|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-223 |
5.89e-112 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 320.07 E-value: 5.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:COG1136 4 LLELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-219 |
1.94e-105 |
|
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: 303.26 E-value: 1.94e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:cd03255 1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
2-223 |
1.34e-95 |
|
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: 278.47 E-value: 1.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:TIGR02211 1 LLKCENLGKRYQEGK-LDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:TIGR02211 80 LRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-223 |
6.20e-93 |
|
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: 272.00 E-value: 6.20e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:COG4181 8 IIELRGLTKTVGTGAG-ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDwnVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:COG4181 87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-223 |
2.57e-84 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 250.12 E-value: 2.57e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHElTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQT-DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
4.87e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 218.38 E-value: 4.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFigGDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG2884 1 MI-RFENVSKRY--PGGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG2884 76 YLRRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQRAD-RIMELRDGCLH 222
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLV 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-221 |
6.42e-69 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 210.79 E-value: 6.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:PRK10584 6 IVEVHHLKKS-VGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.69e-66 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 205.71 E-value: 1.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGela 80
Cdd:COG1116 6 PALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrnktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG1116 82 ------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRI 213
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRV 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-219 |
1.93e-63 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 208.04 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:PRK10535 4 LLELKDIRRSYPSGEE-QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-203 |
9.32e-62 |
|
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: 192.30 E-value: 9.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsGELAEV 82
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03293 72 GPD-RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.55e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 192.58 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG3638 1 PMLELRNLSKRYPGGT----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKtVGFVFQFHHLLREFTVLENVMMPCL--------ISGLdWNVAD-ERARELLVAVGLEGRLSHRPAKLSGGEQQR 151
Cdd:COG3638 77 RLRRR-IGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGL-FPPEDrERALEALERVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-219 |
3.36e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 186.35 E-value: 3.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKMDSGELAE 81
Cdd:COG1126 1 MIEIENLHKSF--GD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDG-EDLTDSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQ----FHHLlrefTVLENVMM-PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:COG1126 75 LRRK-VGMVFQqfnlFPHL----TVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREvADRVVFMDGG 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-202 |
1.23e-57 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 185.67 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG1135 1 MI-ELENLSKTFPTKGG-PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG1135 79 AAR-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTH 202
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-219 |
3.95e-57 |
|
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: 180.52 E-value: 3.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:TIGR02673 1 MIEFHNVSKAYPGG----VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:TIGR02673 77 LRRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRvAHRVIILDDG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-219 |
4.62e-57 |
|
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: 181.23 E-value: 4.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:cd03256 1 IEVENLSKTYPNGK----KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCL--------ISGLdWNVAD-ERARELLVAVGLEGRLSHRPAKLSGGEQQRVA 153
Cdd:cd03256 77 RRQ-IGMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGL-FPKEEkQRALAALERVGLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 154 LARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-219 |
6.90e-57 |
|
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: 180.56 E-value: 6.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:COG1127 5 MIEVRNLTKSF--GD---RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQFHHLLREFTVLENVMMPcLI--SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALS 159
Cdd:COG1127 80 LRRR-IGMLFQGGALFDSLTVFENVAFP-LRehTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADG 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-219 |
9.27e-57 |
|
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: 180.08 E-value: 9.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:cd03258 1 MIELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03258 80 ARRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKG 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-224 |
3.89e-55 |
|
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: 175.02 E-value: 3.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgelaEV 82
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV------PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQ----FHHLlrefTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARAL 158
Cdd:cd03259 70 ERRNIGMVFQdyalFPHL----TVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQV 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-223 |
6.50e-55 |
|
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: 175.21 E-value: 6.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEV 82
Cdd:COG1122 1 IELENLSFSYPGGT----PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnKTVGFVFQF--HHLLREfTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG1122 74 R-RKVGLVFQNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAElADRVIVLDDGRIVA 214
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-216 |
1.82e-54 |
|
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: 173.19 E-value: 1.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNK 85
Cdd:TIGR03608 2 KNISKKF-----GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 TVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLIL 165
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-219 |
2.09e-54 |
|
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: 174.23 E-value: 2.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:cd03261 1 IELRGLTKSF--GG---RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLI-SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03261 76 RRR-MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
2.71e-54 |
|
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: 174.22 E-value: 2.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAev 82
Cdd:COG1124 2 LEVRNLSVSY-GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQ-----FHHLlreFTVLENVMMPCLISGLDwnVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALAR 156
Cdd:COG1124 79 --RRVQMVFQdpyasLHPR---HTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
22-221 |
4.74e-54 |
|
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: 172.51 E-value: 4.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRnKTVGFVFQFHHLLREFT 101
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPC-LISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSH 180
Cdd:TIGR02982 99 ARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 181 ELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
5.12e-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: 180.48 E-value: 5.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQ--FHHLLREFTVLENVMMPCLISG-LDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARA 157
Cdd:COG1123 340 LR-RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDG 481
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-219 |
5.30e-54 |
|
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: 172.33 E-value: 5.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmDSGELAEV 82
Cdd:cd03262 1 IEIKNLHKSF-----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMM-PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03262 75 RQK-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-219 |
2.52e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.90 E-value: 2.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmdsGELAE 81
Cdd:COG3842 5 ALELENVSKRY--GD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNktVGFVFQ----FHHLlrefTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:COG3842 76 KRN--VGMVFQdyalFPHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDG 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-219 |
9.04e-52 |
|
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: 168.59 E-value: 9.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKTVGFVFQFHHLLREFTV 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 LENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHEL 182
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 297171361 183 HDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDG 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-221 |
1.25e-51 |
|
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: 166.91 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsGELAE 81
Cdd:cd03257 1 LLEVKNLSVSF-PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLS-RRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQ--FHHLLREFTVLENVMMPCLISGLDWNVADERAR--ELLVAVGLEGRLSHR-PAKLSGGEQQRVALAR 156
Cdd:cd03257 79 IRRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRyPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-219 |
2.09e-51 |
|
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: 165.66 E-value: 2.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:cd03292 1 IEFINVTKTY----PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03292 77 RRK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTtRHRVIALERG 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-221 |
8.33e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.83 E-value: 8.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEV 82
Cdd:COG4619 1 LELEGLSFRVGGK-----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREfTVLENVMMPCLISGLDWNvaDERARELLVAVGLEGRLSHRPAK-LSGGEQQRVALARALSNY 161
Cdd:COG4619 73 RRQ-VAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
8.74e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.02 E-value: 8.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKMDSGEl 79
Cdd:COG1118 1 MSIEVRNISKRF-----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRE- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 aevRNktVGFVFQ----FHHLlrefTVLENVM--MPCLisGLDWNVADERARELLVAVGLEGrLSHR-PAKLSGGEQQRV 152
Cdd:COG1118 75 ---RR--VGFVFQhyalFPHM----TVAENIAfgLRVR--PPSKAEIRARVEELLELVQLEG-LADRyPSQLSGGQRQRV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-219 |
1.69e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.08 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgELAEV 82
Cdd:COG1131 1 IEVRGLTKRY--GD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:COG1131 72 R-RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAIIDKG 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-219 |
5.90e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 162.85 E-value: 5.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTvGFVFQFHHLLREFTVLENVMMPCLISGLDWNV-------AD-ERARELLVAVGLEGRLSHRPAKLSGGEQQRVA 153
Cdd:TIGR02315 77 LRRRI-GMIFQHYNLIERLTVLENVLHGRLGYKPTWRSllgrfseEDkERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 154 LARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAG 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-209 |
2.47e-49 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 161.41 E-value: 2.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdGHeLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKMDSGELAE 81
Cdd:PRK09493 1 MIEFKNVSKHF----GP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-LKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQFHHLLREFTVLENVMM-PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK09493 75 IR-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR 209
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEK 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-219 |
4.05e-49 |
|
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: 159.55 E-value: 4.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevr 83
Cdd:cd03225 1 ELKNLSFSY---PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 nKTVGFVFQF--HHLLREfTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03225 75 -RKVGLVFQNpdDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-222 |
1.85e-48 |
|
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: 160.31 E-value: 1.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRnKTVGFVFQF-HHLL 97
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFpEHQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 98 REFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:TIGR04521 96 FEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 297171361 177 YMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDGCLH 222
Cdd:TIGR04521 176 KGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-223 |
7.47e-48 |
|
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: 157.90 E-value: 7.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAe 81
Cdd:COG1120 1 MLEAENLSVGY-----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrnKTVGFVFQFHHLLREFTVLENVMM---PCLISGLDWNVADERA-RELLVAVGLEGrLSHRP-AKLSGGEQQRVALAR 156
Cdd:COG1120 75 ---RRIAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAvEEALERTGLEH-LADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVA 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-219 |
1.58e-47 |
|
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: 154.65 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQFHHLLREFTVLENVMMPclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYP 162
Cdd:cd03229 76 RR--IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
4.14e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 159.68 E-value: 4.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQT---SGEVMIDGCQTSKMDsge 78
Cdd:COG1123 4 LLEVRDLSVRYPGGD---VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 79 lAEVRNKTVGFVFQ-FHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:COG1123 78 -EALRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDG 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-202 |
4.24e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 155.73 E-value: 4.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:PRK11153 1 MI-ELKNISKVF-PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK11153 79 KARRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTH 202
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
5.87e-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: 152.49 E-value: 5.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgela 80
Cdd:cd03296 1 MSIEVRNVSKRF--GD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 eVRNKTVGFVFQFHHLLREFTVLENVMMPCLI----SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:cd03296 71 -VQERNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-221 |
8.74e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 152.53 E-value: 8.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaev 82
Cdd:COG3839 4 LELENVSKSY-GGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQ----FHHLlrefTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARAL 158
Cdd:COG3839 75 RN--IAMVFQsyalYPHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTlADRIAVMNDGRI 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-215 |
3.42e-44 |
|
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: 150.20 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL---DRQTSGEVMIDGCQTSKMDSGE 78
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 79 LAEVRNKTVGFVFQ--FHHLLREFTVLENVMMPCLI-SGLDWNVADERARELLVAVGL---EGRLSHRPAKLSGGEQQRV 152
Cdd:COG0444 80 LRKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN----RQLAQR-----ADRIME 215
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgvvAEIADRvavmyAGRIVE 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-221 |
1.45e-43 |
|
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: 146.17 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL-----DRQTSGEVMIDGCQTSKMDSG 77
Cdd:cd03260 1 IELRDLNVYY--GDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELaEVRnKTVGFVFQFHHLLReFTVLENVMMPCLISGLDWN-VADERARELLVAVGLEGRLSHR--PAKLSGGEQQRVAL 154
Cdd:cd03260 76 VL-ELR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 155 ARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-213 |
8.08e-43 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 147.49 E-value: 8.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdGHeLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaev 82
Cdd:TIGR03265 5 LSIDNIRKRF----GA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGrlSHR--PAKLSGGEQQRVALARALSN 160
Cdd:TIGR03265 76 RD--YGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPG--SERkyPGQLSGGQQQRVALARALAT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRI 213
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRI 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
1.01e-42 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 144.82 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMidgcqtskMDSGELAEV 82
Cdd:PRK11247 13 LLLNAVSKRY-----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTvGFVFQFHHLLREFTVLENVMMpclisGL--DWNvadERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK11247 80 REDT-RLMFQDARLLPWKKVIDNVGL-----GLkgQWR---DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-210 |
1.47e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 144.12 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSG-----EVMIDGCQTSKMDSG 77
Cdd:PRK11264 4 IEVKNLVKKF-----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKtVGFVFQFHHLLREFTVLENVMM-PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:PRK11264 79 LIRQLRQH-VGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRgLAMILVTHN----RQLAQRA 210
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEmsfaRDVADRA 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
6.72e-42 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 142.49 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG0411 3 PLLEVRGLTKRF-GG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 E---VRnktvgfVFQFHHLLREFTVLENVMMPCL----------ISGLDWNVADE-----RARELLVAVGLEGRLSHRPA 142
Cdd:COG0411 78 RlgiAR------TFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRARREEreareRAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 143 KLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIM 214
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIV 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-219 |
1.41e-41 |
|
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: 141.28 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELaev 82
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENV-MMPCLisgLDWNVA--DERARELLVAVGLE-GRLSHR-PAKLSGGEQQRVALARA 157
Cdd:cd03295 74 RRK-IGYVIQQIGLFPHMTVEENIaLVPKL---LKWPKEkiRERADELLALVGLDpAEFADRyPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNG 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-222 |
1.45e-41 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 140.78 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 10 KRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRnKTVGF 89
Cdd:PRK10908 9 KAYLGGR----QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 90 VFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADE 169
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 170 PSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQL-AQRADRIMELRDGCLH 222
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLiSRRSYRMLTLSDGHLH 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-224 |
1.79e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 144.07 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiggdGHElTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgela 80
Cdd:PRK10851 1 MSIEIANIKKSF----GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evRNKTVGFVFQFHHLLREFTVLENVMMpclisGL---------DWNVADERARELLVAVGLEgRLSHR-PAKLSGGEQQ 150
Cdd:PRK10851 72 --RDRKVGFVFQHYALFRHMTVFDNIAF-----GLtvlprrerpNAAAIKAKVTQLLEMVQLA-HLADRyPAQLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQA 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-216 |
2.20e-41 |
|
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: 139.98 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFiggDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgelaevr 83
Cdd:cd03235 1 EVEDLTVSY---GGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 NKTVGFVFQFHHLLREF--TVLENVMMPCL--ISGLDWNVADERAR--ELLVAVGLEGrLSHRP-AKLSGGEQQRVALAR 156
Cdd:cd03235 67 RKRIGYVPQRRSIDRDFpiSVRDVVLMGLYghKGLFRRLSKADKAKvdEALERVGLSE-LADRQiGELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMEL 216
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-219 |
2.24e-41 |
|
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: 138.67 E-value: 2.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAev 82
Cdd:cd03228 1 IEFKNVSFSY---PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQFHHLLREfTVLENVmmpclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYP 162
Cdd:cd03228 76 --KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-223 |
4.76e-41 |
|
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: 146.83 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEv 82
Cdd:COG4987 334 LELEDVSFRY---PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnkTVGFVFQFHHLLREfTVLENVMM--PclisgldwNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQ 149
Cdd:COG4987 410 ---RIAVVPQRPHLFDT-TLRENLRLarP--------DATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 150 QRVALARA-LSNYPLILLaDEPSGNLDSYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:COG4987 478 RRLALARAlLRDAPILLL-DEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
6.45e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiggDGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgELA 80
Cdd:COG1121 5 PAIELENLTVSY---GGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---------KPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKTVGFVFQFHHLLREF--TVLENVMMPCL--------ISGLDWnvadERARELLVAVGLEGrLSHRP-AKLSGGEQ 149
Cdd:COG1121 71 RRARRRIGYVPQRAEVDWDFpiTVRDVVLMGRYgrrglfrrPSRADR----EAVDEALERVGLED-LADRPiGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 150 QRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDGCLH 222
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDlGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-219 |
1.48e-40 |
|
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: 138.52 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaev 82
Cdd:cd03300 1 IELENVSKFY-GGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03300 72 RP--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKG 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-223 |
2.03e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.96 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 29 SVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaevrnKTVGFVFQ----FHHLlrefTVLE 104
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQennlFPHL----TVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 105 NV---MMPclisGLDWNVAD-ERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARAL-SNYPLILLaDEPSGNLDSYMS 179
Cdd:COG3840 91 NIglgLRP----GLKLTAEQrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRPILLL-DEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 180 HELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-202 |
2.52e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 138.84 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmdsGELA 80
Cdd:COG4525 2 SMLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----GPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EvRnktvGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG4525 77 D-R----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTH 202
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-219 |
4.81e-40 |
|
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: 137.18 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFI--GGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEV-------MIDGCQTS 72
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 73 KMdsgELAEVRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSH-RPAKLSGGEQQR 151
Cdd:COG4778 84 PR---EILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 152 VALARAL-SNYPLILLaDEPSGNLDSYMSHELHDLLfQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG4778 161 VNIARGFiADPPLLLL-DEPTASLDAANRAVVVELI-EEAKARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-223 |
9.91e-40 |
|
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: 136.41 E-value: 9.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEv 82
Cdd:cd03219 1 LEVRGLTKRF-GG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQFHHLLREFTVLENVMMPCLISG----LDWNV------ADERARELLVAVGLEGRLSHRPAKLSGGEQQRV 152
Cdd:cd03219 75 --LGIGRTFQIPRLFPELTVLENVMVAAQARTgsglLLARArreereARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIA 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-218 |
1.07e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 135.30 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskMDSGELA 80
Cdd:COG4133 1 MMLEAENLSCRR-----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-----EPIRDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDwnVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA-LS 159
Cdd:COG4133 71 EDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLlLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 160 NYPLILLaDEPSGNLDSYMSHELHDLLFQLKKDRGlaMILVTHNRQLAQRADRIMELRD 218
Cdd:COG4133 149 PAPLWLL-DEPFTALDAAGVALLAELIAAHLARGG--AVLLTTHQPLELAAARVLDLGD 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
1.27e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 136.30 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKrFIGGdgHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ---TSKMDSG 77
Cdd:COG4161 1 MSIQLKNINC-FYGS--HQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKtVGFVFQFHHLLREFTVLENVM-MPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:COG4161 76 AIRLLRQK-VGMVFQQYNLWPHLTVMENLIeAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKvASQVVYMEKG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
1.42e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.83 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRfIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:PRK13548 1 AMLEARNLSVR-LGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRnktvGFVFQFHHLLREFTVLENVMMPcLISGLDWNVADERA-RELLVAVGLEGrLSHRP-AKLSGGEQQRVALARAL 158
Cdd:PRK13548 76 RRR----AVLPQHSSLSFPFTVEEVVAMG-RAPHGLSRAEDDALvAAALAQVDLAH-LAGRDyPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 159 ------SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:PRK13548 150 aqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVA 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-221 |
2.21e-39 |
|
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: 133.68 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDGhelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgELAEV 82
Cdd:cd03230 1 IEVRNLSKRY--GKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVmmpclisgldwnvaderarellvavglegrlshrpaKLSGGEQQRVALARALSNYP 162
Cdd:cd03230 72 KRR-IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-170 |
4.48e-39 |
|
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: 132.00 E-value: 4.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelAEVRNKTVGFVFQFHHLLREFTV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE----RKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 103 LENVMMPCLISGLDWNVADERARELLVAVGLEG----RLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-219 |
5.80e-39 |
|
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: 133.92 E-value: 5.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaev 82
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03301 72 RD--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDG 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-219 |
6.38e-39 |
|
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: 136.85 E-value: 6.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 38 VVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCqtskmdsgELAEV--RNKTVGFVFQFHHLLREFTVLENVMMPCLISGL 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE--------DVTNVppHLRHINMVFQSYALFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 116 DWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD----SYMSHELHDLLFQLkk 191
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL-- 150
|
170 180
....*....|....*....|....*....
