|
Name |
Accession |
Description |
Interval |
E-value |
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-227 |
4.73e-131 |
|
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: 368.30 E-value: 4.73e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAA 160
Cdd:COG4181 84 RARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 161 DPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAA 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-223 |
5.17e-109 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 312.36 E-value: 5.17e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRA 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 RVRAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAA 160
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 161 DPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-221 |
2.90e-98 |
|
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: 284.77 E-value: 2.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVR 85
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-221 |
1.36e-86 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 255.86 E-value: 1.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQR 81
Cdd:PRK10584 3 AENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEGRKD--AREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFA 159
Cdd:PRK10584 83 AKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSrqSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 160 ADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-223 |
2.30e-78 |
|
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: 234.55 E-value: 2.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARV 84
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-226 |
7.72e-76 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 228.01 E-value: 7.72e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARV 84
Cdd:COG2884 1 MIRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RaEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELNKeRNTTLVLVTHDERLAHRCR-RLIRLEGGRLVAPQE 226
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-222 |
2.18e-64 |
|
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: 199.34 E-value: 2.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAeH 88
Cdd:cd03258 5 KNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-222 |
5.39e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.84 E-value: 5.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAeH 88
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARR-K 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIAGvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHRCrrlIRLEGGRLV 222
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvvRRICDRV---AVLENGRIV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
3.02e-63 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 197.62 E-value: 3.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDq 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 rarvraehVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:COG1116 82 --------RGVVFQEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD--E--RLAHR 209
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvdEavFLADR 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-220 |
1.96e-61 |
|
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: 191.31 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 10 NLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEHV 89
Cdd:TIGR02673 6 NVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 90 GFVFQSFQLLDSLNALENVMLPMELEGRK--DAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKKerEIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 168 DEPTGNLDSHTGERISDLLFELNKeRNTTLVLVTHDERLAHRCR-RLIRLEGGR 220
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAhRVIILDDGR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
2.50e-60 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 189.50 E-value: 2.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:COG3638 1 PMLELRNLSKRYP---GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 VRAEhVGFVFQSFQLLDSLNALENVMLpmeleGR---------------KDAREKARDLLERVGLGKRLTHTPRQLSGGE 148
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVLA-----GRlgrtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 149 QQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-223 |
2.97e-60 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 199.95 E-value: 2.97e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 VRAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAAD 161
Cdd:PRK10535 83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-223 |
1.33e-59 |
|
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: 187.49 E-value: 1.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAeHVGFVFQSFQLLDSLNALENVMLPMELEGRKD---AREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARA 157
Cdd:COG1127 77 LYELRR-RIGMLFQGGALFDSLTVFENVAFPLREHTDLSeaeIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 158 FAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIA 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-222 |
5.02e-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: 185.97 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeLDEDQRARV 84
Cdd:COG1126 1 MIEIENLHK----SFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEhVGFVFQSFQLLDSLNALENVML-PMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAAD 161
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKmsKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 162 PHVLFADEPTGNLDShtgERIS---DLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:COG1126 155 PKVMLFDEPTSALDP---ELVGevlDVMRDLAKE-GMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-209 |
2.88e-58 |
|
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: 183.44 E-value: 2.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDqrarvr 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aehVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03293 75 ---RGYVFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD--E--RLAHR 209
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDidEavFLADR 201
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-216 |
3.75e-58 |
|
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: 182.82 E-value: 3.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEH 88
Cdd:TIGR03608 2 KNISK----KFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLskKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERLAHRCRRLIRL 216
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-221 |
1.37e-57 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 182.32 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVpsTEGDLT--ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDE 78
Cdd:PRK11629 1 MNKILLQCDNLCKRY--QEGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 79 DQRARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIAR 156
Cdd:PRK11629 79 AAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 157 AFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
24-222 |
3.58e-56 |
|
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: 178.29 E-value: 3.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEHVGFVFQSFQLLDSLN 103
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR-RRIGYIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELE---GRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:TIGR02982 99 ARQNVQMALELQpnlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492156113 181 RISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-222 |
3.72e-56 |
|
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: 178.47 E-value: 3.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRaRV 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEHVGFVFQsfqllDSLNAL-------ENVMLPMELEGRKDAREKAR----DLLERVGLGK-RLTHTPRQLSGGEQQRV 152
Cdd:cd03257 80 RRKEIQMVFQ-----DPMSSLnprmtigEQIAEPLRIHGKLSKKEARKeavlLLLVGVGLPEeVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERL-AHRCRRLIRLEGGRLV 222
