELLERVGlGHRLSHKPAE-LSGGERQRVAIARALVNRPQLVLLDEPTGNL 177
Cdd:PRK13638 89 QIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598183 178 DqhtAQGIQELMLELSRSLQTSFLVV--THDLQLAGHM-DRILRLEEGRLIAA 227
Cdd:PRK13638 168 D---PAGRTQMIAIIRRIVAQGNHVIisSHDIDLIYEIsDAVYVLRQGQILTH 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-216 |
4.24e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPS----AGSVWLAGEELSALNETAR 82
Cdd:COG4170 4 LDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRNRALGFVYQ--FHHLLPEFTALENVC--MPLLIGRTPI----AEARQRAAELLERVGL-GHR--LSHKPAELSGGE 151
Cdd:COG4170 84 RKIIGREIAMIFQepSSCLDPSAKIGDQLIeaIPSWTFKGKWwqrfKWRKKRAIELLHRVGIkDHKdiMNSYPHELTEGE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRI 216
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWaDTI 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-225 |
4.25e-19 |
|
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: 81.69 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYdeGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLR 86
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRaLGFVYQfhhllpEFTalenvcmpLLIG--RTPI-AEARQRAAELLERVglghRLSHKPAELSGGERQRVAIARALVN 163
Cdd:cd03369 82 SS-LTIIPQ------DPT--------LFSGtiRSNLdPFDEYSDEEIYGAL----RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-188 |
5.93e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 23 VQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgllRNRALGFVYQFHHLLPE 102
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSS---QEAGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 FTALENVcmplLIGRTPI--------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:PRK10762 94 LTIAENI----FLGREFVnrfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170
....*....|....*...
gi 15598183 175 GNL-DQHTAQ---GIQEL 188
Cdd:PRK10762 170 DALtDTETESlfrVIREL 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-225 |
1.53e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKST-------LLNMLGGldTPSAGSVWLA--G 71
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGG--LVQCDKMLLRrrS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 72 EELSALNETARGLLR-----NRALGFVYQFHHLLPEFTALENVCMPLLI----GRTpiaEARQRAAELLERVGLGHR--- 139
Cdd:PRK10261 85 RQVIELSEQSAAQMRhvrgaDMAMIFQEPMTSLNPVFTVGEQIAESIRLhqgaSRE---EAMVEAKRMLDQVRIPEAqti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 140 LSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILR 218
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIaDRVLV 241
|
....*..
gi 15598183 219 LEEGRLI 225
Cdd:PRK10261 242 MYQGEAV 248
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
35-226 |
2.04e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLdTPSAGSVWLAGEELSALneTARGLLRNRAlgfvYQFHHLLPEFTalenvcMPL- 113
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW--SAAELARHRA----YLSQQQTPPFA------MPVf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 114 ------LIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL-----VNRP--QLVLLDEPTGNLDQH 180
Cdd:PRK03695 88 qyltlhQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 181 TAQGIQELMLELSRsLQTSFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:PRK03695 168 QQAALDRLLSELCQ-QGIAVVMSSHDLnHTLRHADRVWLLKQGKLLA 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-207 |
2.10e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 36 GERVAIVGSSGSGKSTLLNMLGGLdtpsagsVWLAGEELSALNETARGLLRNRALGFVYQFHHLLPEFTAL-ENVCMPLL 114
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGF-------VRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLvEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 115 IG-----RTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELM 189
Cdd:PRK15056 106 YGhmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLL 185
|
170
....*....|....*...
gi 15598183 190 LELsRSLQTSFLVVTHDL 207
Cdd:PRK15056 186 REL-RDEGKTMLVSTHNL 202
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-219 |
2.13e-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: 79.84 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELS-ALNETARGLLrnrALGFVYQFHHLLpef 103
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfQRDSIARGLL---YLGHAPGIKTTL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCMPLLIGrtpiaeARQRAAELLERVGLGHrLSHKP-AELSGGERQRVAIARALVNRPQLVLLDEPTGNLDqhtA 182
Cdd:cd03231 89 SVLENLRFWHADH------SDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD---K 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598183 183 QGIQELMLELSRSLQTSFLVV--TH-DLQLAGHMDRILRL 219
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVltTHqDLGLSEAGARELDL 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-225 |
2.82e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAG-----SVWLAGEELSALNETargLLRNRALGFVYQFHHL 99
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDV---LEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 100 LPeFTALENVCMPLLIGR-TPIAEARQRAAELLERVGL----GHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598183 175 GNLDQHTAQGIQELMLELSRSLqtSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARIsDRAALFFDGRLV 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-224 |
3.32e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSksyDEGpqsvqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETA 81
Cdd:PRK15439 264 AGAPVLTVEDLT---GEG------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RgllrnRALGFVY-----QFHHLLPEFTALENVCmPLLIGRTPIAEARQRAAELLERV--GLGHRLSHKPAE---LSGGE 151
Cdd:PRK15439 335 R-----LARGLVYlpedrQSSGLYLDAPLAWNVC-ALTHNRRGFWIKPARENAVLERYrrALNIKFNHAEQAartLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHM-DRILRLEEGRL 224
Cdd:PRK15439 409 QQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-222 |
4.85e-18 |
|
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: 79.30 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLL-NMLGGLDTPSAGSVWLAGEELSALNETARGllRNR-ALGFVYQFHHLLpEF 103
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRS--RNRySVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCMplligRTPIAEARQRAA----------ELLErVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEP 173
Cdd:cd03290 94 TVEENITF-----GSPFNKQRYKAVtdacslqpdiDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598183 174 TGNLDQHTAQGI-QELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEG 222
Cdd:cd03290 168 FSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-226 |
8.03e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.87 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSA--------GSVWLAGEELSALNetARGLLRNRAlgfvyqf 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAID--APRLARLRA------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 97 hhLLPE-------FTALENVcmplLIGRTPIAEA--------RQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARAL 161
Cdd:PRK13547 87 --VLPQaaqpafaFSAREIV----LLGRYPHARRagalthrdGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 162 VN---------RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAG-HMDRILRLEEGRLIA 226
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVA 235
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-211 |
9.66e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.44 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDegpqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLL---NMLGGLdTPSA---GSVWLAGEELSAlNE 79
Cdd:PRK14243 10 VLRTENLNVYYG----SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDL-IPGFrveGKVTFHGKNLYA-PD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 80 TARGLLRNRaLGFVYQFHHLLPEfTALENVCM-PLLIGRT----PIAEARQRAAELLERVGlgHRLSHKPAELSGGERQR 154
Cdd:PRK14243 84 VDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYgARINGYKgdmdELVERSLRQAALWDEVK--DKLKQSGLSLSGGQQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 155 VAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslQTSFLVVTHDLQLAG 211
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAA 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-220 |