gi 297171361 192 drGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:TIGR01187 151 --GITFVFVTHDQEEAmTMSDRIAIMRKG 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
1.55e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 134.76 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKMDSGELAEVRNKtVGFVFQF-HHLLREF 100
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERViTAGKKNKKLKPLRKK-VGIVFQFpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 TVLENVMMPCLISGLDWNVADERARELLVAVGL-EGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMS 179
Cdd:PRK13634 102 TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 180 HELHDLLFQLKKDRGLAMILVTHNRQ-LAQRADRIMELRDG 219
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKG 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-224 |
2.39e-38 |
|
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: 131.02 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevr 83
Cdd:cd03214 1 EVENLSVGY-----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 nKTVGFVFQfhhllreftVLEnvmmpclisgldwnvaderarellvAVGLEGrLSHRP-AKLSGGEQQRVALARALSNYP 162
Cdd:cd03214 73 -RKIAYVPQ---------ALE-------------------------LLGLAH-LADRPfNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-225 |
2.48e-38 |
|
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: 133.06 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgela 80
Cdd:COG4555 1 MI-EVENLSKKY-----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:COG4555 71 EARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLAQR-ADRIMELRDGCLHAIN 225
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQG 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-219 |
3.03e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 134.45 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFigGDGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG1125 1 MI-EFENVTKRY--PDGT--VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evRNktVGFVFQFHHLLREFTVLENVMM-PCLisgLDWNVA--DERARELLVAVGLE-GRLSHR-PAKLSGGEQQRVALA 155
Cdd:COG1125 76 --RR--IGYVIQQIGLFPHMTVAENIATvPRL---LGWDKEriRARVDELLELVGLDpEEYRDRyPHELSGGQQQRVGVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 156 RALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG1125 149 RALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKlGDRIAVMREG 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-219 |
3.56e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 133.00 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDgHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKM-------- 74
Cdd:COG4598 9 LEVRDLHKSF--GD-LE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG-EEIRLkpdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 75 ---DSGELAEVRNKtVGFVFQFHHLLREFTVLENVMM-PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQ 150
Cdd:COG4598 83 vpaDRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELhdllfqLKKDRGLA-----MILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEV------LKVMRDLAeegrtMLVVTHEMGFARDvSSHVVFLHQG 230
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-221 |
3.98e-38 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 132.80 E-value: 3.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDR-----QTSGEVMIDG--CQTSKM 74
Cdd:TIGR00972 1 AIEIENLNLFY--GEKE---ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGqdIYDKKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 75 DsgeLAEVRnKTVGFVFQ----FhhllrEFTVLENVMMPCLISGL-DWNVADERARELLVAVGL----EGRLSHRPAKLS 145
Cdd:TIGR00972 76 D---VVELR-RRVGMVFQkpnpF-----PMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALwdevKDRLHDSALGLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:TIGR00972 147 GGQQQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARiSDRTAFFYDGEL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-219 |
1.51e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 134.30 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggDGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelAE 81
Cdd:PRK09452 14 LVELRGISKSF---DGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK09452 85 NRH--VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDG 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-224 |
1.72e-37 |
|
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: 130.11 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 32 SGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqTSKMDS--GELAEVRNKTVGFVFQFHHLLREFTVLENVMmp 109
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSrkKINLPPQQRKIGLVFQQYALFPHLNVRENLA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 110 CLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQL 189
Cdd:cd03297 98 FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 297171361 190 KKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-219 |
3.06e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 3.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ---TSKMDSGELAEVRNKtVGFVFQFHHLLR 98
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRELRRN-VGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVM-MPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSY 177
Cdd:PRK11124 96 HLTVQQNLIeAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 178 MSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK11124 176 ITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENG 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-219 |
3.56e-37 |
|
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: 129.15 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 28 ISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaevrnKTVGFVFQFHHLLREFTVLENVM 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 108 MPcLISGLDWNVADERARELLVA-VGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLL 186
Cdd:cd03298 93 LG-LSPGLKLTAEDRQAIEVALArVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....
gi 297171361 187 FQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-221 |
4.71e-37 |
|
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: 136.89 E-value: 4.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEV 82
Cdd:COG2274 474 IELENVSFRY---PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREfTVLENvmmpclISGLDWNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQQR 151
Cdd:COG2274 548 RRQ-IGVVLQDVFLFSG-TIREN------ITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-221 |
4.83e-37 |
|
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: 135.58 E-value: 4.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKS----TLLHLLGGLDRQTSGEVMIDGCQTSKMDSG 77
Cdd:COG4172 6 LLSVEDLSVAF-GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKTVGFVFQfhhllrE--------FTVLENVMMP-CLISGLDWNVADERARELLVAVGL---EGRLSHRPAKLS 145
Cdd:COG4172 85 ELRRIRGNRIAMIFQ------EpmtslnplHTIGKQIAEVlRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-219 |
2.02e-36 |
|
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: 125.43 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFIGGdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevr 83
Cdd:cd00267 1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 nKTVGFVFQfhhllreftvlenvmmpclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYPL 163
Cdd:cd00267 73 -RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 164 ILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRA-DRIMELRDG 219
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-224 |
2.72e-36 |
|
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: 127.24 E-value: 2.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtsKMDSGELAEV 82
Cdd:cd03263 1 LQIRNLTKTYKKGT---KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING----YSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLsHRPAK-LSGGEQQRVALARALSNY 161
Cdd:cd03263 74 RQS-LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRARtLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEAlCDRIAIMSDGKLRCI 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-221 |
3.10e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 128.27 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRF----IGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSG 77
Cdd:PRK10419 3 LLNVSGLSHHYahggLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRnKTVGFVFQ--FHHLLREFTVLENVMMPCL-ISGLDWNVADERARELLVAVGL-EGRLSHRPAKLSGGEQQRVA 153
Cdd:PRK10419 83 QRKAFR-RDIQMVFQdsISAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 154 LARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-223 |
7.09e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 7.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRfIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:COG4559 2 LEAENLSVR-LGGR----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnktvGFVFQFHHLLREFTVLENVMMPcLISGLDWNVADER-ARELLVAVGLEGrLSHRP-AKLSGGEQQRVALARAL-- 158
Cdd:COG4559 77 R----AVLPQHSSLAFPFTVEEVVALG-RAPHGSSAAQDRQiVREALALVGLAH-LAGRSyQTLSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 159 -----SNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQL-AQRADRIMELRDGCLHA 223
Cdd:COG4559 151 lwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLaAQYADRILLLHQGRLVA 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
2.96e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelA 80
Cdd:COG1129 3 PLLEMRGISKSF-GG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKTVGFVFQFHHLLREFTVLENVMMPCLISG---LDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHnR--QLAQRADRIMELRDGCL 221
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH-RldEVFEIADRVTVLRDGRL 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-219 |
3.40e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 125.62 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdghELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTskMDSGELAEV 82
Cdd:TIGR04520 1 IEVENVSFSYPES---EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVF-----QFHHLLREFTV---LENVMMPclisgldwnvADE---RARELLVAVGLEGRLSHRPAKLSGGEQQR 151
Cdd:TIGR04520 76 RKK-VGMVFqnpdnQFVGATVEDDVafgLENLGVP----------REEmrkRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKG 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-221 |
4.47e-35 |
|
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: 122.71 E-value: 4.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAev 82
Cdd:cd03246 1 LEVENVSFRY---PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQFHHLLrEFTVLENVmmpclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYP 162
Cdd:cd03246 76 --DHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.95e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLckRFIGGDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKMDSGELAE 81
Cdd:PRK13639 1 ILETRDL--KYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK13639 76 VR-KTVGIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVyADKVYVMSDG 213
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-218 |
6.76e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.36 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCkrfIGGDGHELtvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGG-LDR--QTSGEVMIDGCQTSKMDsgel 79
Cdd:COG4136 2 LSLENLT---ITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPafSASGEVLLNGRRLTALP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNktVGFVFQFHHLLREFTVLENVM--MPCLISGldwNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:COG4136 73 AEQRR--IGILFQDDLLFPHLSVGENLAfaLPPTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRD 218
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-221 |
9.27e-35 |
|
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: 129.15 E-value: 9.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLD--RQTSGEVMI-------------- 66
Cdd:TIGR03269 1 IEVKNLTKKFDG-----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 67 --DGCQTSK--------------MDSGELAEVRnKTVGFVFQ-FHHLLREFTVLENVMMPCLISGLDWNVADERARELLV 129
Cdd:TIGR03269 76 skVGEPCPVcggtlepeevdfwnLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 130 AVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ-LAQ 208
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEvIED 234
|
250
....*....|...
gi 297171361 209 RADRIMELRDGCL 221
Cdd:TIGR03269 235 LSDKAIWLENGEI 247
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-221 |
4.06e-34 |
|
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: 127.95 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCkrFIGGDGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAev 82
Cdd:COG4988 337 IELEDVS--FSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQFHHLLREfTVLENVMM--PclisgldwNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQ 149
Cdd:COG4988 411 --RQIAWVPQNPYLFAG-TIRENLRLgrP--------DASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQA 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 150 QRVALARA-LSNYPLILLaDEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:COG4988 480 QRLALARAlLRDAPLLLL-DEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRI 549
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-213 |
5.14e-34 |
|
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: 121.32 E-value: 5.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgELAEV 82
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLeGRLSHRPAK-LSGGEQQRVALARALSNY 161
Cdd:cd03265 72 R-RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGL-LEAADRLVKtYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRI 213
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRV 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-219 |
3.05e-33 |
|
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: 119.49 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnktvgfVFQFHHLLREFTV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 LENVMMPCLISGLDWNVADERA--RELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSH 180
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 297171361 181 ELHDLLFQLKKDRGLAMILVTHNRQLAQ-RADRIMELRDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALlLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-203 |
5.87e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 119.42 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtsKMDSGELAE 81
Cdd:PRK11248 1 MLQISHLYADYGGK-----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VrnktvGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK11248 72 R-----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
23-221 |
1.06e-32 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 120.95 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskMDSGELA-EVRNktVGFVFQFHHLLREFT 101
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDG-----KDITNLPpEKRG--IAYVYQNYMLFPHKT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHR-PAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSH 180
Cdd:NF040840 89 VFENIAFGLKLRKVPKEEIERKVKEIMELLGIS-HLLHRkPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 181 ELHDLLFQLKKDRGLAMILVTHNRQLA-QRADRIMELRDGCL 221
Cdd:NF040840 168 ELIREMKRWHREFGFTAIHVTHNFEEAlSLADRVGIMLNGRL 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-219 |
3.01e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 120.91 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKTVGFVFQFHHLLREFTV 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 LENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHEL 182
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190
....*....|....*....|....*....|....*...
gi 297171361 183 HDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNG 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-215 |
3.97e-32 |
|
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: 116.38 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCkrfiGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEv 82
Cdd:cd03224 1 LEVENLN----AGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnKTVGFVFQFHHLLREFTVLENVMMPClisgldWNVADERARELLVAV-----GLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:cd03224 75 --AGIGYVPEGRRIFPELTVEENLLLGA------YARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADR--IME 215
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEiADRayVLE 206
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-219 |
4.50e-32 |
|
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: 117.60 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKR-----FIGGDGHeLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDS 76
Cdd:TIGR02769 2 LLEVRDVTHTyrtggLFGAKQR-APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GELAEVRnKTVGFVFQ--FHHLLREFTVLENVMMPCL-ISGLDWNVADERARELLVAVGLEGR-LSHRPAKLSGGEQQRV 152
Cdd:TIGR02769 81 KQRRAFR-RDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKG 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-221 |
5.91e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 117.62 E-value: 5.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKMDSGEL 79
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNKtVGFVFQFHHL-LREFTVLENVMMPCLISGLDWNVADERARELLVAVGL-EGRLSHRPAKLSGGEQQRVALARA 157
Cdd:PRK13641 81 KKLRKK-VSLVFQFPEAqLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNR-QLAQRADRIMELRDGCL 221
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMdDVAEYADDVLVLEHGKL 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-208 |
8.35e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 116.61 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 18 HEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDG----------CQTSKMDSGELAEVRNKtV 87
Cdd:PRK10619 18 HE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdGQLKVADKNQLRLLRTR-L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 88 GFVFQFHHLLREFTVLENVM-MPCLISGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARALSNYPLIL 165
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLAQ 208
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFAR 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-209 |
1.14e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.17 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL-----DRQTSGEVMIDGCQTSKMDSG 77
Cdd:PRK14247 4 IEIRDLKVSF--GQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELaevrNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVAD--ERARELLVAVGL----EGRLSHRPAKLSGGEQQR 151
Cdd:PRK14247 79 EL----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR 209
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-219 |
1.30e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 116.69 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKmdSGEL 79
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDiTDK--KVKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGL--EGRLSHRPAKLSGGEQQRVALAR 156
Cdd:PRK13637 79 SDIR-KKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ-LAQRADRIMELRDG 219
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKG 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-219 |
2.10e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 120.27 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRNKtVGFVFQFHHLLREfT 101
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDTFLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLisgldwNVADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:COG1132 430 IRENIRYGRP------DATDEEVEEAAKAAqahefiealpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:COG1132 504 TSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-226 |
3.86e-31 |
|
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: 114.36 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKrfIGGDGHeltvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelaEV 82
Cdd:cd03299 1 LKVENLSK--DWKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP----EK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03299 71 RD--ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDGCLHAINK 226
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGK 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-212 |
4.66e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 114.36 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL-DRQ----TSGEVMIDGCQ--TSKM 74
Cdd:COG1117 11 KIEVRNLNVYY--GDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIpgarVEGEILLDGEDiyDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 75 DsgeLAEVRnKTVGFVFQ----FHHllrefTVLENVMMPCLISGL-DWNVADERARELLVAVGL----EGRLSHRPAKLS 145
Cdd:COG1117 86 D---VVELR-RRVGMVFQkpnpFPK-----SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR-ADR 212
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARvSDY 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-207 |
8.35e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.97 E-value: 8.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDGhelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgelAEV 82
Cdd:PRK11432 7 VVLKNITKRF--GSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:PRK11432 76 QQRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLA 207
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA 200
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-227 |
2.02e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.18 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL---DRQTSGEVMIDG--CQTSKMDS 76
Cdd:PRK09984 4 IIRVEKLAKTF-----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGrtVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GELAEVRNKTvGFVFQFHHLLREFTVLENVMMPCLISGLDWN--------VADERARELLVAVGLEGRLSHRPAKLSGGE 148
Cdd:PRK09984 79 RDIRKSRANT-GYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 149 QQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELR------DGCL 221
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRqghvfyDGSS 237
|
....*.