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVvAKIADRVAVMYAGKIV 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-221 |
3.54e-55 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 175.29 E-value: 3.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEH 88
Cdd:cd03292 4 INVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMEL--EGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKeRNTTLVLVTHDERLAHRCR-RLIRLEGGRL 221
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-223 |
1.68e-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: 174.61 E-value: 1.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeldeDQRARVR 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT----RRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQsfQLLDSLNALENV----MLPMELEGRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAA 160
Cdd:COG1124 78 RRRVQMVFQ--DPYASLHPRHTVdrilAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 161 DPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERL-AHRCRRLIRLEGGRLVA 223
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVvAHLCDRVAVMQNGRIVE 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-221 |
1.17e-53 |
|
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: 171.56 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeLDEDQRARVR 85
Cdd:cd03262 1 IEIKNLHK----SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AeHVGFVFQSFQLLDSLNALENVML-PMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLaPIKVKGmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERLA-HRCRRLIRLEGGRL 221
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-223 |
3.87e-53 |
|
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: 170.76 E-value: 3.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAeHVGFVFQSFQLL 99
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-RMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDA---REKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:cd03261 90 DSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492156113 177 HTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVA 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-203 |
6.41e-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: 173.75 E-value: 6.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:COG3842 1 MAMPALELENVSK----RYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RarvraeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:COG3842 77 R------NVGMVFQDYALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD 195
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-222 |
1.06e-52 |
|
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: 172.16 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLP---SAGSVILSGRNLSELDEDQR 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARVRAEHVGFVFQsfqllDSLNAL-------ENVMLPMEL---EGRKDAREKARDLLERVGL---GKRLTHTPRQLSGGE 148
Cdd:COG0444 81 RKIRGREIQMIFQ-----DPMTSLnpvmtvgDQIAEPLRIhggLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 149 QQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDerL---AHRCRRLIRLEGGRLV 222
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD--LgvvAEIADRVAVMYAGRIV 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-222 |
1.06e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.06 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEH 88
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARvtELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
3.67e-52 |
|
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: 175.86 E-value: 3.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPS-TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDED 79
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARVRAeHVGFVFQS-FQLLD-SLNALENVMLPMELEG---RKDAREKARDLLERVGLGKRLTH-TPRQLSGGEQQRVA 153
Cdd:COG1123 336 SLRELRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 154 IARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-223 |
1.01e-51 |
|
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: 174.71 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA---GSVILSGRNLSELDED 79
Cdd:COG1123 2 TPLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARvraeHVGFVFQSFqlLDSLNAL---ENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAI 154
Cdd:COG1123 80 LRGR----RIGMVFQDP--MTQLNPVtvgDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-221 |
9.35e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.14 E-value: 9.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARV 84
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raehvGFVFQSFQLLDSlNALENVMLPMELEGRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:COG4619 77 -----AYVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRL 221
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-220 |
2.29e-48 |
|
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: 157.63 E-value: 2.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 10 NLSKVVPSTEGdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHV 89
Cdd:cd03225 4 NLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR----KV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 90 GFVFQSF--QLLdSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03225 78 GLVFQNPddQFF-GPTVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRLIRLEGGR 220
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-222 |
3.41e-48 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 158.50 E-value: 3.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAeH 88
Cdd:cd03256 4 ENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR-Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPM--------ELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-223 |
4.72e-48 |
|
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: 157.49 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvr 85
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQS--FQLLDSlNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAAD 161
Cdd:COG1122 76 --KVGLVFQNpdDQLFAP-TVEEDVAFGPENLGlpREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-223 |
1.09e-47 |
|
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: 156.14 E-value: 1.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvr 85
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03259 73 --NIGMVFQDYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRLVA 223
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqeeaLALAD---RIAVMNEGRIVQ 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-222 |
1.12e-47 |
|
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: 157.81 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQSFQLLDSLNA 104
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:cd03294 120 LENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 183 SDLLFELNKERNTTLVLVTHD--E--RLAHrcrRLIRLEGGRLV 222
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDldEalRLGD---RIAIMKDGRLV 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-223 |
1.51e-47 |
|
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: 157.13 E-value: 1.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELdedqRARV 84
Cdd:COG1120 1 MLEAENLSVGY----GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEHVGFVFQSFQLLDSLNALENVML-------PMELEGRKDaREKARDLLERVGLGKrLTHTP-RQLSGGEQQRVAIAR 156
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryphlgLFGRPSAED-REAVEEALERTGLEH-LADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 157 AFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVA 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-226 |
3.57e-46 |
|
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: 153.22 E-value: 3.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARV 84
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAeHVGFVFQSFQLLDSLNALENVmlpmeLEGR---------------KDAREKARDLLERVGLGKRLTHTPRQLSGGEQ 149
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENV-----LHGRlgykptwrsllgrfsEEDKERALSALERVGLADKAYQRADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV---APQ 225
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVfdgAPS 231
|
.