1.03e-17 |
|
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: 77.19 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlageelsalnetarGLLRNRALGFVYQfHHL 99
Cdd:cd03223 11 PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------GMPEGEDLLFLPQ-RPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 100 LPEFTALENVCMPLLIgrtpiaearqraaellervglghrlshkpaELSGGERQRVAIARALVNRPQLVLLDEPTGNLDq 179
Cdd:cd03223 75 LPLGTLREQLIYPWDD------------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALD- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598183 180 htaQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLE 220
Cdd:cd03223 124 ---EESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-206 |
3.54e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 79.59 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlageelsALNETARgll 85
Cdd:TIGR03719 322 VIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------EIGETVK--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnraLGFVYQFH-HLLPEFTALENVCMPLLIGRTPIAEARQRA---------AELLERVGlghrlshkpaELSGGERQRV 155
Cdd:TIGR03719 387 ----LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRV 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLqtsfLVVTHD 206
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCA----VVISHD 499
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-224 |
5.48e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.25 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVqvlSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARGLLR 86
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 87 NRALGFVYQFHHLL-PEFTALENvcmplligrtpiaearQRAAELLERVGLGHRLSHKPAE-----LSGGERQRVAIARA 160
Cdd:PRK10522 400 SAVFTDFHLFDQLLgPEGKPANP----------------ALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598183 161 LVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
7-225 |
7.65e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 76.53 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDT--PSAGSVWLAGEELSAL--NETAR 82
Cdd:TIGR01978 1 LKIKDLHVSVEDKE----ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELepDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 -GLLrnraLGFvyQFHHLLP-----EF--TALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAE--LSGGER 152
Cdd:TIGR01978 77 aGLF----LAF--QYPEEIPgvsnlEFlrSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNegFSGGEK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 153 QRVAIARALVNRPQLVLLDEPTGNLD----QHTAQGIQELmlelsRSLQTSFLVVTHDLQLAGHM--DRILRLEEGRLI 225
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDidalKIVAEGINRL-----REPDRSFLIITHYQRLLNYIkpDYVHVLLDGRIV 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-209 |
1.13e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 78.29 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlageelsalnetarGLLRNRALGFVYQfhHLLPEFT 104
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---------------GLAKGIKLGYFAQ--HQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENvcmPLL-IGRTPIAEARQRAAELLERVGL-GHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTA 182
Cdd:PRK10636 390 ADES---PLQhLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180
....*....|....*....|....*..
gi 15598183 183 QGIQELMLELSRSLqtsfLVVTHDLQL 209
Cdd:PRK10636 467 QALTEALIDFEGAL----VVVSHDRHL 489
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2-223 |
1.15e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAgsvwLAGEELSALNETA 81
Cdd:PLN03211 60 NIKRILGHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLLRNraLGFVYQFHHLLPEFTALENV--CMPLLIGRTPIAEARQRAAE-LLERVGL--------GHRLSHKpaeLSGG 150
Cdd:PLN03211 136 KQILKR--TGFVTQDDILYPHLTVRETLvfCSLLRLPKSLTKQEKILVAEsVISELGLtkcentiiGNSFIRG---ISGG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAqgiQELMLELSRSLQTSFLVVTHDLQLAGHM----DRILRLEEGR 223
Cdd:PLN03211 211 ERKRVSIAHEMLINPSLLILDEPTSGLDATAA---YRLVLTLGSLAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGR 284
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-226 |
1.21e-16 |
|
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: 77.92 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSY--DEGPQSVQVlsG-VELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNetaRG 83
Cdd:COG4615 328 LELRGVTYRYpgEDGDEGFTL--GpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---RE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRNRalgF--VYQFHHLLPEftalenvcmplLIGRTPIAEArQRAAELLERVGLGHRLSHK-----PAELSGGERQRVA 156
Cdd:COG4615 403 AYRQL---FsaVFSDFHLFDR-----------LLGLDGEADP-ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLA 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 157 IARALV-NRPqLVLLDEPTGnlDQ--------HTaqgiqELMLELsRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:COG4615 468 LLVALLeDRP-ILVFDEWAA--DQdpefrrvfYT-----ELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-216 |
3.03e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.99 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTP----SAGSVWLAGEELSALNETA 81
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLLRNRALGFVYQF-HHLLPEFTALENVCMPLLIGRTPIAEARQ-------RAAELLERVGL-GHR--LSHKPAELSGG 150
Cdd:PRK15093 83 RRKLVGHNVSMIFQEpQSCLDPSERVGRQLMQNIPGWTYKGRWWQrfgwrkrRAIELLHRVGIkDHKdaMRSFPYELTEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRI 216
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWaDKI 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-222 |
6.72e-16 |
|
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: 73.05 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTpsAGSVwlAGEELsaLNETARG 83
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKT--AGVI--TGEIL--INGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRNRALGFVYQFHHLLPEFTALENVcmplligrtpiaearqraaellervglghRLSHKPAELSGGERQRVAIARALVN 163
Cdd:cd03232 75 KNFQRSTGYVEQQDVHSPNLTVREAL-----------------------------RFSALLRGLSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 164 RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTH--DLQLAGHMDRILRLEEG 222
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQA-ILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-225 |
8.63e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.97 E-value: 8.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDegpqsVQVLSGVELNLLPGERVAIVGSSGSGKStlLNMLGGLDTPSAGSVWLAGEELSALNETARGL 84
Cdd:PRK10418 3 QQIELRNIALQAA-----QPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFVYQ-----FHHLLPEFTALENVCMPLliGRTPiaeARQRAAELLERVGLGHR---LSHKPAELSGGERQRVA 156
Cdd:PRK10418 76 LRGRKIATIMQnprsaFNPLHTMHTHARETCLAL--GKPA---DDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHM-DRILRLEEGRLI 225
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIV 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-209 |
1.96e-15 |
|
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: 74.44 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGpqSVQVLSGvELNllPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlaGEEL----------SALNET 80
Cdd:COG1245 346 DLTKSYGGF--SLEVEGG-EIR--EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLkisykpqyisPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARGLLRNralgfvyqfhHLLPEFTalenvcmplligrTPIAEArqraaELLERVGLgHRLSHKP-AELSGGERQRVAIAR 159
Cdd:COG1245 418 VEEFLRS----------ANTDDFG-------------SSYYKT-----EIIKPLGL-EKLLDKNvKDLSGGELQRVAIAA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598183 160 ALVNRPQLVLLDEPTGNLD--Q--HTAQGIQELMLELSRSLqtsfLVVTHDLQL 209
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDveQrlAVAKAIRRFAENRGKTA----MVVDHDIYL 518
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-224 |
6.25e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 73.36 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQSVQVLS-GVELNllpgERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnetarg 83