gi 297171361 222 HAINKD 227
Cdd:PRK09984 238 QQFDNE 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-219 |
2.10e-30 |
|
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: 111.58 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFiggdGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelaevR 83
Cdd:cd03226 1 RIENISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 NKTVGFVFQ--FHHLLREfTVLENVmmpcLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03226 70 RKSIGYVMQdvDYQLFTD-SVREEL----LLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-221 |
3.26e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.53 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRnKTVGFVFQFHH 95
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVMMPCLIsgldwnVADER---ARELLVAV--------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLI 164
Cdd:cd03245 89 LFYG-TLRDNITLGAPL------ADDERilrAAELAGVTdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 165 LLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-224 |
8.21e-30 |
|
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: 113.27 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 25 EVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDG--CQTSKMDSGELAEVRNktVGFVFQ----FHHLlr 98
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevLQDSARGIFLPPHRRR--IGYVFQearlFPHL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 efTVLENvmmpcLISGLDWNVADERAREL--LVAV-GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:COG4148 93 --SVRGN-----LLYGRKRAPRAERRISFdeVVELlGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 176 SYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVAS 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
8.30e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 112.49 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMI---DGCQTSKMDSG 77
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 E------------------LAEVRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGL-EGRL 137
Cdd:PRK13651 81 EkvleklviqktrfkkikkIKEIR-RRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 138 SHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLA-QRADRIMEL 216
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKRTIFF 238
|
...
gi 297171361 217 RDG 219
Cdd:PRK13651 239 KDG 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-223 |
9.35e-30 |
|
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: 110.94 E-value: 9.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSG-EVMIDGCQTSKMDsgeLAEVRNKtVGFV-FQFHHLLR 98
Cdd:COG1119 17 TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWELRKR-IGLVsPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVmmpcLISGLD-----WNVADE----RARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADE 169
Cdd:COG1119 93 RDETVLDV----VLSGFFdsiglYREPTDeqreRARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 170 PSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRA-DRIMELRDGCLHA 223
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-219 |
9.66e-30 |
|
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: 110.33 E-value: 9.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgELAEV 82
Cdd:cd03218 1 LRAENLSKRY-----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL---PMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHRPA-KLSGGEQQRVALARALSNY 161
Cdd:cd03218 73 ARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHIT-HLRKSKAsSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAmILVT-HN-RQLAQRADRIMELRDG 219
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIG-VLITdHNvRETLSITDRAYIIYEG 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-224 |
1.16e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.26 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAE 81
Cdd:PRK13635 5 IIRVEHISFRY---PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQfhHLLREF---TV-------LENVMMPclisgLDWNVadERARELLVAVGLEGRLSHRPAKLSGGEQQR 151
Cdd:PRK13635 79 VRRQ-VGMVFQ--NPDNQFvgaTVqddvafgLENIGVP-----REEMV--ERVDQALRQVGMEDFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHAI 224
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-219 |
1.30e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.20 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAEvrnK 85
Cdd:PRK11000 7 RNVTKAY--GDVV---ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPAE---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 TVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLIL 165
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTlADKIVVLDAG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-213 |
1.37e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElae 81
Cdd:PRK11607 19 LLEIRNLTKSF---DGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK11607 91 ---RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 162 PLILLADEPSGNLDS----YMSHELHDLLFQLkkdrGLAMILVTHNRQLAQR-ADRI 213
Cdd:PRK11607 168 PKLLLLDEPMGALDKklrdRMQLEVVDILERV----GVTCVMVTHDQEEAMTmAGRI 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-219 |
1.86e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.39 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 5 AKNLCKRFiGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDgcqtskmdsgelaevRN 84
Cdd:COG0488 1 LENLSKSF-GGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 85 KTVGFVFQFHHLLREFTVLENVMMPC-----LISGLD----------------------------WNvADERARELLVAV 131
Cdd:COG0488 61 LRIGYLPQEPPLDDDLTVLDTVLDGDaelraLEAELEeleaklaepdedlerlaelqeefealggWE-AEARAEEILSGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 132 GLEGRLSHRPAK-LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLfqlkKDRGLAMILVTHNRQLAQR- 209
Cdd:COG0488 140 GFPEEDLDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRYFLDRv 215
|
250
....*....|
gi 297171361 210 ADRIMELRDG 219
Cdd:COG0488 216 ATRILELDRG 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-219 |
2.69e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.13 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAEV 82
Cdd:cd03216 1 LELRGITKRF--GGVK---ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQfhhllreftvlenvmmpclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYP 162
Cdd:cd03216 73 RRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRlDEVFEIADRVTVLRDG 158
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-219 |
2.70e-29 |
|
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: 114.01 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDG------HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRqTSGEVMIDGCQTSKMD 75
Cdd:COG4172 275 LLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 76 SGELAEVRNKtVGFVFQ--FHHLLREFTVLENVMMPCLISGLDWNVA--DERARELLVAVGLEGRLSHR-PAKLSGGEQQ 150
Cdd:COG4172 354 RRALRPLRRR-MQVVFQdpFGSLSPRMTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLDPAARHRyPHEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDsyMS--HELHDLLFQLKKDRGLAMILVTHN----RQLaqrADRIMELRDG 219
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALD--VSvqAQILDLLRDLQREHGLAYLFISHDlavvRAL---AHRVMVMKDG 502
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
2.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLA 80
Cdd:PRK13632 7 MI-KVENVSFSY---PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKtVGFVFQ-----FHHLLREFTV---LENVMmpclisgLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRV 152
Cdd:PRK13632 80 EIRKK-IGIIFQnpdnqFIGATVEDDIafgLENKK-------VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHAINK 226
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-219 |
2.96e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 109.93 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDG----HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsg 77
Cdd:COG4167 4 LLEVRNLSKTFKYRTGlfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 elAEVRNKTVGFVFQ-----FHHLLREFTVLEnvmMPcLISGLDWNVAD--ERARELLVAVGLEGRLSH-RPAKLSGGEQ 149
Cdd:COG4167 82 --YKYRCKHIRMIFQdpntsLNPRLNIGQILE---EP-LRLNTDLTAEEreERIFATLRLVGLLPEHANfYPHMLSSGQK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 150 QRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQG 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-226 |
3.90e-29 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 111.74 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 17 GHELTVLKEVEisvgSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKTVGFVFQFHHL 96
Cdd:TIGR02142 11 DFSLDADFTLP----GQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREFTVLENV---MMPCliSGLDWNVADERARELLvavGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGN 173
Cdd:TIGR02142 87 FPHLSVRGNLrygMKRA--RPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 174 LDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAINK 226
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGP 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
29-222 |
6.03e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.52 E-value: 6.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 29 SVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaevrnKTVGFVFQFHHLLREFTVLENVMM 108
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 109 PcLISGLDWNVADERARELLVA-VGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLF 187
Cdd:PRK10771 95 G-LNPGLKLNAAQREKLHAIARqMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 297171361 188 QLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLH 222
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-202 |
8.25e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.06 E-value: 8.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKMDSGEL 79
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARA 157
Cdd:PRK13649 81 KQIR-KKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTH 202
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-216 |
8.71e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 112.77 E-value: 8.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelAEV 82
Cdd:TIGR02857 322 LEFSGVSVAYPGRR----PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQFHHLLrEFTVLENVMMPCLisgldwNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQQR 151
Cdd:TIGR02857 394 WRDQIAWVPQHPFLF-AGTIAENIRLARP------DASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQR 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMEL 216
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-215 |
1.07e-28 |
|
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: 107.76 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFigGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG0410 2 PMLEVENLHAGY--GGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EvrnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERAR--ELLVAvgLEGRLSHRPAKLSGGEQQRVALARAL 158
Cdd:COG0410 77 R---LGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERvyELFPR--LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN-RQLAQRADR--IME 215
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNaRFALEIADRayVLE 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-214 |
1.14e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.82 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRF-IGGD--GHELTVLK---EVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMD 75
Cdd:COG4608 7 LLEVRDLKKHFpVRGGlfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 76 SGELAEVRnKTVGFVFQ--FHHLLREFTVLENVMMPCLISGL-DWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQR 151
Cdd:COG4608 87 GRELRPLR-RRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 152 VALARALSNYPLILLADEPSGNLD-SYMSHELhDLLFQLKKDRGLAMILVTHN----RQLaqrADRIM 214
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDvSIQAQVL-NLLEDLQDELGLTYLFISHDlsvvRHI---SDRVA 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-203 |
2.09e-28 |
|
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: 111.68 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnKTVGFVFQFHHLLrEFT 101
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLisgldwNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:TIGR02868 425 VRENLRLARP------DATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 297171361 171 SGNLDSYMSHELHDLLFQlkKDRGLAMILVTHN 203
Cdd:TIGR02868 499 TEHLDAETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-219 |
2.86e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 106.10 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 25 EVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGElaevrnKTVGFVFQFHHLLREFTVLE 104
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 105 NVMMPcLISGLDWN-VADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELH 183
Cdd:TIGR01277 90 NIGLG-LHPGLKLNaEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 297171361 184 DLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-224 |
4.81e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.55 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnKTVGFVFQFHHLLR 98
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVMM---PCLISGLDWNVADERARELLVAVGLEGRLSHRP-AKLSGGEQQRVALARALSNYPLILLADEPSGNL 174
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAAVERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 297171361 175 DsyMSHELHDL-LFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHAI 224
Cdd:PRK09536 171 D--INHQVRTLeLVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAA 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-219 |
5.76e-28 |
|
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: 105.06 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdSGELAEV 82
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03269 69 RNR-IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-209 |
6.13e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.46 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLckRFIGGDGHeltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL-----DRQTSGEVMIDGCQTSKMDSG 77
Cdd:PRK14267 5 IETVNL--RVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELaEVRnKTVGFVFQFHHLLREFTVLENVMMPCLISGL--DWNVADERARELLVAVGL----EGRLSHRPAKLSGGEQQR 151
Cdd:PRK14267 80 PI-EVR-REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR 209
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAAR 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-223 |
2.72e-27 |
|
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: 108.68 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVrnktVGFVFQFHHLLrEFT 101
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELF-DGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENvmmpclISGLDwNVADER----ARelLVAV---------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLAD 168
Cdd:COG4618 422 IAEN------IARFG-DADPEKvvaaAK--LAGVhemilrlpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 169 EPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-223 |
3.82e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.22 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHELTVlKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgELAE 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:cd03266 76 ARRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVY 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
3.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdghELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAE 81
Cdd:PRK13652 3 LIETRDLCYSYSG----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK13652 76 VR-KFVGLVFQNpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQL-AQRADRIMELRDG 219
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-221 |
4.75e-27 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 103.46 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRnKTVGFVFQFHHLLR 98
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR-RAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EfTVLENVMMPClisgldWNVADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLA 167
Cdd:cd03253 89 D-TIGYNIRYGR------PDATDEEVIEAAKAAqihdkimrfpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 168 DEPSGNLDSYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDGCL 221
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-219 |
1.28e-26 |
|
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: 102.30 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRNKtVGFVFQFHHLLREfT 101
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSM-IGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLISgldwnvADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:cd03254 93 IMENIRLGRPNA------TDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKDRGLAMIlvTHNRQLAQRADRIMELRDG 219
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKGRTSIII--AHRLSTIKNADKILVLDDG 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-214 |
1.53e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.76 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAe 81
Cdd:PRK11300 5 LLSVSGLMMRF-GG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrNKTVGFVFQFHHLLREFTVLENVMMP-------CLISGL--------DWNVADERARELLVAVGLeGRLSHRPA-KLS 145
Cdd:PRK11300 79 --RMGVVRTFQHVRLFREMTVIENLLVAqhqqlktGLFSGLlktpafrrAESEALDRAATWLERVGL-LEHANRQAgNLA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIM 214
Cdd:PRK11300 156 YGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIY 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-219 |
1.54e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.52 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskMDSGELAEV 82
Cdd:cd03268 1 LKTNDLTKTY-----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-----KSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQFHHLLREFTVLENVMMPCLISGLDwnvaDERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03268 71 LRR-IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLlSEIQKVADRIGIINKG 202
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-223 |
1.93e-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: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 17 GHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnKTVGFVFQFHHL 96
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LrEFTVLENvmmpclISGLDWNVADER---------ARELLVAV--GLEGRLSHRPAKLSGGEQQRVALARALSNYPLIL 165
Cdd:TIGR01842 404 F-PGTVAEN------IARFGENADPEKiieaaklagVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-202 |
2.92e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 100.73 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDgheltVLKEVEISVGSGeAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelaEV 82
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:cd03264 71 R-RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTH 202
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTH 187
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-203 |
4.62e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.87 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG1137 2 MTLEAENLVKSY-GK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHRPA-KLSGGEQQRVALARALS 159
Cdd:COG1137 77 ---RLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGIT-HLRKSKAySLSGGERRRVEIARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAmILVT-HN 203
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIG-VLITdHN 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-219 |
4.78e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 4.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGD-GHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmDSGELA 80
Cdd:PRK13633 4 MIKCKNVSYKYESNEeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKTvGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALS 159
Cdd:PRK13633 82 DIRNKA-GMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSG 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-216 |
6.03e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 14 GGDGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVmidgcqtskmdsgelAEVRNKTVGFVFQF 93
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 94 HHLLREF--TVLENVMMPCL--ISGLDWNVADERAR--ELLVAVGLEGrLSHRP-AKLSGGEQQRVALARALSNYPLILL 166
Cdd:NF040873 64 SEVPDSLplTVRDLVAMGRWarRGLWRRLTRDDRAAvdDALERVGLAD-LAGRQlGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 167 ADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-202 |
6.15e-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: 100.42 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 15 GDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQ---TSGEVMIDGCQTSKmdsgelAEVRnKTVGFVF 91
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP------DQFQ-KCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 92 QFHHLLREFTVLENVMMpCLISGLDwNVADERARELLVAVGLEGRLSHRPAK------LSGGEQQRVALARALSNYPLIL 165
Cdd:cd03234 88 QDDILLPGLTVRETLTY-TAILRLP-RKSSDAIRKKRVEDVLLRDLALTRIGgnlvkgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTH 202
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIH 201
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-219 |
6.71e-26 |
|
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: 100.38 E-value: 6.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgELAEVRNKtVGFVFQFHH 95
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ-IGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVMMpclisGLDwNVADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLI 164
Cdd:cd03251 87 LFND-TVAENIAY-----GRP-GATREEVEEAARAAnahefimelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 165 LLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVLEDG 212
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-203 |
7.49e-26 |
|
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: 100.43 E-value: 7.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:TIGR04406 1 TLVAENLIKSY-----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VrnkTVGFVFQFHHLLREFTVLENVMMPCLISG-LDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:TIGR04406 76 L---GIGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN 203
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHN 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-219 |
7.88e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.34 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFiGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgelA 80
Cdd:COG3845 4 PALELRGITKRF-GG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----------K 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 EVRNKT--------VGFVFQfhH--LLREFTVLENVMM---PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGG 147