gi 492156113 226 E 226
Cdd:TIGR02315 232 E 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-221 |
8.09e-46 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 152.17 E-value: 8.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArVRAEhVGFVFQSFQLL 99
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IRQE-AGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVML-PMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:PRK09493 90 PHLTALENVMFgPLRVRGasKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 177 HTGERISDLLFELNKErNTTLVLVTHDERLAHRC-RRLIRLEGGRL 221
Cdd:PRK09493 170 ELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVaSRLIFIDKGRI 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-223 |
8.44e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.44 E-value: 8.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldedQRARVR 85
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVRENLRFFARLYGlpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVA 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-226 |
1.29e-44 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.22 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSesiLSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldeDQ 80
Cdd:COG1118 1 MS---IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-----FT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQLLDSLNALENVM--LPMELEGRKDAREKARDLLERV---GLGKRLthtPRQLSGGEQQRVAIA 155
Cdd:COG1118 69 NLPPRERRVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVqleGLADRY---PSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA---PQE 226
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQvgtPDE 220
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
6-207 |
1.71e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 149.57 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR----------NLSE 75
Cdd:COG4598 9 LEVRDLHK----SFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 76 LDEDQRARVRAEhVGFVFQSFQLLDSLNALENVML-PMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRV 152
Cdd:COG4598 85 ADRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGrpKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDShtgERISDLLF---ELNKERNTTLVlVTHDERLA 207
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDP---ELVGEVLKvmrDLAEEGRTMLV-VTHEMGFA 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-220 |
3.07e-44 |
|
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: 146.18 E-value: 3.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 10 NLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaeHV 89
Cdd:cd03229 5 NVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR--RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 90 GFVFQSFQLLDSLNALENVMLPmelegrkdarekardllervglgkrlthtprqLSGGEQQRVAIARAFAADPHVLFADE 169
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 170 PTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGR 220
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
3.99e-44 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 154.84 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKS-TLLGLLAGLDLPSA---GSVILSGRNLSEL 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DEDQRARVRAEHVGFVFQsfQLLDSLNAL----ENVMLPMELE---GRKDAREKARDLLERVGL---GKRLTHTPRQLSG 146
Cdd:COG4172 82 SERELRRIRGNRIAMIFQ--EPMTSLNPLhtigKQIAEVLRLHrglSGAAARARALELLERVGIpdpERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRLV 222
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRFAD---RVAVMRQGEIV 236
|
250
....*....|....*
gi 492156113 223 ----------APQEP 227
Cdd:COG4172 237 eqgptaelfaAPQHP 251
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-223 |
6.16e-44 |
|
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: 154.92 E-value: 6.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQL 98
Cdd:COG4987 345 GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR----RIAVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LD-SLnaLENVMLpmeleGRKDA-REKARDLLERVGLGKRLTHTP-----------RQLSGGEQQRVAIARAFAADPHVL 165
Cdd:COG4987 421 FDtTL--RENLRL-----ARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:COG4987 494 LLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-222 |
1.24e-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: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKST-----LLGLLAGLDLPSAGSVILSGRNLSELDEDqRARVRAEhVGFVFQ 94
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTllrllNRLNDLIPGAPDEGEVLLDGKDIYDLDVD-VLELRRR-VGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQLLDsLNALENVMLPMELEGRKDAR---EKARDLLERVGL---GKRLTHtPRQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:cd03260 89 KPNPFP-GSIYDNVAYGLRLHGIKLKEeldERVEEALRKAALwdeVKDRLH-ALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 169 EPTGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHRC-RRLIRLEGGRLV 222
Cdd:cd03260 167 EPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVaDRTAFLLNGRLV 219
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-226 |
8.37e-43 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 146.39 E-value: 8.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeH 88
Cdd:COG1125 5 ENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGL-----GKRLthtPRQLSGGEQQRVAIARAFAAD 161
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGwdKERIRARVDELLELVGLdpeeyRDRY---PHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD--E--RLAHrcrRLIRLEGGRLV---APQE 226
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDidEalKLGD---RIAVMREGRIVqydTPEE 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-222 |
5.20e-42 |
|
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: 142.44 E-value: 5.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVPSTEgdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeH 88
Cdd:cd03295 4 ENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGL--GKRLTHTPRQLSGGEQQRVAIARAFAADPHV 164
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 165 LFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIV 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