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLNfGIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA------- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 llrnralgfVYQFHHLlpefTALENVCMPLL-IGRTPIAEARQRAAELLERVGLGHRLSHKPA-ELSGGERQRVAIARAL 161
Cdd:PLN03073 576 ---------VFSQHHV----DGLDLSSNPLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKIT 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 162 VNRPQLVLLDEPTGNLDQHTAQG-IQELMLelsrsLQTSFLVVTHDLQL-AGHMDRILRLEEGRL 224
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDAVEAlIQGLVL-----FQGGVLMVSHDEHLiSGSVDELWVVSEGKV 702
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-225 |
8.53e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegPqSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSA---GSVWLAGEELSAlnetaR 82
Cdd:NF040905 1 ILEMRGITKTF---P-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGEVCRF-----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRNRALGFV--YQFHHLLPEFTALENVCMPLLIGRTPI---AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAI 157
Cdd:NF040905 71 DIRDSEALGIViiHQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLvVTHDL----QLAghmDRILRLEEGRLI 225
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLneirRVA---DSITVLRDGRTI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-220 |
1.99e-14 |
|
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: 70.13 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPG-----ERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSalnetargllrnralgfvY 94
Cdd:cd03237 4 PTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------------Y 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 95 QFHHLLPEFtalENVCMPLLIGRTPIA-EARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEP 173
Cdd:cd03237 66 KPQYIKADY---EGTVRDLLSSITKDFyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598183 174 TGNLDQ----HTAQGIQELMLELSRslqTSFlVVTHDLQLAGHM-DRILRLE 220
Cdd:cd03237 143 SAYLDVeqrlMASKVIRRFAENNEK---TAF-VVEHDIIMIDYLaDRLIVFE 190
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
11-217 |
2.65e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 11 NLSKSYDEGpqSVQVLSGvELNllPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwLAGEELS--------ALNETAR 82
Cdd:PRK13409 345 DLTKKLGDF--SLEVEGG-EIY--EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISykpqyikpDYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRN--RALGFVYQFHhllpeftalenvcmplligrtpiaearqraaELLERVGLGHRLSHKPAELSGGERQRVAIARA 160
Cdd:PRK13409 419 DLLRSitDDLGSSYYKS-------------------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAAC 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 161 LVNRPQLVLLDEPTGNLD--QH--TAQGIQELMlelsRSLQTSFLVVTHDLQLAGHM-DRIL 217
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDveQRlaVAKAIRRIA----EEREATALVVDHDIYMIDYIsDRLM 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-225 |
3.39e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGG---------------------LDTPS 63
Cdd:PRK11147 2 SLISIHGAWLSFSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqQDPPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 64 A--GSVW-LAGEELSALNEtargLLRnralgfvyQFHHLLpefTALENVCMPLLIGRTPIAEAR----------QRAAEL 130
Cdd:PRK11147 78 NveGTVYdFVAEGIEEQAE----YLK--------RYHDIS---HLVETDPSEKNLNELAKLQEQldhhnlwqleNRINEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 131 LERVGLGhrlSHKP-AELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLelsrSLQTSFLVVTHDLQL 209
Cdd:PRK11147 143 LAQLGLD---PDAAlSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSF 215
|
250
....*....|....*..
gi 15598183 210 AGHM-DRILRLEEGRLI 225
Cdd:PRK11147 216 IRNMaTRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-225 |
3.98e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRnRALGFVYQFHHL 99
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LR-RVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 100 --------LPEFTALENVCMPLLIGRTPIAEARQRAAellerVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLD 171
Cdd:PLN03232 1322 fsgtvrfnIDPFSEHNDADLWEALERAHIKDVIDRNP-----FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598183 172 EPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-207 |
4.53e-14 |
|
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: 70.58 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-----W------LAGEELSA-LNETARGLLRnralgFVY--QFHHLL 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepsWdevlkrFRGTELQDyFKKLANGEIK-----VAHkpQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 101 PEF------TALENVcmplligrtpiaEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPT 174
Cdd:COG1245 173 PKVfkgtvrELLEKV------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598183 175 GNLDQH----TAQGIQELMLElsrslQTSFLVVTHDL 207
Cdd:COG1245 241 SYLDIYqrlnVARLIRELAEE-----GKYVLVVEHDL 272
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-225 |
7.05e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALnetarGL--LRNRaLGFVYQfh 97
Cdd:PLN03130 1249 PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF-----GLmdLRKV-LGIIPQ-- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 98 hllpeftalenvcMPLLIGRT------PIAEarQRAAEL---LER-----------VGLGHRLSHKPAELSGGERQRVAI 157
Cdd:PLN03130 1321 -------------APVLFSGTvrfnldPFNE--HNDADLwesLERahlkdvirrnsLGLDAEVSEAGENFSVGQRQLLSL 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 158 ARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlqTSFLVVTHDLQLAGHMDRILRLEEGRLI 225
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-207 |
1.42e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-----W------LAGEELSALNEtargLLRNRALGFVY--QFHHLLP 101
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepsWdevlkrFRGTELQNYFK----KLYNGEIKVVHkpQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EF---TALEnvcmpLLIGrtpiAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLD 178
Cdd:PRK13409 174 KVfkgKVRE-----LLKK----VDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180 190
....*....|....*....|....*....|...
gi 15598183 179 --QH--TAQGIQELmlelsrSLQTSFLVVTHDL 207
Cdd:PRK13409 245 irQRlnVARLIREL------AEGKYVLVVEHDL 271
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-222 |
2.36e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsalnetargllrnraLGFVYQFHHLLPEfT 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVcmplLIGRTpIAEARQR----AAELLERVGLGHRLSHKP-----AELSGGERQRVAIARALVNRPQLVLLDEPTG 175
Cdd:TIGR01271 503 IKDNI----IFGLS-YDEYRYTsvikACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598183 176 NLDQHTAQGIQE-----LMLELSRslqtsfLVVTHDLQLAGHMDRILRLEEG 222
Cdd:TIGR01271 578 HLDVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-206 |
2.51e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEgpqsvQVL-SGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVwlageelsALNETARgl 84
Cdd:PRK11819 324 VIEAENLSKSFGD-----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI--------KIGETVK-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 lrnraLGFVYQFH-HLLPEFTALENVCMPL---LIGRTpiaEARQRA---------AELLERVGlghrlshkpaELSGGE 151
Cdd:PRK11819 389 -----LAYVDQSRdALDPNKTVWEEISGGLdiiKVGNR---EIPSRAyvgrfnfkgGDQQKKVG----------VLSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLElsrslqtsF----LVVTHD 206
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE--------FpgcaVVISHD 501
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-224 |
5.17e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSkSYDEGPqsvqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEEL---SAL 77
Cdd:PRK09700 260 LAHETVFEVRNVT-SRDRKK-----VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 78 NETARGLL----RNRALGFvyqfhhlLPEFTALENVCMPL---------LIGRTPIAEARQRAAELLERVGLG-HRLSHK 143
Cdd:PRK09700 334 DAVKKGMAyiteSRRDNGF-------FPNFSIAQNMAISRslkdggykgAMGLFHEVDEQRTAENQRELLALKcHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 144 PAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGR 223
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
.