Cdd:COG3845 68 PVRIRSprdaialgIGMVHQ--HfmLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 148 EQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN----RQLaqrADRIMELRDG 219
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKlrevMAI---ADRVTVLRRG 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-221 |
2.13e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 15 GDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ-TSKMDSGELAEVRnKTVGFVFQF 93
Cdd:PRK13646 15 GTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIRPVR-KRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 94 -HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGR-LSHRPAKLSGGEQQRVALARALSNYPLILLADEPS 171
Cdd:PRK13646 94 pESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 172 GNLDSYMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-203 |
2.89e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGeLAE 81
Cdd:PRK13636 5 ILKVEELNYNY--SDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKG-LMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHRPAK-LSGGEQQRVALARALS 159
Cdd:PRK13636 80 LR-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-203 |
3.33e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.39 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelAE 81
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP----EY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQ------FHHLlrefTVLENVMM-------PCLISGLDwnvADERA--RELL--VAVGLEGRLSHRPAKL 144
Cdd:COG1101 77 KRAKYIGRVFQdpmmgtAPSM----TIEENLALayrrgkrRGLRRGLT---KKRRElfRELLatLGLGLENRLDTKVGLL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 145 SGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-221 |
5.54e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 98.17 E-value: 5.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEvrnk 85
Cdd:cd03267 20 IGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 tVGFVF-QFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHRPA-KLSGGEQQRVALARALSNYPL 163
Cdd:cd03267 96 -IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLE-ELLDTPVrQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 164 ILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKGRL 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
23-221 |
7.00e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLL---GGLDRQ--TSGEVMIDGCQ--TSKMDSGELaevrNKTVGFVFQ--- 92
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEvtITGSIVYNGHNiySPRTDTVDL----RKEIGMVFQqpn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 93 -FhhllrEFTVLENVMMPCLISGL-DWNVADERARELLVAVGL----EGRLSHRPAKLSGGEQQRVALARALSNYPLILL 166
Cdd:PRK14239 97 pF-----PMSIYENVVYGLRLKGIkDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 167 ADEPSGNLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRiSDRTGFFLDGDL 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
22-220 |
7.15e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.91 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmDSGELAEVRnktVGFVFQFHHLLREFT 101
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARAR---IGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHE 181
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 297171361 182 LHDLLFQLKKdRGLAMILVTHNRQLAQR-ADRIMELRDGC 220
Cdd:PRK13536 211 IWERLRSLLA-RGKTILLTTHFMEEAERlCDRLCVLEAGR 249
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-216 |
1.34e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 8 LCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelaEVRNKTV 87
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP----EIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 88 GFVFQFHHLLREfTVLENVMMPCLISGldwNVADERA-RELLVAVGL-EGRLSHRPAKLSGGEQQRVALARALSNYPLIL 165
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIFPWQIRN---QQPDPAIfLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-219 |
4.28e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.47 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV 82
Cdd:PRK09700 6 ISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnkTVGFVFQFHHLLREFTVLENVMMP-------CLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALA 155
Cdd:PRK09700 81 ---GIGIIYQELSVIDELTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 156 RALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-219 |
6.68e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMI-DGCQTSKMDSGELAEVRNKtVGFVFQF-HHLLREF 100
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRKK-VGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 TVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMS 179
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 180 HELHDlLFQLKKDRGLAMILVTH-NRQLAQRADRIMELRDG 219
Cdd:PRK13643 181 IEMMQ-LFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-219 |
9.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAE 81
Cdd:PRK13650 4 IIEVKNLTFKY--KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQfhHLLREF---TVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARAL 158
Cdd:PRK13650 79 IRHK-IGMVFQ--NPDNQFvgaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-219 |
9.80e-24 |
|
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: 93.15 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmdsgELAEVRNKTVGFVFQFHH 95
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-----DLEKALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVmmpclisgldwnvaderarellvavgleGRlshrpaKLSGGEQQRVALARA-LSNYPLILLaDEPSGNL 174
Cdd:cd03247 86 LFDT-TLRNNL----------------------------GR------RFSGGERQRLALARIlLQDAPIVLL-DEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 175 DSYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03247 130 DPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMDKILFLENG 172
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-221 |
1.27e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDR------QTSGEVMIDGCQTSKMDSGELaevrNKTVGFVFQFHH 95
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREFTVLENVMMPCLISGL-DWNVADERARELLVAVGL----EGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKDrgLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNpQQVARVADYVAFLYNGEL 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-203 |
1.51e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.19 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKR------FIGGDGHeLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMD 75
Cdd:PRK11308 5 LLQAIDLKKHypvkrgLFKPERL-VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 76 SGELAEVRNKtVGFVFQ--FHHLLREFTVLENVMMPCLI-SGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQR 151
Cdd:PRK11308 84 PEAQKLLRQK-IQIVFQnpYGSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRPEHYDRyPHMFSGGQRQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.70e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MIlEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:COG4604 1 MI-EIKNVSKRY-----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrnKTVGFVFQFHHLLREFTVLENVMM---PclISGLDWNVADERA-RELLVAVGLEGrLSHRPAK-LSGGEQQRVALA 155
Cdd:COG4604 75 ----KRLAILRQENHINSRLTVRELVAFgrfP--YSKGRLTAEDREIiDEAIAYLDLED-LADRYLDeLSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 156 RAL---SNYplILLaDEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:COG4604 148 MVLaqdTDY--VLL-DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVA 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-214 |
3.00e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgelaEV 82
Cdd:PRK11650 4 LKLQAVRKSYDGK----TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL------EP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:PRK11650 74 ADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 163 LILLADEPSGNLDS----YMSHELHDLLFQLkkdrGLAMILVTHNRQLAQR-ADRIM 214
Cdd:PRK11650 154 AVFLFDEPLSNLDAklrvQMRLEIQRLHRRL----KTTSLYVTHDQVEAMTlADRVV 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-219 |
3.49e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDsgelAE 81
Cdd:COG4152 1 MLELKGLTKRF--GD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLD----PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFvfqfhhLLRE------FTVLEnvmmpCLI-----SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQ 150
Cdd:COG4152 69 DRRR-IGY------LPEErglypkMKVGE-----QLVylarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 151 RVALARALSNYP--LILlaDEP-SGnLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG4152 137 KVQLIAALLHDPelLIL--DEPfSG-LDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEElCDRIVIINKG 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-202 |
7.83e-23 |
|
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: 91.46 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDG-HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDR--QTSGEVMIDGCQTSKmdsg 77
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSkSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 elaEVRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLdwnvaderarellvavglegrlshrpaklSGGEQQRVALARA 157
Cdd:cd03213 78 ---RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTH 202
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-219 |
8.68e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 8.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdgcqtskmdsGElae 81
Cdd:COG0488 315 VLELEGLSKSY--GD---KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL----------GE--- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrNKTVGFVFQFHHLLR-EFTVLENvmmpclISGLDWNVADERARELLVAVGLEGRLSHRPAK-LSGGEQQRVALARAL- 158
Cdd:COG0488 377 --TVKIGYFDQHQEELDpDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGvLSGGEKARLALAKLLl 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 159 SNYPLILLaDEPSGNLDSYMSHELHDLL--FQlkkdrGlAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:COG0488 449 SPPNVLLL-DEPTNHLDIETLEALEEALddFP-----G-TVLLVSHDRYFLDRvATRILEFEDG 505
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-219 |
1.10e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.16 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 14 GGDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELaevrNKTVGFVFQ- 92
Cdd:cd03252 11 KPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 93 ---FHHLLREFTVLENVMMPC--LISGLDWNVADERARELlvAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLA 167
Cdd:cd03252 85 nvlFNRSIRDNIALADPGMSMerVIEAAKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 168 DEPSGNLDSYMSH----ELHDLLfqlkkdRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03252 163 DEATSALDYESEHaimrNMHDIC------AGRTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
1.16e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMI-------DGCQTSKM 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 75 DSGELAEVRN-----KTVGFVFQF--HHLLREfTVLENVMMPCLISGLDWNVADERARELLVAVGL-EGRLSHRPAKLSG 146
Cdd:PRK13631 101 TNPYSKKIKNfkelrRRVSMVFQFpeYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 147 GEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKG 252
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-218 |
1.29e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDR---QTSGEVMIDGcqtSKMDSGELAEVrnktVGFVFQFHH 95
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNG---MPIDAKEMRAI----SAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREFTVLENVM------MPcliSGLDWNVADERARELLVAVGL----------EGRLShrpaKLSGGEQQRVALARALS 159
Cdd:TIGR00955 110 FIPTLTVREHLMfqahlrMP---RRVTKKEKRERVDEVLQALGLrkcantrigvPGRVK----GLSGGERKRLAFASELL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHnrqlaQRADRIMELRD 218
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH-----QPSSELFELFD 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-209 |
1.94e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDG------HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMD 75
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 76 SGELAEVRnKTVGFVFQ--FHHLLREFTVLENVMMPCLISGL-DWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQR 151
Cdd:PRK10261 393 PGKLQALR-RDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 152 VALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR 209
Cdd:PRK10261 472 ICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVER 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-221 |
2.51e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELaevrNKTVGFVFQFHHLLREfT 101
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMpclisGLDwNVADERARELLVAVGLEGRLSHRP-----------AKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:TIGR00958 571 VRENIAY-----GLT-DTPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 171 SGNLDSymshELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:TIGR00958 645 TSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-219 |
2.69e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.02 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 37 AVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGEL--AEVRNktVGFVFQFHHLLREFTVLENvmmpcLISG 114
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClpPEKRR--IGYVFQDARLFPHYKVRGN-----LRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 115 LDWNVADERAR--ELLvavGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKD 192
Cdd:PRK11144 101 MAKSMVAQFDKivALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180
....*....|....*....|....*...
gi 297171361 193 RGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK11144 178 INIPILYVSHSLDEILRlADRVVVLEQG 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-202 |
3.02e-22 |
|
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: 90.11 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNL-CKRfiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskMDSGELAE 81
Cdd:TIGR01189 1 LAARNLaCSR------GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG-----TPLAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLISGldwnVADERARELLVAVGLEGrLSHRPA-KLSGGEQQRVALARA-LS 159
Cdd:TIGR01189 70 EPHENILYLGHLPGLKPELSALENLHFWAAIHG----GAQRTIEDALAAVGLTG-FEDLPAaQLSAGQQRRLALARLwLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 160 NYPLILLaDEPSGNLDSyMSHELHDLLFQLKKDRGLAMILVTH 202
Cdd:TIGR01189 145 RRPLWIL-DEPTTALDK-AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-219 |
3.08e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 90.67 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGDGH-----------------ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVM 65
Cdd:cd03220 1 IELENVSKSYPTYKGGssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 66 IDGCQTSKMDSGelaevrnktVGFvfqfhhlLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLsHRPAK-L 144
Cdd:cd03220 81 VRGRVSSLLGLG---------GGF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPVKtY 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 145 SGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDpSSIKRLCDRALVLEKG 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
3.82e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHEltVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelAE 81
Cdd:PRK13647 4 IIEVEDLHFRY--KDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE---KW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQ------FhhllrEFTVLENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHR-PAKLSGGEQQRVAL 154
Cdd:PRK13647 77 VRSK-VGLVFQdpddqvF-----SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKpPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 155 ARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLA-QRADRIMELRDG 219
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAaEWADQVIVLKEG 214
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-219 |
5.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFigGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAE 81
Cdd:PRK13642 4 ILEVENLVFKY--EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQF-HHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK13642 79 LRRK-IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-219 |
5.38e-22 |
|
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: 90.29 E-value: 5.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRNKtVGFVFQFHHLLr 98
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQ-IGLVSQEPVLF- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVMMpclisGLDWNVADERARELLVAV----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLAD 168
Cdd:cd03249 90 DGTIAENIRY-----GKPDATDEEVEEAAKKANihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 169 EPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRNADLIAVLQNG 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-203 |
6.54e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKtVGFVFQFHHLLREFT 101
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLI-SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSH 180
Cdd:PRK11831 101 VFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
170 180
....*....|....*....|...
gi 297171361 181 ELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK11831 181 VLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
8.04e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdgcQTSKMDSGELAEVRnKTVGFVFQ-----FHHLL 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLR-KHIGIVFQnpdnqFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 98 REFTV---LENVMMPclisgldWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNL 174
Cdd:PRK13648 101 VKYDVafgLENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 175 DSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-224 |
9.13e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGH-----------------ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEV 64
Cdd:COG1134 4 MIEVENVSKSYRLYHEPsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 65 MIDGCQTSkmdsgeLAEVrnkTVGFVfqfhhllREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLsHRPAK- 143
Cdd:COG1134 84 EVNGRVSA------LLEL---GAGFH-------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQPVKt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 144 LSGGEQQRVALARALSNYPLILLADEpsgNL---DSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDE---VLavgDAAFQKKCLARIRELRE-SGRTVIFVSHSmGAVRRLCDRAIWLEKG 222
|
....*
gi 297171361 220 CLHAI 224
Cdd:COG1134 223 RLVMD 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-219 |
9.86e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.99 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGheltvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:PRK11701 6 LLSVRGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTV-----GFVFQfhhllreftvleNVMMpclisGLDWNV-ADERARELLVAVG--------------LE------G 135
Cdd:PRK11701 81 AERRRLlrtewGFVHQ------------HPRD-----GLRMQVsAGGNIGERLMAVGarhygdiratagdwLErveidaA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 136 RLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQ-RADRIM 214
Cdd:PRK11701 144 RIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLL 223
|
....*
gi 297171361 215 ELRDG 219
Cdd:PRK11701 224 VMKQG 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-219 |
1.13e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdghELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLlggLDRQ---TSGEVMIDGCQTSKMDSGEL 79
Cdd:PRK11160 339 LTLNNVSFTYPDQ---PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRAwdpQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 aevRNkTVGFVFQFHHLLREfTVLENVMMPCLisgldwNVADERARELLVAVGLEGRLSH------------RPakLSGG 147
Cdd:PRK11160 413 ---RQ-AISVVSQRVHLFSA-TLRDNLLLAAP------NASDEALIEVLQQVGLEKLLEDdkglnawlgeggRQ--LSGG 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 148 EQQRVALARA-LSNYPLILLaDEPSGNLDSYMSHELHDLLFQLKKDRGLAMIlvTHNRQLAQRADRIMELRDG 219
Cdd:PRK11160 480 EQRRLGIARAlLHDAPLLLL-DEPTEGLDAETERQILELLAEHAQNKTVLMI--THRLTGLEQFDRICVMDNG 549
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-219 |
1.15e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdGCQTSKMDSGELAEVRN--KTVGFVFQF--H 94
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEVKRlrKEIGLVFQFpeY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 95 HLLREfTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRVALARALSNYPLILLADEPSGN 173
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 297171361 174 LDSYMSHELHDLLFQLKKDRGLAMILVTHNR-QLAQRADRIMELRDG 219
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEG 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-219 |
1.30e-21 |
|
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: 86.73 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDgcqtskmdsgelaev 82
Cdd:cd03221 1 IELENLSKTY-----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKTVGFVFQfhhllreftvlenvmmpclisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARALSNYP 162
Cdd:cd03221 61 STVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDllfQLKKDRGlAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEE---ALKEYPG-TVILVSHDRYFLDQvATKIIELEDG 143
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-223 |
1.51e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL---DRQTSGEVMIDGcqtSKMDSGELAEVRNKtVGFVFQfhHLLR 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLTAKTVWDIREK-VGIVFQ--NPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EF---TVLENVMMpclisGLDwNVADER------ARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADE 169
Cdd:PRK13640 96 QFvgaTVGDDVAF-----GLE-NRAVPRpemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 170 PSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCLHA 223
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-215 |
2.84e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.17 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKS-TLLHLLGGLDR--QTSGEVMIDGCQTSKMDSGE 78
Cdd:PRK09473 12 LLDVKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 79 LAEVRNKTVGFVFQ-----FHHLLREFTVLENVMMpcLISGLDWNVADERARELLVAVGL---EGRLSHRPAKLSGGEQQ 150
Cdd:PRK09473 91 LNKLRAEQISMIFQdpmtsLNPYMRVGEQLMEVLM--LHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTH---------NRQLAQRADRIME 215
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHdlgvvagicDKVLVMYAGRTME 242
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-209 |
2.97e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdgCQTSKMDSGELAE 81
Cdd:PRK13537 7 PIDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL--CGEPVPSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnktVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNY 161
Cdd:PRK13537 80 QR---VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 297171361 162 PLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHNRQLAQR 209