7.91e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.83 E-value: 7.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSEsiLSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:COG3839 1 MAS--LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RarvraeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:COG3839 75 R------NIAMVFQSYALYPHMTVYENIAFPLKLRKvpKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD--E--RLAHrcrRLIRLEGGRLV---APQE 226
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqvEamTLAD---RIAVMNDGRIQqvgTPEE 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-203 |
1.47e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.92 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrar 83
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 vraehvGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAAD 161
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-227 |
1.65e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 141.43 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGDlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSV------ILSGRNLSElded 79
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQ---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARVRA--EHVGFVFQSFQLLDSLNALENVM---LPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAI 154
Cdd:PRK11264 76 QKGLIRQlrQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 155 ARAFAADPHVLFADEPTGNLDShtgERISDLLFELNK--ERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV--------- 222
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVeqgpakalf 232
|
....*.
gi 492156113 223 -APQEP 227
Cdd:PRK11264 233 aDPQQP 238
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
25-226 |
7.04e-41 |
|
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: 140.66 E-value: 7.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEHVGFVFQsF---QLLdS 101
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ-FpehQLF-E 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 102 LNALENVML-PMEL-EGRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHT 178
Cdd:TIGR04521 98 ETVYKDIAFgPKNLgLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 179 GERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA---PQE 226
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVLdgtPRE 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-226 |
8.57e-41 |
|
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: 139.79 E-value: 8.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQR 81
Cdd:COG0411 1 SDPLLEVRGLTK----RFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 AR---VRAehvgfvFQSFQLLDSLNALENVML-----------------PMELEGRKDAREKARDLLERVGLGKRLTHTP 141
Cdd:COG0411 77 ARlgiART------FQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGR 220
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGR 230
|
....*....
gi 492156113 221 LVA---PQE 226
Cdd:COG0411 231 VIAegtPAE 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-221 |
1.22e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.37 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSkvVpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldedQ 80
Cdd:COG1121 2 MMMPAIELENLT--V--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRaehVGFVFQSFQLLDS--LNALENVML----PMELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRV 152
Cdd:COG1121 72 RARRR---IGYVPQRAEVDWDfpITVRDVVLMgrygRRGLFRRpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRLIRLEGGRL 221
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-223 |
1.48e-38 |
|
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: 139.89 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 11 LSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVG 90
Cdd:COG4988 339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR----QIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 91 FVFQSFQLL-DSLnaLENVMLpmeleGRKDA-REKARDLLERVGLGKRLT------HTP-----RQLSGGEQQRVAIARA 157
Cdd:COG4988 415 WVPQNPYLFaGTI--RENLRL-----GRPDAsDEELEAALEAAGLDEFVAalpdglDTPlgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 158 FAADPHVLFADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-220 |
1.57e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 132.60 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvr 85
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aEHVGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:COG4133 75 -RRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHRCRRLiRLEGGR 220
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARVL-DLGDFK 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-220 |
1.68e-38 |
|
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: 131.35 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQL 98
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK----NIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLnaLENVmlpmelegrkdarekardllervglgkrlthtprqLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03228 88 FsGTI--RENI-----------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492156113 178 TGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGR 220
Cdd:cd03228 131 TEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-223 |
4.66e-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: 130.25 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLL 99
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR----KIAYVPQALELL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DslnalenvmlpmelegrkdarekARDLLERvglgkRLThtprQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTG 179
Cdd:cd03214 86 G-----------------------LAHLADR-----PFN----ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 180 ERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVA 178
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-222 |
5.12e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 132.06 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR--NLSELDEDQRARVRAEHVGFVFQSFQ 97
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLDSLNALENVM-LPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:COG4161 93 LWPHLTVMENLIeAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 175 DSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:COG4161 173 DPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKvASQVVYMEKGRII 220
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
20-226 |