gi 15598183 224 L 224
Cdd:PRK09700 487 L 487
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-222 |
6.16e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.46 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLN-MLGGLDTPSAGSVWLAGeelsalnetargllrnrALGFVYQFHHLLpEFT 104
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------------TVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVcmplLIGRTPIAEARQRAAELlerVGLGHRLSHKPA-----------ELSGGERQRVAIARALVNRPQLVLLDEP 173
Cdd:PLN03130 695 VRDNI----LFGSPFDPERYERAIDV---TALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 174 TGNLDQHTAQGIQELMLELSRSLQTSFLvVTHDLQLAGHMDRILRLEEG 222
Cdd:PLN03130 768 LSALDAHVGRQVFDKCIKDELRGKTRVL-VTNQLHFLSQVDRIILVHEG 815
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-226 |
1.18e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.91 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 4 KSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSG--KSTLLNMLGGLDT---PSAGSVWLAGEElsALN 78
Cdd:NF000106 11 RNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrPWRF*TWCANRR--ALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 ETArGLLRNRALGfvyqfhhLLPEFTALENVCMpllIGRT---PIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRV 155
Cdd:NF000106 85 RTI-G*HRPVR*G-------RRESFSGRENLYM---IGR*ldlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRLIA 226
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-208 |
1.45e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 2 NDKSVLSCRNLSKSYD--EGPQSVQVLSGVElnllPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEE-LSALN 78
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSgtSSPAVDRLCVGVR----PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 79 EtargllrnralgfVYQFHHLLPEFTALENvcmpLLIGRTPI---AEARQRAAELLERV--------GLGHRLSHKPAEL 147
Cdd:TIGR01257 2009 D-------------VHQNMGYCPQFDAIDD----LLTGREHLylyARLRGVPAEEIEKVanwsiqslGLSLYADRLAGTY 2071
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 148 SGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDLQ 208
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSME 2131
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-225 |
1.47e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-WlageelsalNETARgll 85
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkW---------SENAN--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnraLGFVYQFHHllPEFTALENVC--MplligrtpiAEARQ-RAAELLERVGLGHRL-----SHKPAE-LSGGERQRVA 156
Cdd:PRK15064 384 ----IGYYAQDHA--YDFENDLTLFdwM---------SQWRQeGDDEQAVRGTLGRLLfsqddIKKSVKvLSGGEKGRML 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598183 157 IARALVNRPQLVLLDEPTGNLDQhtaQGIQELMLELSRsLQTSFLVVTHDLQ----LAghmDRILRLEEGRLI 225
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEK-YEGTLIFVSHDREfvssLA---TRIIEITPDGVV 514
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-222 |
3.82e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 64.11 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelsalnetargllrnraLGFVYQFHHLLPEfT 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVcmplLIGrtpIAEARQRAAELLERVGLGHRLSHKPAE-----------LSGGERQRVAIARALVNRPQLVLLDEP 173
Cdd:cd03291 114 IKENI----IFG---VSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598183 174 TGNLDQHTAQGIQE-----LMLELSRSLqtsflvVTHDLQLAGHMDRILRLEEG 222
Cdd:cd03291 187 FGYLDVFTEKEIFEscvckLMANKTRIL------VTSKMEHLKKADKILILHEG 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-225 |
4.46e-12 |
|
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: 62.67 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 5 SVLSCRNLSKSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGlDTPSAGSVwlageelsalnetaRGL 84
Cdd:cd03233 2 STLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN-RTEGNVSV--------------EGD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LR---NRALGFVYQFHHLLpEFTALENVCMPLLIGRtpiaearqraaELLERVGL--GHRLSHKpaeLSGGERQRVAIAR 159
Cdd:cd03233 67 IHyngIPYKEFAEKYPGEI-IYVSEEDVHFPTLTVR-----------ETLDFALRckGNEFVRG---ISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 160 ALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVThdLQLAGHM----DRILRLEEGRLI 225
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL--YQASDEIydlfDKVLVLYEGRQI 199
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-181 |
4.73e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 36 GERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWL-AGEELSALNETARGLLRNRALGFVYQFHHLL-------------P 101
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFAFEEFTVLDTVIMGHTELwevkqerdriyalP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EFTalENVCMPLLIGRTPIAE-----ARQRAAELLERVGLGHRLSHKP-AELSGGERQRVAIARALVNRPQLVLLDEPTG 175
Cdd:PRK15064 107 EMS--EEDGMKVADLEVKFAEmdgytAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184
|
....*.
gi 15598183 176 NLDQHT 181
Cdd:PRK15064 185 NLDINT 190
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-205 |
5.28e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEElsalNET 80
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEP----VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT----ATR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 81 ARgllRNRALGFVYQFHHLLPEFTALENV-CMPLLIGRTPiaeaRQRAAELLERVGLGHRLSHKPAELSGGERQRVAIAR 159
Cdd:PRK13543 78 GD---RSRFMAYLGHLPGLKADLSTLENLhFLCGLHGRRA----KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598183 160 ALVNRPQLVLLDEPTGNLDqhtAQGIQELMLELSRSLQT--SFLVVTH 205
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLD---LEGITLVNRMISAHLRGggAALVTTH 195
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-222 |
5.33e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLN-MLGGLDTPSAGSVWLAGEELSA------LNETARgllRNRALGFVYQfhh 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAYVpqvswiFNATVR---ENILFGSDFE--- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 llpeftalenvcmPLLIGRTPIAEARQRAAELL---ERVGLGHRlshkPAELSGGERQRVAIARALVNRPQLVLLDEPTG 175
Cdd:PLN03232 707 -------------SERYWRAIDVTALQHDLDLLpgrDLTEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 176 NLDQHTAQGIQELMLELSRSLQTSFLvVTHDLQLAGHMDRILRLEEG 222
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVL-VTNQLHFLPLMDRIILVSEG 815
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
35-224 |
6.22e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.42 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGE-ELSALNETARGLLRNrALGFVYQFHHllpEFTALENV---- 109
Cdd:PRK10636 26 PGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQP-ALEYVIDGDR---EYRQLEAQlhda 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 -------CMPLLIGRTPIAEA---RQRAAELLERVGLGH-RLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLD 178
Cdd:PRK10636 102 nerndghAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 179 QHTAQGIQELMlelsRSLQTSFLVVTHDLQ-LAGHMDRILRLEEGRL 224
Cdd:PRK10636 182 LDAVIWLEKWL----KSYQGTLILISHDRDfLDPIVDKIIHIEQQSL 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-205 |
1.19e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGlDTPSAGS--VWLAGEELSAlNETARGLLRN 87
Cdd:PRK10938 264 NNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGYSndLTLFGRRRGS-GETIWDIKKH 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 88 raLGFVYQFHHLlpEF---TALENVCMPLLIGRTPIAEA-----RQRAAELLERVGLGHRLSHKP-AELSGGERQRVAIA 158
Cdd:PRK10938 338 --IGYVSSSLHL--DYrvsTSVRNVILSGFFDSIGIYQAvsdrqQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIV 413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 159 RALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTH 205
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-204 |
1.32e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPsagsvwLAGEELSALNETARgllrnraLGFvYQFHHLLPEF 103
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPL------LSGERQSQFSHITR-------LSF-EQLQKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCM----PLLIGRTpIAE-------ARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDE 172
Cdd:PRK10938 83 WQRNNTDMlspgEDDTGRT-TAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190
....*....|....*....|....*....|..