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAER 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-219 |
3.54e-21 |
|
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: 86.72 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfiggdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelAE 81
Cdd:cd03215 4 VLEVRGLSVK---------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP---RD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHH---LLREFTVLENVMMPCLisgldwnvaderarellvavglegrlshrpakLSGGEQQRVALARAL 158
Cdd:cd03215 72 AIRAGIAYVPEDRKregLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILV-THNRQLAQRADRIMELRDG 219
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLIsSELDELLGLCDRILVMYEG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-219 |
4.81e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 86.75 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRqTSGEVMIdgcqtskmdsgelaevrNKTVGFVFQFHHLLREf 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSV-----------------PGSIAYVSQEPWIQNG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 TVLENVMMpclisGLDWNvaDERARELLVAVGLEGRLSHRPAK-----------LSGGEQQRVALARAL-SNYPLILLaD 168
Cdd:cd03250 81 TIRENILF-----GKPFD--EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVySDADIYLL-D 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 169 EPSGNLDSYMSHELHDLLFQ--LKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILglLLNNK--TRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-217 |
5.08e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNL-CKRfiggDGHELtvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelae 81
Cdd:PRK13538 2 LEARNLaCER----DERIL--FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrnktvgfvfQFHHLL----------REFTVLENVMMPCLISGLdwnVADERARELLVAVGLEGRLsHRPAK-LSGGEQQ 150
Cdd:PRK13538 71 ----------EYHQDLlylghqpgikTELTALENLRFYQRLHGP---GDDEALWEALAQVGLAGFE-DVPVRqLSAGQQR 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 151 RVALAR-ALSNYPLILLaDEPSGNLDSYMSHELHDLLFQlKKDRGLAMILVTHnRQLAQRADRIMELR 217
Cdd:PRK13538 137 RVALARlWLTRAPLWIL-DEPFTAIDKQGVARLEALLAQ-HAEQGGMVILTTH-QDLPVASDKVRKLR 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-219 |
5.83e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 90.57 E-value: 5.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKTVGFVFQFhhllrEFT 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF-----SGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMpclisGLDWNVADERARELL-----------VAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:TIGR01193 564 ILENLLL-----GAKENVSQDEIWAACeiaeikddienMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKDrglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-219 |
7.09e-21 |
|
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: 90.25 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMID-GCQTSKM-DSGEL 79
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMtKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNKT-VGFVFQFHHLLREFTVLENvmmpcLISGLDWNVADERARE----LLVAVGLEGR-----LSHRPAKLSGGEQ 149
Cdd:TIGR03269 359 GRGRAKRyIGILHQEYDLYPHRTVLDN-----LTEAIGLELPDELARMkaviTLKMVGFDEEkaeeiLDKYPDELSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 150 QRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDG 504
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
7.97e-21 |
|
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: 86.76 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEVrnktVGFVFQ----FHHLL 97
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK----VSLVGQepvlFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 98 REFTV--LENVMMPCLISGLDWNVADERARELlvAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:cd03248 105 QDNIAygLQSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 297171361 176 SYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03248 183 AESEQQVQQALYDWPERRTV--LVIAHRLSTVERADQILVLDGG 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-219 |
9.89e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRFIGGDG----HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDS 76
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GelaeVRNKTVGFVFQ-----FHHLLREFTVLENVMMpcLISGLDWNVADERARELLVAVGL-EGRLSHRPAKLSGGEQQ 150
Cdd:PRK15112 83 S----YRSQRIRMIFQdpstsLNPRQRISQILDFPLR--LNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVT-HNRQLAQRADRIMELRDG 219
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQG 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-219 |
1.52e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.47 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelAEVRNKTVGFVFQFHHLLR 98
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AKIMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVMMPCLISGLD-WNVADERARELLVAvgLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSY 177
Cdd:PRK11614 94 RMTVEENLAMGGFFAERDqFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 178 MSHELHDLLFQLKKDrGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK11614 172 IIQQIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENG 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-203 |
1.89e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNL-CKRfiGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGEL 79
Cdd:PRK13539 1 MMLEGEDLaCVR--GGR----VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEvrnktvgfvfQFHHL------LREFTVLENVMMpclisgldW----NVADERARELLVAVGLeGRLSHRPAK-LSGGE 148
Cdd:PRK13539 72 AE----------ACHYLghrnamKPALTVAENLEF--------WaaflGGEELDIAAALEAVGL-APLAHLPFGyLSAGQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 149 QQRVALARAL-SNYPLILLaDEPSGNLDSYmSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK13539 133 KRRVALARLLvSNRPIWIL-DEPTAALDAA-AVALFAELIRAHLAQGGIVIAATHI 186
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-219 |
2.54e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELtvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMI-DG------CQTSKMDSGELAEVrnktvg 88
Cdd:COG4178 374 DGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGarvlflPQRPYLPLGTLREA------ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 89 fvfqfhhLLREFTVLEnvmmpclisgldwnVADERARELLVAVGLeGRLSHR-------PAKLSGGEQQRVALARALSNY 161
Cdd:COG4178 446 -------LLYPATAEA--------------FSDAELREALEAVGL-GHLAERldeeadwDQVLSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 162 PLILLADEPSGNLDsymsHELHDLLFQLKKDR--GLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:COG4178 504 PDWLFLDEATSALD----EENEAALYQLLREElpGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-219 |
2.69e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL--DRQTSGEVMIDGcqtSKMDSGEL 79
Cdd:PRK13549 5 LLEMKNITKTFGG-----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEG---EELQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNKTVGFVFQFHHLLREFTVLENVMMPCLISG---LDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:PRK13549 77 RDTERAGIAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKA-HGIACIYISHKlNEVKAISDTICVIRDG 219
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-203 |
2.69e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRF-IGGDGH-------ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTS 72
Cdd:PRK15079 7 VLLEVADLKVHFdIKDGKQwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 73 KMDSGELAEVRnKTVGFVFQ--FHHLLREFTVLENVMMPCLI--SGLDWNVADERARELLVAVGLEGRLSHR-PAKLSGG 147
Cdd:PRK15079 87 GMKDDEWRAVR-SDIQMIFQdpLASLNPRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 148 EQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN 203
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-219 |
3.38e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.36 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCkrFIGGDGHELTvlKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRQtsGEVMIDGCQTSKMDsgeLAE 81
Cdd:PRK11174 350 IEAEDLE--ILSPDGKTLA--GPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFLPYQ--GSLKINGIELRELD---PES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRnKTVGFVFQFHHLLREfTVLENVMMPclisglDWNVADERARELL-----------VAVGLEGRLSHRPAKLSGGEQQ 150
Cdd:PRK11174 421 WR-KHLSWVGQNPQLPHG-TLRDNVLLG------NPDASDEQLQQALenawvseflplLPQGLDTPIGDQAAGLSVGQAQ 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKkdRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK11174 493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-203 |
4.38e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgELAE 81
Cdd:PRK10895 3 TLTAKNLAKAYKG-----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHHLLREFTVLENVMMPCLI-SGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSN 160
Cdd:PRK10895 75 RARRGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 161 YPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN 203
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHN 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-219 |
5.80e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTS--GEVMIDG--CQTSKMDSG 77
Cdd:NF040905 1 ILEMRGITKTFPG-----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevCRFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ElaevrnkTVGFVF--QFHHLLREFTVLENVMM--PCLISGL-DWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRV 152
Cdd:NF040905 76 E-------ALGIVIihQELALIPYLSIAENIFLgnERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-219 |
6.56e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGdGHELTVLKEVEISVGSGEAVAVVGSSGAGKS-TLLHLLGGLDRQ----TSGEVMIDGCQTSKMDS 76
Cdd:PRK15134 5 LLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GELAEVRNKTVGFVFQ--------FHHLLRE-FTVLEnvmmpcLISGLDWNVADERARELLVAVGLE---GRLSHRPAKL 144
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQepmvslnpLHTLEKQlYEVLS------LHRGMRREAARGEILNCLDRVGIRqaaKRLTDYPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 145 SGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-224 |
7.63e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSgelAE 81
Cdd:COG3845 257 VLEVENLSVR----DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP---RE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQ--FHH-LLREFTVLENVMM-----PCLISG--LDWNVADERARELLVAVGLEGRLSHRPAK-LSGGEQQ 150
Cdd:COG3845 330 RRRLGVAYIPEdrLGRgLVPDMSVAENLILgryrrPPFSRGgfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN----RQLaqrADRIMELRDGCLHAI 224
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDldeiLAL---SDRIAVMYEGRIVGE 483
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-217 |
1.11e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.31 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNL-CKRfiggdgHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsGELAE 81
Cdd:cd03231 1 LEADELtCER------DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--------GPLDF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVGFVFQFHH---LLREFTVLENVMMPCLISGldwnvaDERARELLVAVGLEGrLSHRP-AKLSGGEQQRVALARA 157
Cdd:cd03231 67 QRDSIARGLLYLGHapgIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 158 LSNYPLILLADEPSGNLDSyMSHELHDLLFQLKKDRGLAMILVTHnRQLAQRADRIMELR 217
Cdd:cd03231 140 LLSGRPLWILDEPTTALDK-AGVARFAEAMAGHCARGGMVVLTTH-QDLGLSEAGARELD 197
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-219 |
1.31e-19 |
|
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: 84.11 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGheltvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG-----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTV-----GFVFQ--FHHLLREFTVLENV-MMPCLISGLDWNVADERARELLVAVGLE-GRLSHRPAKLSGGEQQRV 152
Cdd:TIGR02323 78 AERRRLmrtewGFVHQnpRDGLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQ-RADRIMELRDG 219
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQG 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-214 |
1.34e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 85.18 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKS-TLLHLLGGLDrqTSGEVMIDGCQTSKMDSGELA 80
Cdd:PRK11022 3 LLNVDKLSVHF-GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 E-VRNKTVG----FVFQ--FHHLLREFTVLENVMMPCLI-SGLDWNVADERARELLVAVGL---EGRLSHRPAKLSGGEQ 149
Cdd:PRK11022 80 EkERRNLVGaevaMIFQdpMTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 150 QRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQL-AQRADRIM 214
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKII 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-219 |
3.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSkmDSGELAEVRnKTVGFVFQ------FHHL 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG--DFSKLQGIR-KLVGIVFQnpetqfVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREFTVL--ENVMMPCLisgldwnVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNL 174
Cdd:PRK13644 95 VEEDLAFgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 297171361 175 DSYMSHElhdLLFQLKK--DRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK13644 168 DPDSGIA---VLERIKKlhEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-219 |
3.76e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 26 VEISVGSGEAVAVVGSSGAGKS-TLLHLLGGLD---RQTSGEVMIDGCQTSkmdsgeLAEVRNKTVGFVFQ-----FHHL 96
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVA------PCALRGRKIATIMQnprsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LrefTVLENVMMPCLISGLdwNVADERARELLVAVGLEGR---LSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGN 173
Cdd:PRK10418 96 H---TMHTHARETCLALGK--PADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 297171361 174 LDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-219 |
3.84e-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: 85.26 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTS--GEVMIDGcqtSKMDSGEL 79
Cdd:TIGR02633 1 LLEMKGIVKTFGG-----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSG---SPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNKTVGFVFQFHHLLREFTVLENVMMPCLISG----LDWNVADERARELLVAVGLEGRLSHRP-AKLSGGEQQRVAL 154
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLGNEITLpggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 155 ARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-220 |
5.02e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ---TSKMDSgel 79
Cdd:PRK11288 5 LSFDGIGKTFPG-----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfASTTAA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 aevRNKTVGFVFQFHHLLREFTVLENVM---MPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:PRK11288 77 ---LAAGVAIIYQELHLVPEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHnrqlaqRADRIMELRDGC 220
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSH------RMEEIFALCDAI 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-221 |
2.27e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgELAEVRNKtVGFVFQFHH 95
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLRNQ-VALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVMMPClisGLDWNVAD-ERARELLVAV--------GLEGRLSHRPAKLSGGEQQRVALARA-LSNYPlIL 165
Cdd:PRK11176 428 LFND-TIANNIAYAR---TEQYSREQiEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARAlLRDSP-IL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 166 LADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-219 |
2.58e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnKTVGFVFQFHHLLREF 100
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 TVLENVM---MPCLISGLDWNVADERA-RELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDs 176
Cdd:PRK10253 97 TVQELVArgrYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 297171361 177 yMSHE--LHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK10253 176 -ISHQidLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREG 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-219 |
2.58e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDG----------CQT 71
Cdd:PRK10261 12 VLAVENLNIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 72 SKMDSGELAEVRNKTVGFVFQ--FHHLLREFTVLENVMMPC-LISGLDWNVADERARELLVAVGL---EGRLSHRPAKLS 145
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ-LAQRADRIMELRDG 219
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
3.12e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSG-----EVMIDGcqTSKMDSG 77
Cdd:PRK14271 22 MAAVNLTLGFAGK-----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGG--RSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKtVGFVFQFHHLLrEFTVLENVMMPC----LISGLDWN-VADERARELLVAVGLEGRLSHRPAKLSGGEQQRV 152
Cdd:PRK14271 95 DVLEFRRR-VGMLFQRPNPF-PMSIMDNVLAGVrahkLVPRKEFRgVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRgLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:PRK14271 173 CLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADR-LTVIIVTHNlAQAARISDRAALFFDGRL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-205 |
3.16e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFIGgdghELTVLKEVEISVGSGEAVAVVGSSGAGKST----LLHLLggldrQTSGEVMIDGCQTSKMDSGELAE 81
Cdd:PRK15134 289 KGILKRTVD----HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKtVGFVFQ--FHHLLREFTVLE------NVMMPCLISGldwnVADERARELLVAVGLEGRLSHR-PAKLSGGEQQRV 152
Cdd:PRK15134 360 VRHR-IQVVFQdpNSSLNPRLNVLQiieeglRVHQPTLSAA----QREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRI 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ 205
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-219 |
7.00e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgeLAE 81
Cdd:PRK15439 11 LLCARSISKQYSG-----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-----LTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTVG--FVFQFHHLLREFTVLENVMMpclisGLDWNVAD-ERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARAL 158
Cdd:PRK15439 81 AKAHQLGiyLVPQEPLLFPNLSVKENILF-----GLPKRQASmQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 159 SNYPLILLADEPSGNLdsyMSHELHDLLFQLKK--DRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK15439 156 MRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKlPEIRQLADRISVMRDG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-219 |
2.07e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfiggdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgelAE 81
Cdd:COG1129 256 VLEVEGLSVG---------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG-----------KP 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 VRNKTV------GFVF-----QFHHLLREFTVLENVMMPCLISGLDWNVADeRARELLVAVGLEGRLSHRPA-------K 143
Cdd:COG1129 316 VRIRSPrdairaGIAYvpedrKGEGLVLDLSIRENITLASLDRLSRGGLLD-RRRERALAEEYIKRLRIKTPspeqpvgN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 144 LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVT-------HNrqlaqrADRIMEL 216
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISselpellGL------SDRILVM 467
|
...
gi 297171361 217 RDG 219
Cdd:COG1129 468 REG 470
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-222 |
2.36e-17 |
|
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: 80.44 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtsKMDSGELAEVRnK 85
Cdd:TIGR01257 932 KNLVKIF---EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIETNLDAVR-Q 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 TVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLIL 165
Cdd:TIGR01257 1004 SLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 166 LADEPSGNLDSYMSHELHDLLfqLKKDRGLAMILVTHNRQLAQ-RADRIMELRDGCLH 222
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-223 |
2.57e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 29 SVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQtSGEVMIDGCQTSKMDSGELAEVR------NKTVGF--VFQFHHLLREf 100
Cdd:COG4138 18 QVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRaylsqqQSPPFAmpVFQYLALHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 tvlenvmmpcliSGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARA-LSNYPLI------LLADEPSGN 173
Cdd:COG4138 96 ------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegqlLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 297171361 174 LDsyMSHE--LHDLLFQLkKDRGLAMILVTH--NRQLaQRADRIMELRDGCLHA 223
Cdd:COG4138 164 LD--VAQQaaLDRLLREL-CQQGITVVMSSHdlNHTL-RHADRVWLLKQGKLVA 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-219 |
3.97e-17 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.99 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 17 GHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmDSGELAEVRNK-TVGFVFQFHH 95
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESE-PSFEATRSRNRySVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVMMPCLISGLDWNVADErAREL-----LVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:cd03290 90 LLNA-TVEENITFGSPFNKQRYKAVTD-ACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 171 SGNLDSYMS-HELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03290 168 FSALDIHLSdHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-219 |
1.05e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.05 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDgcqtskmdsgelaevRNKTVGFVFQFHHLLREFT 101
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ---------------PGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCL-----------ISGL------DWNV-ADERAR--ELLVAVG---LEGRLS------------HRPAKLSG 146
Cdd:TIGR03719 85 VRENVEEGVAeikdaldrfneISAKyaepdaDFDKlAAEQAElqEIIDAADawdLDSQLEiamdalrcppwdADVTKLSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 147 GEQQRVALARALSNYPLILLADEPSGNLD----SYMSHELHDLlfqlkkdRGlAMILVTHNRQ-LAQRADRIMELRDG 219
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDaesvAWLERHLQEY-------PG-TVVAVTHDRYfLDNVAGWILELDRG 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-209 |
1.36e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.36 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDR-----QTSGEVMIDGCQ--TSKMDSgelAEVRNKtVGFVFQFHH 95
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDP---VEVRRR-IGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREfTVLENVMMPCLISGLDWNVADERARELLVAV---GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSG 172
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAAlwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 297171361 173 NLDSYMSHELHDLLFQLKKDrgLAMILVTHNRQLAQR 209
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAAR 215
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-203 |
1.37e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgelaEVRNKTVGFVFQFHH 95
Cdd:PRK15056 18 NGH--TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREFTVL-ENVMMPCLISGLDW-NVADERAREL----LVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADE 169
Cdd:PRK15056 89 VDWSFPVLvEDVVMMGRYGHMGWlRRAKKRDRQIvtaaLARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|....