1.45e-37 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 131.08 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrarVRAEHVGFVFQSFQLL 99
Cdd:TIGR00968 11 GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRKIGFVFQHYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:TIGR00968 85 KHLTVRDNIAFGLEIRKHPKAKIKARveELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV---APQE 226
Cdd:TIGR00968 165 VRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKIEqigSPDE 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-223 |
1.89e-37 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 130.63 E-value: 1.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVR 85
Cdd:cd03219 1 LEVRGLTK----RFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aehVGFVFQSFQLLDSLNALENVMLPMEL------------EGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVA 153
Cdd:cd03219 77 ---IGRTFQIPRLFPELTVLENVMVAAQArtgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 154 IARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNkERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDmDVVMSLADRVTVLDQGRVIA 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-226 |
1.90e-37 |
|
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: 131.40 E-value: 1.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGrnLSELDEDQRARVR 85
Cdd:TIGR04520 1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aEHVGFVFQ---------------SFqlldslnALENVMLPmelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQ 150
Cdd:TIGR04520 77 -KKVGMVFQnpdnqfvgatveddvAF-------GLENLGVP-----REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 151 RVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA---PQE 226
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAegtPRE 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
5-210 |
2.67e-37 |
|
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: 129.86 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKV-VPSTEGDLTI--LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR----NLSELD 77
Cdd:COG4778 4 LLEVENLSKTfTLHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHT-PRQLSGGEQQRVAI 154
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGvdREEARARARELLARLNLPERLWDLpPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD----ERLAHRC 210
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDeevrEAVADRV 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-204 |
1.55e-36 |
|
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: 128.12 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvraeHVGFVFQSFQLL 99
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR------PVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDA--REKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180
....*....|....*....|....*..
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQ 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-222 |
2.50e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.82 E-value: 2.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR--NLSELDEDQRARVRAEHVGFVFQSFQ 97
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLDSLNALENVM-LPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:PRK11124 93 LWPHLTVQQNLIeAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 175 DSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK11124 173 DPEITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-223 |
3.79e-36 |
|
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: 134.58 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQLL-DSL 102
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFsGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 naLENVMLpmeleGRKDA-REKARDLLERVGLG---KRLT---HTP-----RQLSGGEQQRVAIARAFAADPHVLFADEP 170
Cdd:COG2274 566 --RENITL-----GDPDAtDEEIIEAARLAGLHdfiEALPmgyDTVvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 171 TGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-207 |
6.53e-36 |
|
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: 126.68 E-value: 6.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrarVRAEH 88
Cdd:cd03296 6 RNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLPMELEGRK------DAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSerppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLA 207
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-203 |
3.32e-35 |
|
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: 124.76 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEgdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvr 85
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNALENVM--LPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03299 72 --DISYVPQNYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD 189
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-220 |
3.88e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 122.35 E-value: 3.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 7 SAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvra 86
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 87 eHVGFVFQsfqlldslnalenvmlpmelegrkdarekardllervglgkrlthtprqLSGGEQQRVAIARAFAADPHVLF 166
Cdd:cd00267 74 -RIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGR 220
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-209 |
5.14e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 126.77 E-value: 5.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVP-------STEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNL 73
Cdd:COG4608 3 MAEPLLEVRDLKKHFPvrgglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 74 SELDEDQRARVRAeHVGFVFQsfqllD---SLN-------ALENVMLPMELEGRKDAREKARDLLERVGLgkRLTHT--- 140
Cdd:COG4608 83 TGLSGRELRPLRR-RMQMVFQ-----DpyaSLNprmtvgdIIAEPLRIHGLASKAERRERVAELLELVGL--RPEHAdry 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 141 PRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHR 209
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsvvRHISDR 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-204 |
8.72e-35 |
|
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: 123.13 E-value: 8.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvraeHVGFVFQSFQLL 99
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKvpKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180
....*....|....*....|....*..