gi 15598183 173 PTGNLDQHTAQGIQELMLELSRSLQTSFLVVT 204
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVLVLN 193
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-207 |
1.58e-11 |
|
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: 62.00 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV-----W------LAGEELSALNETarglLRNRALGFVY--QFHHLLP 101
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdWdeildeFRGSELQNYFTK----LLEGDVKVIVkpQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 102 EfTALENVCmpLLIGRTpiaEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLD--Q 179
Cdd:cd03236 101 K-AVKGKVG--ELLKKK---DERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikQ 174
|
170 180 190
....*....|....*....|....*....|
gi 15598183 180 H--TAQGIQELMLElsrslQTSFLVVTHDL 207
Cdd:cd03236 175 RlnAARLIRELAED-----DNYVLVVEHDL 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-222 |
3.92e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 24 QVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTpsaGSVWLAGEELSalNETARGLLRNRALGFVYQFHHLLPEF 103
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLV--NGRPLDSSFQRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 104 TALENVCMPLLIGR---TPIAEAR---QRAAELLERVGLGHRLSHKPAE-LSGGERQRVAIARALVNRPQLVL-LDEPTG 175
Cdd:TIGR00956 852 TVRESLRFSAYLRQpksVSKSEKMeyvEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 176 NLDQHTAQGIQELMLELSRSLQTsFLVVTH--DLQLAGHMDRILRLEEG 222
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLADHGQA-ILCTIHqpSAILFEEFDRLLLLQKG 979
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-208 |
4.72e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 32 NLLPGERVAIVGSSGSGKSTLLN-MLGGLdTPSAGSVWlAGEELsalnETArgllrnralgFVYQFHHLL-PEFTALENV 109
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKlMLGQL-QADSGRIH-CGTKL----EVA----------YFDQHRAELdPEKTVMDNL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 110 cmplligrtpiAEARQRaaellerVGLGHRLSH------------KPA-----ELSGGERQRVAIARALVNRPQLVLLDE 172
Cdd:PRK11147 405 -----------AEGKQE-------VMVNGRPRHvlgylqdflfhpKRAmtpvkALSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598183 173 PTGNLDQHTAqgiqELMLELSRSLQTSFLVVTHDLQ 208
Cdd:PRK11147 467 PTNDLDVETL----ELLEELLDSYQGTVLLVSHDRQ 498
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-174 |
4.80e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSalNETAR--- 82
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRrav 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 ---------GLLRNralgfvyqfhhLLPEFTALENV-CMPLLIGRTPiAEARQRAAELLERVGLgHRLSHKPA-ELSGGE 151
Cdd:NF033858 75 cpriaympqGLGKN-----------LYPTLSVFENLdFFGRLFGQDA-AERRRRIDELLRATGL-APFADRPAgKLSGGM 141
|
170 180
....*....|....*....|...
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPT 174
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-209 |
7.20e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETARgll 85
Cdd:PRK13540 1 MLDVIELDFDYHDQP----LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVYQFHHLLPEFTALENVCMPLLIGRTPIAearqrAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:PRK13540 74 --KQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598183 166 QLVLLDEPTGNLDQHTAQGIQElMLELSRSLQTSFLVVTH-DLQL 209
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIIT-KIQEHRAKGGAVLLTSHqDLPL 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-224 |
1.23e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 23 VQVLSG-----VELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlNETARGLlrnrALGFVY--- 94
Cdd:PRK10762 260 VDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-RSPQDGL----ANGIVYise 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 95 --QFHHLLPEFTALENVCMPLLIGRTPIAEARQRAAELL-----------------ERVGLghrlshkpaeLSGGERQRV 155
Cdd:PRK10762 335 drKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQavsdfirlfniktpsmeQAIGL----------LSGGNQQKV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 156 AIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-225 |
2.09e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEGPqsvqVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLD--TPSAGSVWLAGEELSALNETARG 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 llrNRALGFVYQFHHLLPeftaleNVCMPLLIgRTPIAEARQ-RAAELLERVGLGHRLSHK------PAEL--------- 147
Cdd:PRK09580 77 ---GEGIFMAFQYPVEIP------GVSNQFFL-QTALNAVRSyRGQEPLDRFDFQDLMEEKiallkmPEDLltrsvnvgf 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 148 SGGERQRVAIARALVNRPQLVLLDEPTGNLD----QHTAQGIQELmlelsRSLQTSFLVVTHDLQLAGHM--DRILRLEE 221
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDidalKIVADGVNSL-----RDGKRSFIIVTHYQRILDYIkpDYVHVLYQ 221
|
....
gi 15598183 222 GRLI 225
Cdd:PRK09580 222 GRIV 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-226 |
2.65e-10 |
|
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: 59.45 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSkSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNML-GGLDTPSAGSVWLAGEEL---SALNETA 81
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVdirNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 82 RGLL-----RNRalgfvyqfHHLLPEFTALENVCMPLL---IGRTPIAEARQRAAELLERVGLGHRLSHKP---AELSGG 150
Cdd:TIGR02633 336 AGIAmvpedRKR--------HGIVPILGVGKNITLSVLksfCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpiGRLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598183 151 ERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDL-QLAGHMDRILRLEEGRLIA 226
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELaEVLGLSDRVLVIGEGKLKG 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-224 |
3.93e-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: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelsalnetargllrnrALGFVYQfHHLLPEFTA 105
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------------SVAYVPQ-QAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 106 LENVcmplLIGRtPIAEARQRA-----AEL--LERVGLGHR--LSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGN 176
Cdd:TIGR00957 716 RENI----LFGK-ALNEKYYQQvleacALLpdLEILPSGDRteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 177 LDQHTAQGIQELMLELSRSLQT-SFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGPEGVLKNkTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-217 |
4.67e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 4.67e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRIL 217
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-205 |
6.80e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 1 MNDKSVLSCRNLSKSYDEgpqsVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGldTPS----AGSVWLAGEELSA 76
Cdd:CHL00131 2 NKNKPILEIKNLHASVNE----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 77 LNETAR---GLLrnraLGFVY--------------------QFHHLLPEFTALENVcmplligrtpiaearQRAAELLER 133
Cdd:CHL00131 76 LEPEERahlGIF----LAFQYpieipgvsnadflrlaynskRKFQGLPELDPLEFL---------------EIINEKLKL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 134 VGLG-HRLSHKPAE-LSGGERQRVAIARALVNRPQLVLLDEPTGNLD----QHTAQGIQELMlelsrSLQTSFLVVTH 205
Cdd:CHL00131 137 VGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLM-----TSENSIILITH 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
147-220 |
9.19e-10 |
|
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: 56.46 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQ------RVAIARALVNRPQLVLLDEPTGNLD-QHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILRL 219
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
.