gi 297171361 170 PSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN 203
Cdd:PRK15056 169 PFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-223 |
1.97e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKrfigGDGHElTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELA 80
Cdd:PRK11231 1 MTLRTENLTV----GYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrnKTVGFVFQfHHLLRE-FTVLEnvmmpclisgldwnvaderarelLVAVG------LEGRLS--------------- 138
Cdd:PRK11231 76 ----RRLALLPQ-HHLTPEgITVRE-----------------------LVAYGrspwlsLWGRLSaednarvnqameqtr 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 139 ------HRPAKLSGGEQQRVALARALS-NYPLILLaDEPSGNLDsyMSH--ELHDLLFQLkKDRGLAMILVTHNRQLAQR 209
Cdd:PRK11231 128 inhladRRLTDLSGGQRQRAFLAMVLAqDTPVVLL-DEPTTYLD--INHqvELMRLMREL-NTQGKTVVTVLHDLNQASR 203
|
250
....*....|....*
gi 297171361 210 -ADRIMELRDGCLHA 223
Cdd:PRK11231 204 yCDHLVVLANGHVMA 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-223 |
2.15e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGG--------LDRQTSGEVMIDGCQTSKMDSGELAEVRnktvGFVFQ 92
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAIDAPRLARLR----AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 93 FHHLLREFTVLENVMMPCL--------ISGLDWNVADeRARELLVAVGLEGRlshRPAKLSGGEQQRVALARALSNY--- 161
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYpharragaLTHRDGEIAW-QALALAGATALVGR---DVTTLSGGELARVQFARVLAQLwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 162 ------PLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCLHA 223
Cdd:PRK13547 167 hdaaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVA 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-219 |
2.48e-16 |
|
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: 77.17 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDG------CQTSkmdsgelaeVRnKTVGFVFQfh 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvTQAS---------LR-AAIGIVPQ-- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 95 hllreFTVLENvmmpcliSGLDWNVADERA---RELLVAV---------------GLEGRLSHRPAKLSGGEQQRVALAR 156
Cdd:COG5265 440 -----DTVLFN-------DTIAYNIAYGRPdasEEEVEAAaraaqihdfieslpdGYDTRVGERGLKLSGGEKQRVAIAR 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 157 ALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:COG5265 508 TLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVDADEILVLEAG 568
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-211 |
4.01e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.07 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDrQTSGEVMIDG-----CQTSKMDSGELAEVRnKTVGFVFQFHHL 96
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGrveffNQNIYERRVNLNRLR-RQVSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LrEFTVLENVMMPCLISGLDWNVA-DERARELLVAVGLEGRLSHRPAK----LSGGEQQRVALARALSNYPLILLADEPS 171
Cdd:PRK14258 100 F-PMSVYDNVAYGVKIVGWRPKLEiDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 172 GNLDSYMSHELHDLLFQLKKDRGLAMILVTHN-RQLAQRAD 211
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSD 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-219 |
4.14e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAevrnKTVGFVFQFHHLLREF 100
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 TVLENVMmpclISGLDWN-------VAD-ERARELLVAVGLEgRLSHRPA-KLSGGEQQRVALARALSNYPLILLADEPS 171
Cdd:PRK10575 101 TVRELVA----IGRYPWHgalgrfgAADrEKVEEAISLVGLK-PLAHRLVdSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 172 GNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-221 |
6.45e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRnKTVGFVFQfHHLLREFTV 102
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 LENVMMPCLisgldwNVADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPS 171
Cdd:PRK13657 426 EDNIRVGRP------DATDEEMRAAAERAqahdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 172 GNLDSYMSHELHDLLFQLKKDRGLAMIlvTHNRQLAQRADRIMELRDGCL 221
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTTFII--AHRLSTVRNADRILVFDNGRV 547
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-209 |
7.55e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFI------GGDG----------HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVM 65
Cdd:COG4586 1 IIEVENLSKTYRvyekepGLKGalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 66 IDGCQTSKmDSGELAevrnKTVGFVF-QFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLsHRPA-K 143
Cdd:COG4586 81 VLGYVPFK-RRKEFA----RRIGVVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELL-DTPVrQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 144 LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHN----RQLAQR 209
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEALCDR 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-223 |
9.38e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 29 SVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQtSGEVMIDGCQTSKMDSGELAEVR-----NKTVGF---VFQFHHLLREf 100
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTLHQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 tvlenvmmpcliSGLDWNVADERARELLVAVGLEGRLsHRPA-KLSGGEQQRVALA-------RALSNYPLILLADEPSG 172
Cdd:PRK03695 96 ------------DKTRTEAVASALNEVAEALGLDDKL-GRSVnQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 173 NLDSYMSHELHDLLFQLKKdRGLAMILVTH--NRQLaQRADRIMELRDGCLHA 223
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQ-QGIAVVMSSHdlNHTL-RHADRVWLLKQGKLLA 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-175 |
1.38e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelaevRNKTVGFVFQFHHLLREFT 101
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 102 VLENVMMPCLISGldwnvadERAREL----LVAVGLEGRLSHRPAKLSGGEQQRVALARA-LSNYPLILLaDEPSGNLD 175
Cdd:PRK13543 99 TLENLHFLCGLHG-------RRAKQMpgsaLAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLWLL-DEPYANLD 169
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-202 |
2.29e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRF-IGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGG--LDRQTSGEVMIDGCQTSkmdsgela 80
Cdd:COG2401 26 RVAIVLEAFgVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrnktvgfvfqfhhllREFTVLENVmmpclisGLDWNVADerARELLVAVGLEGRLSHR--PAKLSGGEQQRVALARAL 158
Cdd:COG2401 98 -----------------REASLIDAI-------GRKGDFKD--AVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTH 202
Cdd:COG2401 152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-219 |
5.19e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 70.99 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFIGGdghELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRNK 85
Cdd:cd03244 6 KNVSLRYRPN---LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 tVGFVFQFHHLLrEFTVLENvmmpclisgLD----------WNVADE-RARELLVAV--GLEGRLSHRPAKLSGGEQQRV 152
Cdd:cd03244 80 -ISIIPQDPVLF-SGTIRSN---------LDpfgeysdeelWQALERvGLKEFVESLpgGLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 153 ALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-219 |
5.30e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELaevrNKTVGFVFQFHHLLREfT 101
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMmpclisgLDWNVADERARELLVAV-----------GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:PRK10790 431 FLANVT-------LGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVEADTILVLHRG 550
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-221 |
5.49e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLggldrqtSGEVMidgcqtskMDSGELAEVRNKTV------------GFV 90
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVL--------LDDGRIIYEQDLIVarlqqdpprnveGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 91 F---------------QFHHLLR--EFTVLENVM--MPCLISGLD----WNVaDERARELLVAVGLEG--RLShrpaKLS 145
Cdd:PRK11147 84 YdfvaegieeqaeylkRYHDISHlvETDPSEKNLneLAKLQEQLDhhnlWQL-ENRINEVLAQLGLDPdaALS----SLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 146 GGEQQRVALARALSNYPLILLADEPSGNLDSymshELHDLLFQLKKDRGLAMILVTHNRQLAQR-ADRIMELRDGCL 221
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-216 |
5.67e-14 |
|
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: 67.18 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGC-------QTSKMDSGELAEVrnktvgfvfqf 93
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGedllflpQRPYLPLGTLREQ----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 94 hhllreftvlenVMMPclisgldWNvaderarellvavglegrlshrpAKLSGGEQQRVALARALSNYPLILLADEPSGN 173
Cdd:cd03223 84 ------------LIYP-------WD-----------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297171361 174 LDsymsHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:cd03223 122 LD----EESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-219 |
7.55e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTS---KMDSGE 78
Cdd:PRK10762 4 LLQLKGIDKAFPG-----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 79 LAevrnktVGFVFQFHHLLREFTVLENVMM----PCLISGLDWNVADERARELLVAVGLEgRLSHRP-AKLSGGEQQRVA 153
Cdd:PRK10762 79 AG------IGIIHQELNLIPQLTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLR-FSSDKLvGELSIGEQQMVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 154 LARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-213 |
1.00e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 4 EAKNLCKRFigGDgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELaEVR 83
Cdd:NF033858 268 EARGLTMRF--GD---FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDI-ATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 84 nKTVGFVFQFHHLLREFTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPL 163
Cdd:NF033858 339 -RRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 164 ILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRI 213
Cdd:NF033858 418 LLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRI 467
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-213 |
1.12e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.68 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLD----RQTSGEVMIDGCQTSKMDSG 77
Cdd:PRK15093 3 LLDIRNLTIEFKTSDG-WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKTVGFVFQF-HHLLREFTVLENVMM---PCLISGLDW----NVADERARELLVAVGLEGR---LSHRPAKLSG 146
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEpQSCLDPSERVGRQLMqniPGWTYKGRWwqrfGWRKRRAIELLHRVGIKDHkdaMRSFPYELTE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 147 GEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ-LAQRADRI 213
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKI 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-204 |
1.74e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMidgcqtskmdsgeLAEvrNKTVGFVFQFHHLLREFT 101
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------------PAP--GIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPC-----LISGLDW-------------NVADERAR--ELLVAVG---LEGRLS------------HRPAKLSG 146
Cdd:PRK11819 87 VRENVEEGVaevkaALDRFNEiyaayaepdadfdALAAEQGElqEIIDAADawdLDSQLEiamdalrcppwdAKVTKLSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297171361 147 GEQQRVALARALSNYPLILLADEPSGNLD----SYMSHELHDLlfqlkkdRGlAMILVTHNR 204
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDaesvAWLEQFLHDY-------PG-TVVAVTHDR 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-206 |
1.88e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgelaEVRnktVGFVFQFHHLlreft 101
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------KLR---IGYVPQKLYL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 vleNVMMPCLISG---LDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYM 178
Cdd:PRK09544 79 ---DTTLPLTVNRflrLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*...
gi 297171361 179 SHELHDLLFQLKKDRGLAMILVTHNRQL 206
Cdd:PRK09544 156 QVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-221 |
3.43e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtSKMDSGELAEVRnKTVGFVFQFHHLLREftv 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---KPVTAEQPEDYR-KLFSAVFTDFHLFDQ--- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 lenvmmpcLISGLDWNVADERARELLVAVGLEGRLSHRPA-----KLSGGEQQRVALARALSNYPLILLADEPSGNLDSY 177
Cdd:PRK10522 412 --------LLGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 297171361 178 MSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-219 |
4.14e-13 |
|
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: 65.51 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEV 82
Cdd:cd03369 7 IEVENLSVRY---APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNKtVGFVFQfhhllreftvlenvmMPCLISG-LDWNV------ADERARELLvavglegRLSHRPAKLSGGEQQRVALA 155
Cdd:cd03369 81 RSS-LTIIPQ---------------DPTLFSGtIRSNLdpfdeySDEEIYGAL-------RVSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 297171361 156 RALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAG 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-219 |
8.14e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 26 VEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKMDSGELA---------EVRnKTVGFVfQFHhl 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDIRSPRDAiragimlcpEDR-KAEGII-PVH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 lrefTVLENVMMPCLISGLDWNVADERARELLVAVGLEGRL-----SHRPA--KLSGGEQQRVALARALSNYPLILLADE 169
Cdd:PRK11288 347 ----SVADNINISARRHHLRAGCLINNRWEAENADRFIRSLniktpSREQLimNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 170 PSGNLDSYMSHELHDLLFQLKKdRGLAMILVThnRQLAQR---ADRIMELRDG 219
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAA-QGVAVLFVS--SDLPEVlgvADRIVVMREG 472
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-218 |
8.65e-13 |
|
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: 64.57 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGldRQTS----GEVMIDGCQtskmdsg 77
Cdd:cd03232 3 VLTWKNLNYT-VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAgvitGEILINGRP------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 eLAEVRNKTVGFVFQFHHLLREFTVLENVMMPCLISGLdwnvaderarellvavGLEGRlshrpaklsggeqQRVALARA 157
Cdd:cd03232 73 -LDKNFQRSTGYVEQQDVHSPNLTVREALRFSALLRGL----------------SVEQR-------------KRLTIGVE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHnrqlaQRADRIMELRD 218
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIH-----QPSASIFEKFD 177
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-217 |
2.05e-12 |
|
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: 63.78 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 37 AVVGSSGAGKSTLLH-----LLGGLDRQTSGEVMIDGCQTSKMDSGELA---EVRNKTVgfvfqfHHLLREFTVLENVMM 108
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyaLTGELPPNSKGGAHDPKLIREGEVRAQVKlafENANGKK------YTITRSLAILENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 109 pCLISGLDWNVADERARellvavglegrlshrpakLSGGEQQ------RVALARAL-SNYPLILLaDEPSGNLDS-YMSH 180
Cdd:cd03240 100 -CHQGESNWPLLDMRGR------------------CSGGEKVlasliiRLALAETFgSNCGILAL-DEPTTNLDEeNIEE 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 297171361 181 ELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELR 217
Cdd:cd03240 160 SLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
28-204 |
2.52e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 28 ISV--GSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDgcqtskmdsgelaevRNKTVGFVFQFHHLLREFTVLEN 105
Cdd:PRK15064 20 ISVkfGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD---------------PNERLGKLRQDQFAFEEFTVLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 106 VMMpclisGLD--WNVADERAR-----------------------------------ELLVAVGLEGRLSHRP-AKLSGG 147
Cdd:PRK15064 85 VIM-----GHTelWEVKQERDRiyalpemseedgmkvadlevkfaemdgytaearagELLLGVGIPEEQHYGLmSEVAPG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 148 EQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLfqlkKDRGLAMILVTHNR 204
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHDR 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-219 |
3.74e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVmidgcqtskmdsgELAEv 82
Cdd:PRK15064 320 LEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSE- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rNKTVGFVFQFHHllREFTVLENVMmpclisglDW--NVADERARELLVAvGLEGRL------SHRPAK-LSGGEQQRVA 153
Cdd:PRK15064 381 -NANIGYYAQDHA--YDFENDLTLF--------DWmsQWRQEGDDEQAVR-GTLGRLlfsqddIKKSVKvLSGGEKGRML 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 154 LARALSNYPLILLADEPSGNLDsyM-SHElhDLLFQLKKDRGlAMILVTHNRQLAQR-ADRIMELRDG 219
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMD--MeSIE--SLNMALEKYEG-TLIFVSHDREFVSSlATRIIEITPD 511
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
6.22e-12 |
|
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: 64.58 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRqTSGEVMIDGcqtskmdsgelaevrnkTVGFVFQfHHLLREFT 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKG-----------------SVAYVPQ-QAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLISgldwnvaDERARELLVAVGLEGRLSHRPA-----------KLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:TIGR00957 715 LRENILFGKALN-------EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 171 SGNLDSYMS-HELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:TIGR00957 788 LSAVDAHVGkHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-213 |
6.29e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 63.77 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGDGhELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRQ---TSGEVMIDGCQTSKMDSG 77
Cdd:COG4170 3 LLDIRNLTIEIDTPQG-RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNwhvTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 78 ELAEVRNKTVGFVFQ--FHHL---LREFTVLENVMMPCLISGLDWNVAD---ERARELLVAVGLEgrlSHR------PAK 143
Cdd:COG4170 82 ERRKIIGREIAMIFQepSSCLdpsAKIGDQLIEAIPSWTFKGKWWQRFKwrkKRAIELLHRVGIK---DHKdimnsyPHE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 144 LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILVTHNRQ-LAQRADRI 213
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsISQWADTI 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-227 |
7.06e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 24 KEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGE-LAEvrnktvGFVF-----QFHHLL 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLAR------GLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 98 reftvlenvmmpcLISGLDWNVAD----------ERARELLV------AVGLegRLSH--RPAK-LSGGEQQRVALARAL 158
Cdd:PRK15439 354 -------------LDAPLAWNVCAlthnrrgfwiKPARENAVleryrrALNI--KFNHaeQAARtLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 159 SNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHN-RQLAQRADRIMELRDGCL------HAINKD 227
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDlEEIEQMADRVLVMHQGEIsgaltgAAINVD 493
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-223 |
8.80e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.69 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 25 EVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRQTSGEVMIDGCQTSKMDSGELAEVRNKTVGFVFQFHHLLREFTVL 103
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 104 ENVMMPCLISGLDWNVADERARELLVAVGLEgRLSHRPA-------KLSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIGSAIQ-RLKVKTAspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 177 YMSHELHDLLFQLKKdRGLAMILVThnRQLAQ---RADRIMELRDGCLHA 223
Cdd:TIGR02633 437 GAKYEIYKLINQLAQ-EGVAIIVVS--SELAEvlgLSDRVLVIGEGKLKG 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-219 |
1.04e-11 |
|
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: 62.95 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgelaevrnkTVGFVFQFHHLLrEFT 101
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIM-PGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVmmpclISGLDWNvaDERARELLVAVGLEGRLSHRPAK-----------LSGGEQQRVALARALSNYPLILLADEP 170
Cdd:cd03291 114 IKENI-----IFGVSYD--EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 297171361 171 SGNLDSYMSHELHD-LLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:cd03291 187 FGYLDVFTEKEIFEsCVCKLMANK--TRILVTSKMEHLKKADKILILHEG 234
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-175 |
1.13e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 36 VAVVGSSGAGKSTLLHLLGGLDRQTSGEVMidgcqtskmdsgELAEVRNKtvgfVFQFHHL----LREFTVLenVMMPCL 111
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF------------RSAKVRMA----VFSQHHVdgldLSSNPLL--YMMRCF 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297171361 112 ISgldwnVADERARELLVAVGLEGRLSHRPA-KLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:PLN03073 600 PG-----VPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-176 |
1.54e-11 |
|
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: 62.04 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 27 EISVGS---GEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgELAEVRNKTVGFVFQFhhlLREFTvl 103
Cdd:cd03237 16 EVEGGSiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY----KPQYIKADYEGTVRDL---LSSIT-- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 104 envmmPCLISGLDWNVaderarELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:cd03237 87 -----KDFYTHPYFKT------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-219 |
2.24e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCkrfigGDGheltvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSK------MDS 76
Cdd:PRK10762 258 LKVDNLS-----GPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdgLAN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 G--ELAEVRnKTVGFVFqfhhllrEFTVLENVMMPCL----ISGLDWNVADERArellvAVGLEGRL--------SHRPA 142
Cdd:PRK10762 328 GivYISEDR-KRDGLVL-------GMSVKENMSLTALryfsRAGGSLKHADEQQ-----AVSDFIRLfniktpsmEQAIG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 143 KLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNR-QLAQRADRIMELRDG 219
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMpEVLGMSDRILVMHEG 471
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-219 |
2.33e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVmidgcqtskmdsgeLAEvrnKTVGFVFQFHHLLREfT 101
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAE---RSIAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMpclisgldwnVADERARELLVAV--------------GLEGRLSHRPAKLSGGEQQRVALARAL-SNYPLILL 166
Cdd:PTZ00243 737 VRGNILF----------FDEEDAARLADAVrvsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVyANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 167 aDEPSGNLDSYMSHELHDLLFqLKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PTZ00243 807 -DDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-219 |
3.16e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.62 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgelaevrnkTVGFVFQFHHLLrEFT 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------------RISFSPQTSWIM-PGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVmmpclISGLDWnvaDE-RARELLVAVGLEGRLSHRPAK-----------LSGGEQQRVALARALSNYPLILLADE 169
Cdd:TIGR01271 503 IKDNI-----IFGLSY---DEyRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 170 PSGNLDSYMSHELHD-LLFQLKKDRglAMILVTHNRQLAQRADRIMELRDG 219
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEsCLCKLMSNK--TRILVTSKLEHLKKADKILLLHEG 623
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-175 |
3.21e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFigGDGHELtVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgelaev 82
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG------- 1354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 rnktvgfvfqFHHLLREFTVLENvmMPCLISG-LDWNV------ADERARELLVAVGLEGRLSHRPAK-----------L 144
Cdd:TIGR00957 1355 ----------LHDLRFKITIIPQ--DPVLFSGsLRMNLdpfsqySDEEVWWALELAHLKTFVSALPDKldhecaeggenL 1422
|
170 180 190
....*....|....*....|....*....|.