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-203 |
9.49e-35 |
|
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: 123.03 E-value: 9.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldEDQRARVraehvGFVFQSFQLLDS- 101
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKRI-----GYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 102 -LNALENVML----PMELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:cd03235 84 pISVRDVVLMglygHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180
....*....|....*....|....*....
gi 492156113 175 DSHTGERISDLLFELNKErNTTLVLVTHD 203
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHD 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-203 |
1.26e-34 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 125.61 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS---AGSVILSGRNLSELD 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARVRAEHVGFVFQSfqLLDSLNA--------LENVMLPMELeGRKDAREKARDLLERVGLG---KRLTHTPRQLSG 146
Cdd:PRK09473 88 EKELNKLRAEQISMIFQD--PMTSLNPymrvgeqlMEVLMLHKGM-SKAEAFEESVRMLDAVKMPearKRMKMYPHEFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-171 |
1.86e-34 |
|
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: 120.06 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLLDSLNA 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 105 LENVMLPMELEGRKDAREKAR--DLLERVGLG----KRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARaeEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-221 |
2.16e-34 |
|
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: 120.58 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvr 85
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aEHVGFVFQSFQLLDSLNALENVmlpmelegrkdarekardllervglgkrlthtprQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGRL 221
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-222 |
4.02e-34 |
|
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: 122.99 E-value: 4.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPS-----TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDE 78
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 79 DQRARVRAEhVGFVFQsfqllDSLNAL-------ENVMLPME-LEGRKDAREKAR--DLLERVGL-GKRLTHTPRQLSGG 147
Cdd:TIGR02769 81 KQRRAFRRD-VQLVFQ-----DSPSAVnprmtvrQIIGEPLRhLTSLDESEQKARiaELLDMVGLrSEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 148 EQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIV 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-223 |
1.06e-33 |
|
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: 120.09 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 27 ELSLELNkGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQSFQLLDSLNALE 106
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 107 NVMLPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLL 186
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 492156113 187 FELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRLQY 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-221 |
1.58e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 121.23 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEL-DED 79
Cdd:PRK10619 1 MSENKLNVIDLHK----RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARVRAEH--------VGFVFQSFQLLDSLNALENVM-LPMELEG--RKDAREKARDLLERVGLGKRLTHT-PRQLSGG 147
Cdd:PRK10619 77 GQLKVADKNqlrllrtrLTMVFQHFNLWSHMTVLENVMeAPIQVLGlsKQEARERAVKYLAKVGIDERAQGKyPVHLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 148 EQQRVAIARAFAADPHVLFADEPTGNLDShtgERISDLLFELNK--ERNTTLVLVTHDERLA-HRCRRLIRLEGGRL 221
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaEEGKTMVVVTHEMGFArHVSSHVIFLHQGKI 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-226 |
1.82e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 120.24 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHE-----LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQS 95
Cdd:COG3840 6 DLTYRYGdfplrFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 96 FQLLDSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 174 LDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQE 226
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-222 |
2.59e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.56 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPS-----TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDE 78
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 79 DQRARVRAEhVGFVFQsfqllDSLNAL-------ENVMLPME-LEGRKDAREKAR--DLLERVGLGKR-LTHTPRQLSGG 147
Cdd:PRK10419 82 AQRKAFRRD-IQMVFQ-----DSISAVnprktvrEIIREPLRhLLSLDKAERLARasEMLRAVDLDDSvLDKRPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 148 EQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-222 |
4.86e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.82 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEhVGFVFQSFQLLDSLNA 104
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:PRK10908 97 YDNVAIPLIIAGAsgDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492156113 183 SDLLFELNKErNTTLVLVTHDERL-AHRCRRLIRLEGGRLV 222
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTLSDGHLH 216
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-204 |
1.06e-32 |
|
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: 120.91 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvr 85
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:TIGR03265 77 --DYGIVFQSYALFPNLTVADNIAYGLKNRGmgRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQ 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
1.28e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQ 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEhVGFVFQS--FQLL------DSLNALENVMLPmelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRV 152
Cdd:PRK13635 76 VWDVRRQ-VGMVFQNpdNQFVgatvqdDVAFGLENIGVP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA---PQE 226
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEegtPEE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-207 |