gi 15598183 220 E 220
Cdd:cd03240 196 E 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-222 |
1.74e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSA--LNEtarglLRnRALGFVYQfHHLLPE 102
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRE-----LR-RQFSMIPQ-DPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 FTALENVcmplligrTPIAEARQ----RAAELL---ERV-----GLGHRLSHKPAELSGGERQRVAIARALVNRPQ-LVL 169
Cdd:PTZ00243 1398 GTVRQNV--------DPFLEASSaevwAALELVglrERVaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFIL 1469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598183 170 LDEPTGNLDQHTAQGIQELMlelsRSLQTSFLVVT--HDLQLAGHMDRILRLEEG 222
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATV----MSAFSAYTVITiaHRLHTVAQYDKIIVMDHG 1520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-177 |
2.14e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYdegpQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSAlnETARGLLRNrA 89
Cdd:PRK10982 2 SNISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEALEN-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFVYQFHHLLPEFTALENvcmpLLIGRTPI-------AEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALV 162
Cdd:PRK10982 75 ISMVHQELNLVLQRSVMDN----MWLGRYPTkgmfvdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFS 150
|
170
....*....|....*
gi 15598183 163 NRPQLVLLDEPTGNL 177
Cdd:PRK10982 151 YNAKIVIMDEPTSSL 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-224 |
2.87e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGE-ELSALNETARGLLrnralgfvyqfhhllpefT 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQL------------------T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 105 ALENVCMPLLIGRTPIAEARQRAAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQG 184
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598183 185 IQELMLELSRSLQTSFLvVTHDL-QLAGHMDRILRLEEGRL 224
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFF-VSHNLgQVRQFCTKIAWIEGGKL 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-222 |
3.09e-09 |
|
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: 54.50 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 137 GHRLSHKPA--ELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQ----HTAQGIQELMLELSRSLqtsfLVVTHDLQLA 210
Cdd:cd03222 60 GITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTA----LVVEHDLAVL 135
|
90
....*....|..
gi 15598183 211 GHMDRILRLEEG 222
Cdd:cd03222 136 DYLSDRIHVFEG 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-219 |
4.36e-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: 53.90 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 23 VQVLSGVELNLLpgervAIVGSSGSGKSTLLNMLGgldtpsagsvwlageelsalnetargllrnraLGFVYQFHHLLPE 102
Cdd:cd03227 13 PNDVTFGEGSLT-----IITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 103 FTALENVcmplligrtpiaearQRAAELLERVGLGHRLShkpaelsGGERQRVAIARAL----VNRPQLVLLDEPTGNLD 178
Cdd:cd03227 56 SGVKAGC---------------IVAAVSAELIFTRLQLS-------GGEKELSALALILalasLKPRPLYILDEIDRGLD 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598183 179 QHTAQGIQELMLELSRSlQTSFLVVTHDLQLAGHMDRILRL 219
Cdd:cd03227 114 PRDGQALAEAILEHLVK-GAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-216 |
4.92e-09 |
|
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: 54.57 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLL---------------------NMLGGLDTPSAGSVwlagEELS-ALNETARG 83
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSI----EGLSpAIAIDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 84 LLRN-RA-LGFVYQFHHLLPeftalenvcmpLLIGRTPIaeaRQRAAELLErVGLGH-RLSHKPAELSGGERQRVAIARA 160
Cdd:cd03270 87 TSRNpRStVGTVTEIYDYLR-----------LLFARVGI---RERLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRLATQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 161 LVNRPQLVL--LDEPTGNLDQHTAQGIQELMLELsRSLQTSFLVVTHDLQLAGHMDRI 216
Cdd:cd03270 152 IGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
123-205 |
5.47e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 123 ARQRAAELLERVGLGHRLSHKPAE-LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRslqtSFL 201
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFI 395
|
....
gi 15598183 202 VVTH 205
Cdd:PLN03073 396 VVSH 399
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-224 |
6.91e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 141 SHKPA--ELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTSFLVVTHDLQLAGHMDRILR 218
Cdd:PRK10982 384 GHRTQigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILV 463
|
....*.
gi 15598183 219 LEEGRL 224
Cdd:PRK10982 464 MSNGLV 469
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
6-179 |
8.99e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSKSYDEgpqsvQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGeelSALNETARGLl 85
Cdd:PRK13541 1 MLSLHQLQFNIEQ-----KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKN---CNINNIAKPY- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnraLGFVYQFHHLLPEFTALENVCMPLLIGRTpiAEARQRAAELLErvgLGHRLSHKPAELSGGERQRVAIARALVNRP 165
Cdd:PRK13541 72 ----CTYIGHNLGLKLEMTVFENLKFWSEIYNS--AETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170
....*....|....
gi 15598183 166 QLVLLDEPTGNLDQ 179
Cdd:PRK13541 143 DLWLLDEVETNLSK 156
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-224 |
9.74e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 25 VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLA------GEELSALNETARGllrnRALGFVyqfhh 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAErsiayvPQQAWIMNATVRG----NILFFD----- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 llPEFTA-LENV--CMPLLigrtpiAEARQRAAellervGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTG 175
Cdd:PTZ00243 746 --EEDAArLADAvrVSQLE------ADLAQLGG------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598183 176 NLDQHTAQGIQELMLeLSRSLQTSFLVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:PTZ00243 812 ALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-222 |
1.35e-08 |
|
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: 54.57 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLlnMLGgldtpsagsvwlageeLSALNETARGLLRNRA 89
Cdd:TIGR00957 1288 RNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSL--TLG----------------LFRINESAEGEIIIDG 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 90 LGFV-YQFHHLLPEFTALENvcMPLLIGRT------PIAEARQRaaELLERVGLGH----------RLSHKPAE----LS 148
Cdd:TIGR00957 1348 LNIAkIGLHDLRFKITIIPQ--DPVLFSGSlrmnldPFSQYSDE--EVWWALELAHlktfvsalpdKLDHECAEggenLS 1423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 149 GGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQElmlelsrSLQTSF-----LVVTHDLQLAGHMDRILRLEEG 222
Cdd:TIGR00957 1424 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS-------TIRTQFedctvLTIAHRLNTIMDYTRVIVLDKG 1495
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-221 |
2.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.61 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 35 PGERVAIVGSSGSGKSTLLNMLGG-LDTPSAGSVWLAGEELsalnetargllrnralgfvyqfhhllpeftalenvcmpl 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 114 ligrtpiaearqraAELLERVGLGHRLSHKPAELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQEL----- 188
Cdd:smart00382 42 --------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|...