gi 297171361 145 SGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-175 |
3.88e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 62.24 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLdRQTSGEVMIDGCQtskMDSGELAEVRnKTVGF----VFQFHHL 96
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVS---WNSVTLQTWR-KAFGVipqkVFIFSGT 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREftvlenvmmpclisGLD----------WNVADErarellvaVGLEGRLSHRPAK-----------LSGGEQQRVALA 155
Cdd:TIGR01271 1308 FRK--------------NLDpyeqwsdeeiWKVAEE--------VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|
gi 297171361 156 RALSNYPLILLADEPSGNLD 175
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-175 |
6.40e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdGHELtVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdgcqtskmdsGElae 81
Cdd:TIGR03719 322 VIEAENLTKAF----GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI----------GE--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrnkTV--GFVFQFH-HLLREFTVLEnvmmpcLISG----LDWNVADERARELLVAVGLEGRLSHRPAK-LSGGEQQRVA 153
Cdd:TIGR03719 384 ----TVklAYVDQSRdALDPNKTVWE------EISGgldiIKLGKREIPSRAYVGRFNFKGSDQQKKVGqLSGGERNRVH 453
|
170 180
....*....|....*....|..
gi 297171361 154 LARALSNYPLILLADEPSGNLD 175
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD 475
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-175 |
8.06e-11 |
|
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: 60.25 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFIGGdGHelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLdRQTSGEVMIDGCQTSKMdsgELAEV 82
Cdd:cd03289 3 MTVKDLTAKYTEG-GN--AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSV---PLQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RnKTVGF----VFQFHHLLREftvlenvmmpclisGLD----------WNVADErarellvaVGLEGRLSHRPAK----- 143
Cdd:cd03289 76 R-KAFGVipqkVFIFSGTFRK--------------NLDpygkwsdeeiWKVAEE--------VGLKSVIEQFPGQldfvl 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 297171361 144 ------LSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:cd03289 133 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-219 |
8.08e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 6 KNLCKRFIGgdgheLTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEvrnK 85
Cdd:PRK10982 2 SNISKSFPG-----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE---N 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 86 TVGFVFQFHHLLREFTVLENVMM---PCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYP 162
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 297171361 163 LILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN-RQLAQRADRIMELRDG 219
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDG 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-219 |
1.26e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRQTSGEVMIDGcqtskmdsgelaevrnkTVGFVFQFHHLLREfT 101
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------------SVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMpclisGLDWNvaDERARELLVAVGLE-------GR----LSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:PLN03232 695 VRENILF-----GSDFE--SERYWRAIDVTALQhdldllpGRdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 297171361 171 SGNLDSYMSHELHDLLFQlKKDRGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-222 |
2.55e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 8 LCKRFIGGDG---------HELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTS--GEVMIDGcqtskmds 76
Cdd:PLN03211 60 NIKRILGHKPkisdetrqiQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN-------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GELAEVRNKTVGFVFQFHHLLREFTVLENVMMPCLI---SGLDWNVADERARELLVAVGLE-------GRLSHRpaKLSG 146
Cdd:PLN03211 132 RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSLTKQEKILVAESVISELGLTkcentiiGNSFIR--GISG 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 147 GEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILVTH--NRQLAQRADRIMELRDG-CLH 222
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHqpSSRVYQMFDSVLVLSEGrCLF 287
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-175 |
4.20e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDsgeLAEVRnKTVGFVFQfhhllreft 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQ--------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 vlenvmMPCLISG-----LD----WNVAD-----ERARELLV----AVGLEGRLSHRPAKLSGGEQQRVALARALSNYPL 163
Cdd:PLN03130 1321 ------APVLFSGtvrfnLDpfneHNDADlweslERAHLKDVirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170
....*....|..
gi 297171361 164 ILLADEPSGNLD 175
Cdd:PLN03130 1395 ILVLDEATAAVD 1406
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-219 |
1.60e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgelaevrnktvgfvFQFHHLLREFT 101
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-----------------FGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENvmMPCLISGL---------DWNVAD-----ERARELLV----AVGLEGRLSHRPAKLSGGEQQRVALARALSNYPL 163
Cdd:PLN03232 1314 IIPQ--SPVLFSGTvrfnidpfsEHNDADlwealERAHIKDVidrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 164 ILLADEPSGNLDSYMshelhDLLFQ--LKKD-RGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PLN03232 1392 ILVLDEATASVDVRT-----DSLIQrtIREEfKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-219 |
2.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 26 VEISVGSgeAVAVVGSSGAGKSTLLH-LLGGLDRQTSGEVMIDGcqtskmdsgelaevrnkTVGFVFQFHHLLREfTVLE 104
Cdd:PLN03130 638 LDVPVGS--LVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------------TVAYVPQVSWIFNA-TVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 105 NVMMpclisGLDWNVAD-ERA-------REL-LVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:PLN03130 698 NILF-----GSPFDPERyERAidvtalqHDLdLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297171361 176 SYMSHELHDLLfqLKKD-RGLAMILVTHNRQLAQRADRIMELRDG 219
Cdd:PLN03130 773 AHVGRQVFDKC--IKDElRGKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-224 |
2.35e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIGGdgheltvLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQ---TSKMDS-- 76
Cdd:PRK09700 265 VFEVRNVTSRDRKK-------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDispRSPLDAvk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 ---GELAEVRNKTvGFvfqFHHllreFTVLENVMMPCLI--SGLD--WNVADERaRELLVAVGLEGRLSHRPA------- 142
Cdd:PRK09700 338 kgmAYITESRRDN-GF---FPN----FSIAQNMAISRSLkdGGYKgaMGLFHEV-DEQRTAENQRELLALKCHsvnqnit 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 143 KLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSElPEIITVCDRIAVFCEGRL 487
|
...
gi 297171361 222 HAI 224
Cdd:PRK09700 488 TQI 490
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
40-202 |
2.45e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 40 GSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgelaeVRNKTVGFVFQFHHLLREFTVLENVMMpclisgldWNV 119
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN--------IAKPYCTYIGHNLGLKLEMTVFENLKF--------WSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 120 ADERARELLVAV---GLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLdsymSHELHDLLFQL---KKDR 193
Cdd:PRK13541 97 IYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL----SKENRDLLNNLivmKANS 172
|
....*....
gi 297171361 194 GLAMILVTH 202
Cdd:PRK13541 173 GGIVLLSSH 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-200 |
3.10e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFIggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLH-LLGGLDRQTSGEVMIDG-------CQTSk 73
Cdd:PRK13549 259 ILEVRNLTAWDP--VNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGkpvkirnPQQA- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 74 MDSG--ELAEVRNKtvgfvfqfHHLLREFTVLENVMMPCLISGLDWNVADErARELLVAVGLEGRLSHRPA-------KL 144
Cdd:PRK13549 336 IAQGiaMVPEDRKR--------DGIVPVMGVGKNITLAALDRFTGGSRIDD-AAELKTILESIQRLKVKTAspelaiaRL 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 145 SGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdRGLAMILV 200
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVI 461
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-206 |
3.35e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 19 ELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGldrqtsgevmidgcqTSKMDSGELAEVRNKTVGFVFQfHHLlr 98
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG---------------ELAPVSGEIGLAKGIKLGYFAQ-HQL-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 99 EFTVLENVMMPCLiSGLDWNVADERARELLVAVGLEG-RLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSY 177
Cdd:PRK10636 386 EFLRADESPLQHL-ARLAPQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|....*....
gi 297171361 178 MSHELHDLLFQLKKdrglAMILVTHNRQL 206
Cdd:PRK10636 465 MRQALTEALIDFEG----ALVVVSHDRHL 489
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-219 |
3.86e-09 |
|
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: 54.46 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLD--RQTSGEVMIDGCQTSKMDSGELAevrNKTVGFVFQfhhllre 99
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 100 ftvlenvmMPCLISGLdwnvadeRARELLVAVGlEGrlshrpakLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMS 179
Cdd:cd03217 85 --------YPPEIPGV-------KNADFLRYVN-EG--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 297171361 180 HELHDLLFQLkKDRGLAMILVTHNRQLAQ--RADRIMELRDG 219
Cdd:cd03217 141 RLVAEVINKL-REEGKSVLIITHYQRLLDyiKPDRVHVLYDG 181
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-175 |
6.89e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 54.63 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAeVRNKtVGFVFQFHHLLREFT 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA-LRQQ-VATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 102 VLENVMMpclISGLDWNVADE----RARELLVAVGLEgRLSHRPAK-LSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:PRK13638 94 DIDSDIA---FSLRNLGVPEAeitrRVDEALTLVDAQ-HFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-211 |
8.87e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 16 DGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcQTSKMDSGelaeVRNKTVGFVFQFHH 95
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER-QSIKKDLC----TYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 96 LLREFTVLENVMMPCLISGLDWNVAderarELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVGIT-----ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 297171361 176 SyMSHELHDLLFQLKKDRGLAMILVTHNRQLAQRAD 211
Cdd:PRK13540 160 E-LSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-205 |
1.49e-08 |
|
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: 54.63 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 28 ISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtsKMDSGELAEVrNKTVGFVFQFHHLLREFTVLENVM 107
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG----KSILTNISDV-HQNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 108 MPCLISGLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLF 187
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170
....*....|....*...
gi 297171361 188 QLKKDrGLAMILVTHNRQ 205
Cdd:TIGR01257 2115 SIIRE-GRAVVLTSHSME 2131
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-216 |
1.91e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLhlLGGLdrQTSGEVMIDGcQTSKMDsgelaevRNKTVgFVFQFhhllreftv 102
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGL--YASGKARLIS-FLPKFS-------RNKLI-FIDQL--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 lenvmmpclisgldwnvaderarELLVAVGLEG-RLSHRPAKLSGGEQQRVALARAL--SNYPLILLADEPSGNLDsymS 179
Cdd:cd03238 69 -----------------------QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLH---Q 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 297171361 180 HELHDLLFQLKK--DRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:cd03238 123 QDINQLLEVIKGliDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-219 |
1.97e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.06 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 142 AKLSGGEQQRVALAR----ALSNYPLILlaDEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMELR 217
Cdd:PRK00635 475 ATLSGGEQERTALAKhlgaELIGITYIL--DEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRIIDIG 551
|
..
gi 297171361 218 DG 219
Cdd:PRK00635 552 PG 553
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-214 |
2.36e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLL------------------------------------------------ 53
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 54 --GGLDRQT----SGEVMIDG---CQTSKMDSGEL-AEVRNKTVGF---VFQFHHLLREFTVLENVMMPCLISGLDwNVA 120
Cdd:PTZ00265 1263 egGSGEDSTvfknSGKILLDGvdiCDYNLKDLRNLfSIVSQEPMLFnmsIYENIKFGKEDATREDVKRACKFAAID-EFI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 121 DERARELLVAVGLEGRlshrpaKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRGLAMILV 200
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGK------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
250
....*....|....
gi 297171361 201 THNRQLAQRADRIM 214
Cdd:PTZ00265 1416 AHRIASIKRSDKIV 1429
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
2.98e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRFiggdGHELtVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIdgcqtskmdsGElae 81
Cdd:PRK11819 324 VIEAENLSKSF----GDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----------GE--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 82 vrnkTV--GFVFQFH-HLLREFTVLENvmmpclIS-GLDW-NVADER--ARELLVAVGLEGRLSHRPAK-LSGGEQQRVA 153
Cdd:PRK11819 386 ----TVklAYVDQSRdALDPNKTVWEE------ISgGLDIiKVGNREipSRAYVGRFNFKGGDQQKKVGvLSGGERNRLH 455
|
170 180
....*....|....*....|....*
gi 297171361 154 LARAL---SNypLILLaDEPSGNLD 175
Cdd:PRK11819 456 LAKTLkqgGN--VLLL-DEPTNDLD 477
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-216 |
3.25e-08 |
|
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: 52.26 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 126 ELLVAVGLEG-RLSHRPAKLSGGEQQRVALARALSN--YPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTH 202
Cdd:cd03270 119 GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEH 197
|
90
....*....|....
gi 297171361 203 NRQLAQRADRIMEL 216
Cdd:cd03270 198 DEDTIRAADHVIDI 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-175 |
4.41e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 30 VGSGEAVAVVGSSGAGKSTLLHLLGGLDRQT-SGEVMIDGCQTSkmdSGELAEVRNKTVGFVF-QFHHLLREFTVLENVm 107
Cdd:PRK10938 283 VNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRRRG---SGETIWDIKKHIGYVSsSLHLDYRVSTSVRNV- 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 108 mpcLISG------LDWNVADER---ARELLVAVGLEGRLSHRP-AKLSGGeQQRVAL-ARALSNYPLILLADEPSGNLD 175
Cdd:PRK10938 359 ---ILSGffdsigIYQAVSDRQqklAQQWLDILGIDKRTADAPfHSLSWG-QQRLALiVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-217 |
4.83e-08 |
|
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: 50.82 E-value: 4.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 17 GHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLhllggldRQTSgevmidgcqtskmdsgelaevrnktVGFVFQFHHL 96
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTIL-------DAIG-------------------------LALGGAQSAT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREFTVLENVmmpclisgldwNVADERArELLVAVGlegrlshrpaKLSGGEQQRVALARALSN-----YPLILLaDEPS 171
Cdd:cd03227 53 RRRSGVKAGC-----------IVAAVSA-ELIFTRL----------QLSGGEKELSALALILALaslkpRPLYIL-DEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 297171361 172 GNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMELR 217
Cdd:cd03227 110 RGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-218 |
5.57e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 11 RFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGL---DRQTSGEVMIDGcqtskMDSGELAEVRNKTV 87
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNG-----IPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 88 GFVFQFHHLLREFTVlenvmmpclisgldwnvaderaRELL-VAVGLEGRLSHRpaKLSGGEQQRVALARALSNYPLILL 166
Cdd:cd03233 86 IYVSEEDVHFPTLTV----------------------RETLdFALRCKGNEFVR--GISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 297171361 167 ADEPSGNLDSYMSHELhdllfqLKKDRGLAMIL-VTHNRQLAQRADRIMELRD 218
Cdd:cd03233 142 WDNSTRGLDSSTALEI------LKCIRTMADVLkTTTFVSLYQASDEIYDLFD 188
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-218 |
1.15e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLckRFIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDgcqtskmDSGELAEV 82
Cdd:PTZ00265 383 IQFKNV--RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN-------DSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 83 RNK----TVGFVFQFHHL---------------LREFTVLE----------------------------NVMMPCLIS-G 114
Cdd:PTZ00265 454 NLKwwrsKIGVVSQDPLLfsnsiknnikyslysLKDLEALSnyynedgndsqenknkrnscrakcagdlNDMSNTTDSnE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 115 L-----------DWNVADERARELL------VAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSY 177
Cdd:PTZ00265 534 LiemrknyqtikDSEVVDVSKKVLIhdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 297171361 178 MSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADRIMELRD 218
Cdd:PTZ00265 614 SEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-205 |
2.03e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 1 MILEAKNLCKRfIGGDghelTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMidgCQTsKMDsgela 80
Cdd:PRK11147 318 IVFEMENVNYQ-IDGK----QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH---CGT-KLE----- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 evrnktVGFVFQFHHLLR-EFTVLENVmmpclisgldwnvADERaRELLVavglEGRLSH----------------RPAK 143
Cdd:PRK11147 384 ------VAYFDQHRAELDpEKTVMDNL-------------AEGK-QEVMV----NGRPRHvlgylqdflfhpkramTPVK 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 144 -LSGGEQQRVALARAL---SNypLILLaDEPSGNLDSymshELHDLLFQLKKDRGLAMILVTHNRQ 205
Cdd:PRK11147 440 aLSGGERNRLLLARLFlkpSN--LLIL-DEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQ 498
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
3.31e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.14 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 32 SGEAVAVVGSSGAGKSTLLHLLGG-LDRQTSGEVMIDGcqtskmdsgelaevrnktvgfvfqfhhllreftvlenvmmpc 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 111 lisgldwnvadERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHEL-----HDL 185
Cdd:smart00382 39 -----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 297171361 186 LFQLKKDRGLAMILVTHNRQ------LAQRADRIMELRDG 219
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKdlgpalLRRRFDRRIVLLLI 147
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
144-219 |
4.50e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 4.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 144 LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQL-KKDRGLAMIlVTHNRQLAQRADRIMELRDG 219
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIII-SSEMPELLGITDRILVMSNG 467
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-170 |
4.94e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 21 TVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsGELAEVRNKT-----VGFVFQF-- 93
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG--------GDMADARHRRavcprIAYMPQGlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 94 HHLLREFTVLENV-MMPCLIsGLDwnvADERAR---ELLVAVGLEgRLSHRPA-KLSGGEQQRVALARALSNYP--LILl 166
Cdd:NF033858 87 KNLYPTLSVFENLdFFGRLF-GQD---AAERRRridELLRATGLA-PFADRPAgKLSGGMKQKLGLCCALIHDPdlLIL- 160
|
....
gi 297171361 167 aDEP 170
Cdd:NF033858 161 -DEP 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
15-216 |
5.61e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 49.63 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 15 GDGHELTV-------LKEVEISVGSGEAVAVVGSSGAGKSTLLH--LLGGLDRQTSGEVMIDGCQTS-----KMD----- 75
Cdd:TIGR00630 609 GNGKFLTLkgarennLKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPGRYTSiegleHLDkvihi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 76 ----------------SGELAEVRN--------KTVGFV---FQFH-------------HLLREFTVLENVMMPC-LISG 114
Cdd:TIGR00630 689 dqspigrtprsnpatyTGVFDEIRElfaetpeaKVRGYTpgrFSFNvkggrceacqgdgVIKIEMHFLPDVYVPCeVCKG 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 115 LDWN------------VAD------ERARE-------------LLVAVGLEG-RLSHRPAKLSGGEQQRVALARALS--- 159
Cdd:TIGR00630 769 KRYNretlevkykgknIADvldmtvEEAYEffeavpsisrklqTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSkrs 848
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 297171361 160 NYPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:TIGR00630 849 TGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLDVIKTADYIIDL 904
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-176 |
7.50e-07 |
|
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: 49.01 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 33 GEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVmidgcqtskmdSGELA------EVRNKTVGFVFQFhhllreftvLENV 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKisykpqYISPDYDGTVEEF---------LRSA 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297171361 107 MMPCLISGLDWNvaderarELLVAVGLEgRLSHRPAK-LSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:COG1245 426 NTDDFGSSYYKT-------EIIKPLGLE-KLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-202 |
8.23e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 33 GEAVAVVGSSGAGKSTLLHLLggldrqtSGEVMIDGCQTSKMDSGE--------------LAEVRNKTVGFVF--QFHHL 96
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------SGELIPNLGDYEEEPSWDevlkrfrgtelqnyFKKLYNGEIKVVHkpQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREF---TV---LENVmmpclisgldwnvaDER--ARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLAD 168
Cdd:PRK13409 172 IPKVfkgKVrelLKKV--------------DERgkLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....
gi 297171361 169 EPSGNLDSYMSHELHDLLFQLKKDRglAMILVTH 202
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGK--YVLVVEH 269
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-209 |
1.00e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 3 LEAKNLCKRFiggdgHELTVLKEVEISVGSGEAVAVVGSSGAG--KSTLLHLLGGLDRQTSGEVMIDGCQTSKmdsgela 80
Cdd:NF000106 14 VEVRGLVKHF-----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 81 eVRNKTVGFVFQFHHLLRE-FTVLENVMMpcLISGLDWNVADERAR--ELLVAVGLEGRLSHRPAKLSGGEQQRVALARA 157
Cdd:NF000106 82 -ALRRTIG*HRPVR*GRREsFSGRENLYM--IGR*LDLSRKDARARadELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 297171361 158 LSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDrGLAMILVTHNRQLAQR 209
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQ 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-175 |
1.05e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 33 GEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdsgELA----EVRNKTVGFVFQFhhlLREFTvlenvmm 108
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL---------KISykpqYIKPDYDGTVEDL---LRSIT------- 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 109 pcliSGLD---WNVaderarELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLD 175
Cdd:PRK13409 426 ----DDLGssyYKS------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-206 |
1.67e-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: 48.21 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLdrqtsgevmidgcqtSKMDSGELAEVRNKTVGFVFQFHHLLREfT 101
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL---------------WPVYGGRLTKPAKGKLFYVPQRPYMTLG-T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 102 VLENVMMPCLISGL-DWNVADERARELLVAVGLEGRLSHRPA---------KLSGGEQQRVALARALSNYPLILLADEPS 171
Cdd:TIGR00954 531 LRDQIIYPDSSEDMkRRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*
gi 297171361 172 gnldSYMSHELHDLLFQLKKDRGLAMILVTHNRQL 206
Cdd:TIGR00954 611 ----SAVSVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-204 |
1.68e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISvgSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMDSGELAEV------RNKTvgfvfqfhHL 96
Cdd:PRK10938 21 LPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLvsdewqRNNT--------DM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LRE------FTVLENVmmpclisgLDWNVADERARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEP 170
Cdd:PRK10938 91 LSPgeddtgRTTAEII--------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190
....*....|....*....|....*....|....
gi 297171361 171 SGNLDSYMSHELHDLLFQLKKdRGLAMILVThNR 204
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQ-SGITLVLVL-NR 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-177 |
1.74e-06 |
|
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: 48.24 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 32 SGEAVAVVGSSGAGKSTLLHLLGG--------LDRQTSGEVMIDGCQTSKMDSgELAEVRNKTVGFVF--QFHHLLREF- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGelkpnlgdYDEEPSWDEVLKRFRGTELQD-YFKKLANGEIKVAHkpQYVDLIPKVf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 101 --TVLEnvmmpcLISGldwnvADER--ARELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:COG1245 177 kgTVRE------LLEK-----VDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
.
gi 297171361 177 Y 177
Cdd:COG1245 246 Y 246
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-216 |
2.09e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 126 ELLVAVGLEGRLSHRP-AKLSGGEQQRVALARALSN---YPLILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVT 201
Cdd:PRK00635 791 HALCSLGLDYLPLGRPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIE 869
|
90
....*....|....*
gi 297171361 202 HNRQLAQRADRIMEL 216
Cdd:PRK00635 870 HNMHVVKVADYVLEL 884
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
115-205 |
2.81e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 115 LDWNVADERARELLVAVGLEGRLSHRPAK-LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKdr 193
Cdd:PLN03073 315 IDAYTAEARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK-- 392
|
90
....*....|..
gi 297171361 194 glAMILVTHNRQ 205
Cdd:PLN03073 393 --TFIVVSHARE 402
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-169 |
5.57e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 15 GDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGcqtskmdSGELAEVRNKTVGfvfqfh 94
Cdd:PRK13545 32 KDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISSGLNG------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 95 hllrEFTVLENVMMPCLISGLdwnvADERARELLVAVgLE----GRLSHRPAK-LSGGEQQRVALARALSNYPLILLADE 169
Cdd:PRK13545 99 ----QLTGIENIELKGLMMGL----TKEKIKEIIPEI-IEfadiGKFIYQPVKtYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
16-64 |
1.16e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 45.31 E-value: 1.16e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 297171361 16 DGHELTVLKEVeisVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEV 64
Cdd:PRK01889 181 DGEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-219 |
1.45e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 45.47 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 17 GHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgELAEVRNKtVGFVFQFHHL 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 97 LREfTVLENVMMPCLISGLDW--------NVADERARellVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLAD 168
Cdd:PRK10789 401 FSD-TVANNIALGRPDATQQEiehvarlaSVHDDILR---LPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297171361 169 EPSGNLDSYMSHELHDLLFQLKKDRGLamILVTHNRQLAQRADRIMELRDG 219
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRLSALTEASEILVMQHG 525
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-221 |
1.59e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.51 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 7 NLCKRFiggDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMIDGCQTSKMdsgelaevrnkt 86
Cdd:cd03288 24 DLCVRY---ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 87 vgfvfQFHHLLREFTVLenVMMPCLISG-LDWNV------ADERARELLVAVGLEGRLSHRPAKL-----------SGGE 148
Cdd:cd03288 89 -----PLHTLRSRLSII--LQDPILFSGsIRFNLdpeckcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297171361 149 QQRVALARALSNYPLILLADEPSGNLDSYMSHELHDLLFQLKKDRglAMILVTHNRQLAQRADRIMELRDGCL 221
Cdd:cd03288 162 RQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-216 |
2.00e-05 |
|
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: 45.00 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 128 LVAVGLEG-RLSHRPAKLSGGEQQRVALAR----ALSNYPLILlaDEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTH 202
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEH 548
|
90
....*....|....
gi 297171361 203 NRQLAQRADRIMEL 216
Cdd:TIGR00630 549 DEDTIRAADYVIDI 562
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-216 |
2.79e-05 |
|
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: 43.76 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 126 ELLVAVGLEG-RLSHRPAKLSGGEQQRVALARALSNY---PLILLADEPSGNLDsymSHELHDLLFQLKK--DRGLAMIL 199
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLH---FHDVKKLLEVLQRlvDKGNTVVV 227
|
90
....*....|....*..
gi 297171361 200 VTHNRQLAQRADRIMEL 216
Cdd:cd03271 228 IEHNLDVIKCADWIIDL 244
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
32-64 |
4.43e-05 |
|
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: 42.77 E-value: 4.43e-05
10 20 30
....*....|....*....|....*....|....
gi 297171361 32 SGEAVAVVGSSGAGKSTLL-HLLGGLDRQTsGEV 64
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLnALLPELVLAT-GEI 116
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-203 |
5.07e-05 |
|
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: 43.12 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 32 SGEAVAVVGSSGAGKSTLLHLLggldrqtSGEVMIDGCQTSkmDSGELAEVRNKTVGFVFQFHhllreFTVLENVMMPCL 111
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKLKPNLGKFD--DPPDWDEILDEFRGSELQNY-----FTKLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 112 IS---------------GLDWNVADERAR--ELLVAVGLEGRLSHRPAKLSGGEQQRVALARALSNYPLILLADEPSGNL 174
Cdd:cd03236 91 VKpqyvdlipkavkgkvGELLKKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*....
gi 297171361 175 DSYMSHELHDLLFQLKKDrGLAMILVTHN 203
Cdd:cd03236 171 DIKQRLNAARLIRELAED-DNYVLVVEHD 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-219 |
7.72e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLCKRfIGGDGHELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGldRQ-----TSGEVMIDGcqtskmds 76
Cdd:TIGR00956 759 IFHWRNLTYE-VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVttgviTGGDRLVNG-------- 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 77 GELAEVRNKTVGFVFQFHHLLREFTVLENVM------MPCLISGLDWNVADERARELL-------VAVGLEGrlshrpAK 143
Cdd:TIGR00956 828 RPLDSSFQRSIGYVQQQDLHLPTSTVRESLRfsaylrQPKSVSKSEKMEYVEEVIKLLemesyadAVVGVPG------EG 901
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 144 LSGGEQQRVALARALSNYP-LILLADEPSGNLDSYMSHELHDLLFQLkKDRGLAMILVTHNRQ--LAQRADRIMELRDG 219
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-221 |
1.42e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 23 LKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLDRQTSGEVMidgcqtskmdsgelaevRNKTVGFVFQFHHLLREFTV 102
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 103 LENVMMPCLISGLDWNVADERARELLVAVGLeGRLSHRPAK-LSGGEQQRVALARALSNYPLILLADEPSGNLDSYMSHE 181
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSEL-GEFIYQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 182 LHDLLFQLkKDRGLAMILVTHN-RQLAQRADRIMELRDGCL 221
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNlGQVRQFCTKIAWIEGGKL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-170 |
1.43e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 22 VLKEVEISVGSGEAVAVVGSSGAGKSTL-LHLLG---GldRQTSGEVMIDG--CQTSK----MDSGeLA---EVRnKTVG 88
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsyG--RNISGTVFKDGkeVDVSTvsdaIDAG-LAyvtEDR-KGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 89 FVfqfhhlLREfTVLENVMMPCLISGLDWNVADERaRELLVAVGLEGRLSHRP-------AKLSGGEQQRVALARALSNY 161
Cdd:NF040905 351 LN------LID-DIKRNITLANLGKVSRRGVIDEN-EEIKVAEEYRKKMNIKTpsvfqkvGNLSGGNQQKVVLSKWLFTD 422
|
....*....
gi 297171361 162 PLILLADEP 170
Cdd:NF040905 423 PDVLILDEP 431
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-176 |
1.59e-04 |
|
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: 41.02 E-value: 1.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 297171361 136 RLSHRPAK--LSGGEQQRVALARALSNYPLILLADEPSGNLDS 176
Cdd:cd03222 62 TPVYKPQYidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
123-216 |
1.71e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 123 RAR-ELLVAVGLeGRLS-HRPAK-LSGGEQQRVALARAL-SN-----YplILlaDEPS-GnldsymsheLH--D---LLF 187
Cdd:COG0178 463 RSRlGFLVDVGL-DYLTlDRSAGtLSGGEAQRIRLATQIgSGlvgvlY--VL--DEPSiG---------LHqrDndrLIE 528
|
90 100 110
....*....|....*....|....*....|.
gi 297171361 188 QLKK--DRGLAMILVTHNRQLAQRADRIMEL 216
Cdd:COG0178 529 TLKRlrDLGNTVIVVEHDEDTIRAADYIIDI 559
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
37-215 |
2.29e-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: 40.72 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 37 AVVGSSGAGKSTLLH-----LLGgldrQTSGEvmidgcQTSKMDSGELAEVRNKT-VGFVFQFHHLL----REFtvlenv 106
Cdd:cd03279 32 LICGPTGAGKSTILDaityaLYG----KTPRY------GRQENLRSVFAPGEDTAeVSFTFQLGGKKyrveRSR------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 107 mmpclisGLDwnvADERARELLVAVGLEGRLSHRPAK-LSGGEQQRVALARALS---------NYPL-ILLADEPSGNLD 175
Cdd:cd03279 96 -------GLD---YDQFTRIVLLPQGEFDRFLARPVStLSGGETFLASLSLALAlsevlqnrgGARLeALFIDEGFGTLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 297171361 176 SYMSHELHDLLFQLKKDRglAMILV-THNRQLAQRADRIME 215
Cdd:cd03279 166 PEALEAVATALELIRTEN--RMVGViSHVEELKERIPQRLE 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-206 |
3.46e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 2 ILEAKNLcKRFIGgdghELTVLKEVEISVGSGEAVAVVGSSGAGKSTLLHLLGGLD--RQTSGEVMIDGCQTSKMDsgel 79
Cdd:CHL00131 7 ILEIKNL-HASVN----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLE---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 80 AEVRNKTVGFV-FQFhhllreftvlenvmmPCLISGLdwNVAD------------------------ERARELLVAVGLE 134
Cdd:CHL00131 78 PEERAHLGIFLaFQY---------------PIEIPGV--SNADflrlaynskrkfqglpeldpleflEIINEKLKLVGMD 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297171361 135 GRLSHRPAK--LSGGEQQRVA-LARALSNYPLILLaDEPSGNLD----SYMSHELHDLlfqlkKDRGLAMILVTHNRQL 206
Cdd:CHL00131 141 PSFLSRNVNegFSGGEKKRNEiLQMALLDSELAIL-DETDSGLDidalKIIAEGINKL-----MTSENSIILITHYQRL 213
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
32-64 |
4.82e-04 |
|
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: 39.45 E-value: 4.82e-04
10 20 30
....*....|....*....|....*....|....
gi 297171361 32 SGEAVAVVGSSGAGKSTLL-HLLGGLDRQTsGEV 64
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLnALLPELDLRT-GEI 137
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
144-217 |
4.94e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297171361 144 LSGGEQQ------RVALARALSNYPLILLADEPSGNLDSYMSHELHDLL-FQLKKDRGL-AMILVTHNRQLAQRADRIME 215
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIpQVIMISHHRELLSVADVAYE 881
|
..
gi 297171361 216 LR 217
Cdd:PRK01156 882 VK 883
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
151-212 |
4.47e-03 |
|
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: 37.72 E-value: 4.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 297171361 151 RVALARALSNYPLILLADEPSGNLDSY----MSHELHDLLFQLKKDRGLAMILVTHNRQLAQRADR 212
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDREniesLAHALVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1278
|
|
| |