gi 15598183 189 MLELSRSLQTSFLVVTHDLQLAGHMDRILRLEE 221
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-224 |
2.79e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 6 VLSCRNLSkSYDEGPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNML-GGLDTPSAGSVWLAGEELsalneTARGL 84
Cdd:PRK13549 259 ILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV-----KIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFVY-----QFHHLLPEFTALENVCMPLL---IGRTPIAEARQRAAELLERVGLGHRLSH---KPAELSGGERQ 153
Cdd:PRK13549 333 QQAIAQGIAMvpedrKRDGIVPVMGVGKNITLAALdrfTGGSRIDDAAELKTILESIQRLKVKTASpelAIARLSGGNQQ 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDL-QLAGHMDRILRLEEGRL 224
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELpEVLGLSDRVLVMHEGKL 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-200 |
2.87e-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: 53.76 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTpSAGSVWLAGEELSALN-ETARgll 85
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTlQTWR--- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 86 rnRALGFVYQFHHLLPEfTALENVcmplligrTPIAE-ARQRAAELLERVGLGHRLSHKPAE-----------LSGGERQ 153
Cdd:TIGR01271 1292 --KAFGVIPQKVFIFSG-TFRKNL--------DPYEQwSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQelmlelsRSLQTSF 200
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIR-------KTLKQSF 1400
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-225 |
3.82e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 20 PQSVQ-VLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEELSALNETArglLRNRaLGFVYQFHH 98
Cdd:PRK10789 324 PQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSR-LAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 99 LLPEfTALENVCMplliGRtPIAEARQ--RAAEL------LERVGLGH--RLSHKPAELSGGERQRVAIARALVNRPQLV 168
Cdd:PRK10789 400 LFSD-TVANNIAL----GR-PDATQQEieHVARLasvhddILRLPQGYdtEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 169 LLDEPTGNLDQHTAQGIqelMLELSRSLQTSFLVVT-HDLQLAGHMDRILRLEEGRLI 225
Cdd:PRK10789 474 ILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISaHRLSALTEASEILVMQHGHIA 528
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-224 |
7.20e-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: 51.78 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 7 LSCRNLSKSYDEGPQSVqvLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLdTPSAGSVWLAGEELSALN----ETAR 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPlqkwRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 83 GLLRNRALGFVYQFHHLLPEFTALENvcmplligrtpiaearQRAAELLERVGLGHRLSHKPAE-----------LSGGE 151
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSD----------------EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598183 152 RQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQelmlelsRSLQTSF-----LVVTHDLQLAGHMDRILRLEEGRL 224
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIR-------KTLKQAFadctvILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
23-182 |
1.10e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.77 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 23 VQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPS--AGSVWLAGeeLSALNETARgllrnRALGFVYQFHHLL 100
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG--FPKKQETFA-----RISGYCEQNDIHS 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 101 PEFTALENVCMPLLIgRTPIAEARQ-------RAAELLERVGLGHRLSHKPA--ELSGGERQRVAIARALVNRPQLVLLD 171
Cdd:PLN03140 966 PQVTVRESLIYSAFL-RLPKEVSKEekmmfvdEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170
....*....|.
gi 15598183 172 EPTGNLDQHTA 182
Cdd:PLN03140 1045 EPTSGLDARAA 1055
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
10-219 |
1.26e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 10 RNLSKSYDEgPQSVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLA-GEELSALN----ETARGL 84
Cdd:PTZ00265 386 KNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINlkwwRSKIGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 85 LRNRALGFV--------YQFHHLlPEFTALE-----------------NVCMPLLIGRTPIAEARQRAAELLE------- 132
Cdd:PTZ00265 465 VSQDPLLFSnsiknnikYSLYSL-KDLEALSnyynedgndsqenknkrNSCRAKCAGDLNDMSNTTDSNELIEmrknyqt 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 133 -----------RVGLGHRLSHKP-----------AELSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELML 190
Cdd:PTZ00265 544 ikdsevvdvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
250 260
....*....|....*....|....*....
gi 15598183 191 ELSRSLQTSFLVVTHDLQLAGHMDRILRL 219
Cdd:PTZ00265 624 NLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
129-219 |
3.52e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 129 ELLERVGLGH-RLSHKPAELSGGERQRVAIARALVNR---PQLVLLDEPTGNLdqHTAQgIQELMLELSR--SLQTSFLV 202
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL--HFHD-VKKLLEVLQRlvDKGNTVVV 227
|
90
....*....|....*..
gi 15598183 203 VTHDLQLAGHMDRILRL 219
Cdd:cd03271 228 IEHNLDVIKCADWIIDL 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-207 |
4.89e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSVWLAGEelSALNETARGLlrNRALgfvyqfhhllpefTA 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALIAISSGL--NGQL-------------TG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 106 LENVCMP-LLIGRTPiAEARQRAAELLERVGLGhRLSHKPAE-LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQ 183
Cdd:PRK13545 103 IENIELKgLMMGLTK-EKIKEIIPEIIEFADIG-KFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|....
gi 15598183 184 GIQELMLELSRSLQTSFLvVTHDL 207
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFF-ISHSL 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
129-205 |
2.20e-06 |
|
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: 47.82 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 129 ELLERVGLGHRLSHKPA---------ELSGGERQRVAIARALVNRPQLVLLDEPTGNLdqhtAQGIQELMLELSRSLQTS 199
Cdd:TIGR00954 556 QILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGIT 631
|
....*.
gi 15598183 200 FLVVTH 205
Cdd:TIGR00954 632 LFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-217 |
2.75e-06 |
|
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: 46.16 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 26 LSGVELNLLPGERVAIVGSSGSGKSTLLNmlggldtpsagsvwlageelsalnETARGLLRNRALGFvyqfhhlLPEFta 105
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------------EGLYASGKARLISF-------LPKF-- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 106 lenvcmplliGRTPIAEARQraAELLERVGLGH-RLSHKPAELSGGERQRVAIARALVNRPQ--LVLLDEPTGNLDQHTA 182
Cdd:cd03238 58 ----------SRNKLIFIDQ--LQFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*
gi 15598183 183 QGIQELMLELsRSLQTSFLVVTHDLQLAGHMDRIL 217
Cdd:cd03238 126 NQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWII 159
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-219 |
3.11e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 126 RAAELLERVGLGH-RLSHKPAELSGGERQRVAIARALVNR---PQLVLLDEPTGNLdqHTAQgIQELMLELSR--SLQTS 199
Cdd:TIGR00630 808 RKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGL--HFDD-IKKLLEVLQRlvDKGNT 884
|
90 100
....*....|....*....|
gi 15598183 200 FLVVTHDLQLAGHMDRILRL 219
Cdd:TIGR00630 885 VVVIEHNLDVIKTADYIIDL 904
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-216 |
3.60e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 114 LIGRTPIAEARQRAAELLErVGLGH-RLSHKPAELSGGERQRVAIARALVNRPQLVL--LDEPTGNLDQHTAQGIQELML 190
Cdd:TIGR00630 456 KIAEEVLKEIRERLGFLID-VGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLK 534
|
90 100
....*....|....*....|....*.
gi 15598183 191 ELsRSLQTSFLVVTHDLQLAGHMDRI 216
Cdd:TIGR00630 535 RL-RDLGNTLIVVEHDEDTIRAADYV 559
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-199 |
9.81e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 22 SVQVLSGVELNLLPGERVAIVGSSGSGKSTLLNMLG----GLDTPSAGSVWLAGEELSALNETARGLLRNRALGFVYqFH 97
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVH-FP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 98 HLLP----EFTALenvCM-----PLLIGRTpiAEARQRAAELLERVGLGHRLSHKPAE-----LSGGERQRVAIARALVN 163
Cdd:TIGR00956 152 HLTVgetlDFAAR---CKtpqnrPDGVSRE--EYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLG 226
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598183 164 RPQLVLLDEPTGNLDQHTAqgiqelmLELSRSLQTS 199
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATA-------LEFIRALKTS 255
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
129-174 |
1.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15598183 129 ELLERVGLGH-RLSHkPA-ELSGGERQRVAIARALVNRPQ---LVLLDEPT 174
Cdd:COG0178 808 QTLQDVGLGYiKLGQ-PAtTLSGGEAQRVKLASELSKRSTgktLYILDEPT 857
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
18-67 |
2.29e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.54 E-value: 2.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15598183 18 EGPQSVQVLSGVelnLLPGERVAIVGSSGSGKSTLLNMLGGLDTPSAGSV 67
Cdd:PRK01889 180 LDGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-219 |
2.62e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 131 LERVGLGHRLShkpaELSGGERQRVAIARALVN---RPQLVLLDEPTGNLDQHTAQGIQELMLELSRSLQTsFLVVTHDL 207
Cdd:PRK00635 798 LDYLPLGRPLS----SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT-VVIIEHNM 872
|
90
....*....|..
gi 15598183 208 QLAGHMDRILRL 219
Cdd:PRK00635 873 HVVKVADYVLEL 884
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
147-224 |
1.20e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.20e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 147 LSGGERQRVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLELSRSlQTSFLVVTHDL-QLAGHMDRILRLEEGRL 224
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
129-174 |
2.02e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15598183 129 ELLERVGLGH-RLShKPA-ELSGGERQRVAIARALVNRPQ---LVLLDEPT 174
Cdd:PRK00349 812 QTLVDVGLGYiKLG-QPAtTLSGGEAQRVKLAKELSKRSTgktLYILDEPT 861
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
154-220 |
2.53e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598183 154 RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMLEL--SRSLQTSF--LVVTHDLQLAGHMDRILRLE 220
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIikSRSQQRNFqlLVITHDEDFVELLGRSEYVE 1283
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
115-206 |
3.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 115 IGRTPIAEARQRAaELLERVGLGH----RLShkpAELSGGERQRV----AIARALVNrpqlVL--LDEPTGNLDQHTAQG 184
Cdd:COG0178 454 IAERILKEIRSRL-GFLVDVGLDYltldRSA---GTLSGGEAQRIrlatQIGSGLVG----VLyvLDEPSIGLHQRDNDR 525
|
90 100
....*....|....*....|..
gi 15598183 185 IQELMLELsRSLQTSFLVVTHD 206
Cdd:COG0178 526 LIETLKRL-RDLGNTVIVVEHD 546
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-56 |
3.05e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.46 E-value: 3.05e-04
10 20
....*....|....*....|....*
gi 15598183 32 NLLPGERVAIVGSSGSGKSTLLNML 56
Cdd:cd01854 81 ELLKGKTSVLVGQSGVGKSTLLNAL 105
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
40-220 |
3.32e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 40 AIVGSSGSGKSTLLNmlggldtpsAGSVWLAGEELSALNETARGLLRNRA-----LGFVYQFHHLLPEftalenvcmpll 114
Cdd:cd03279 32 LICGPTGAGKSTILD---------AITYALYGKTPRYGRQENLRSVFAPGedtaeVSFTFQLGGKKYR------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 115 IGRTPIAEARQ----------RAAELLERvglghrlshkPAE-LSGGERQRVAIARALV----------NRPQLVLLDEP 173
Cdd:cd03279 91 VERSRGLDYDQftrivllpqgEFDRFLAR----------PVStLSGGETFLASLSLALAlsevlqnrggARLEALFIDEG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598183 174 TGNLDQHTAQGIQELmLELSRSLQTSFLVVTHDLQLAGHMDRILRLE 220
Cdd:cd03279 161 FGTLDPEALEAVATA-LELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-222 |
5.49e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 125 QRAAELLERVGLGH-RLSHKPAELSGGERQRVAIARALVNRPQ---LVLLDEPTGNLDQHTAQGIQELMLELSrSLQTSF 200
Cdd:PRK00635 1677 QKPLQALIDNGLGYlPLGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGHSV 1755
|
90 100
....*....|....*....|..
gi 15598183 201 LVVTHDLQLAGHMDRILRLEEG 222
Cdd:PRK00635 1756 IYIDHDPALLKQADYLIEMGPG 1777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-220 |
1.59e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 147 LSGGERQ------RVAIARALVNRPQLVLLDEPTGNLDQHTAQGIQELMlelSRSLQ--TSFLVVTHDLQLAGHMDRILR 218
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIM---ERYLRkiPQVIIVSHDEELKDAADYVIR 865
|
..
gi 15598183 219 LE 220
Cdd:PRK03918 866 VS 867
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-217 |
2.55e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 2.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598183 145 AELSGGERQRVAIARALVNRPQLV--LLDEPTGNL---DQHT-AQGIQELmlelsRSLQTSFLVVTHDLQLAGHMDRIL 217
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLhpqDTHKlINVIKKL-----RDQGNTVLLVEHDEQMISLADRII 548
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
38-56 |
3.10e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.44 E-value: 3.10e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-220 |
3.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 144 PAELSGGERQ------RVAIARALVN-------RPQLVLlDEPTGNLDQ-HTAQgiqelMLELSRSLQT----SFLVVTH 205
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAEgiegdapLPPLIL-DEPTVFLDSgHVSQ-----LVDLVESMRRlgveQIVVVSH 852
|
90
....*....|....*
gi 15598183 206 DLQLAGHMDRILRLE 220
Cdd:PRK02224 853 DDELVGAADDLVRVE 867
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
38-57 |
4.12e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 36.62 E-value: 4.12e-03
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
147-179 |
4.73e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.57 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|....*....
gi 15598183 147 LSGGERQ------RVAIARALVNRPQLVLLDEPTGNLDQ 179
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDE 840
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
38-94 |
7.87e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 34.23 E-value: 7.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598183 38 RVAIVGSSGSGKSTLLNML---GGLDTPSAGSVWLAGEELSALNETARGLLRNRALGFVY 94
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLaeqLGGRSVVVLDEIVILEGLYASYKSRDARIRDLADLKIY 60
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
31-56 |
8.69e-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: 35.98 E-value: 8.69e-03
10 20
....*....|....*....|....*.
gi 15598183 31 LNLLPGERVAIVGSSGSGKSTLLNML 56
Cdd:pfam03193 101 KELLKGKTTVLAGQSGVGKSTLLNAL 126
|
|
| |