1.31e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.96 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESIlsaQNLSKVVPSTEgdltILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELdedq 80
Cdd:PRK10851 1 MSIEI---ANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRaeHVGFVFQSFQLLDSLNALENV-----MLPM-ELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAI 154
Cdd:PRK10851 70 HARDR--KVGFVFQHYALFRHMTVFDNIafgltVLPRrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLA 207
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-223 |
1.71e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 123.35 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQL 98
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLnaLENVMLpmeleGRKDA-REKARDLLERVGLGKRLTHTP-----------RQLSGGEQQRVAIARAFAADPHVL 165
Cdd:COG1132 426 FsGTI--RENIRY-----GRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERnTTLVlVTHdeRLA--HRCRRLIRLEGGRLVA 223
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLMKGR-TTIV-IAH--RLStiRNADRILVLDDGRIVE 554
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-227 |
2.61e-32 |
|
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: 117.27 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldEDQRARvr 85
Cdd:COG4555 2 IEVENLSK----KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-227 |
4.93e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.40 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 18 TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrARvraEHVGFVFQS-- 95
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IR---KKIGIIFQNpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 96 FQLL------DSLNALENVMLPmelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADE 169
Cdd:PRK13632 94 NQFIgatvedDIAFGLENKKVP-----PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 170 PTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-227 |
4.95e-32 |
|
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: 121.83 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLL--AGLDLPSAGSVILS----------------GRNLS------- 74
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvGEPCPvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 75 -------ELDEDQRARVRaEHVGFVFQ-SFQLLDSLNALENVMLPMELEGR--KDAREKARDLLERVGLGKRLTHTPRQL 144
Cdd:TIGR03269 91 peevdfwNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYegKEAVGRAVDLIEMVQLSHRITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 145 SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTH-DERLAHRCRRLIRLEGGRLVA 223
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVIEDLSDKAIWLENGEIKE 249
|
....
gi 492156113 224 PQEP 227
Cdd:TIGR03269 250 EGTP 253
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-204 |
5.04e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.67 E-value: 5.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:PRK09452 10 SLSPLVELRGISK----SFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RarvraeHVGFVFQSFQLLDSLNALENVM--LPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:PRK09452 86 R------HVNTVFQSYALFPHMTVFENVAfgLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-227 |
1.09e-31 |
|
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: 120.94 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVP-------STEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDlPSAGSVILSGRNLSELD 77
Cdd:COG4172 275 LLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARVRAeHVGFVFQsfqllD---SLN----ALENVMLPMELEG----RKDAREKARDLLERVGLGKRLTHT-PRQLS 145
Cdd:COG4172 354 RRALRPLRR-RMQVVFQ-----DpfgSLSprmtVGQIIAEGLRVHGpglsAAERRARVAEALEEVGLDPAARHRyPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRL 221
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDlavvRALAH---RVMVMKDGKV 504
|
250
....*....|....*.
gi 492156113 222 V----------APQEP 227
Cdd:COG4172 505 VeqgpteqvfdAPQHP 520
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-210 |
1.24e-31 |
|
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: 114.91 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldedQRARVR 85
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGlpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHD----ERLAHRC 210
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSmdeaEALCDRI 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-203 |
1.62e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.57 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrarvraehvGFVFQSFQLLDSLN 103
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGER 181
Cdd:PRK11248 87 VQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 492156113 182 ISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-227 |
2.31e-31 |
|
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: 116.82 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 40 IVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvraeHVGFVFQSFQLLDSLNALENVMLP--MELEGR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR------HINMVFQSYALFPHMTVEENVAFGlkMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 118 KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTL 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|.
gi 492156113 198 VLVTHDERLA-HRCRRLIRLEGGRLVAPQEP 227
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKIAQIGTP 185
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
25-222 |
2.58e-31 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 117.48 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQSFQLLDSLNA 104
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELE--GRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:NF040840 90 FENIAFGLKLRkvPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492156113 183 SDLLFELNKERNTTLVLVTH--DERLAHRCRRLIRLEgGRLV 222
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHnfEEALSLADRVGIMLN-GRLS 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-226 |
5.36e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 5.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVR 85
Cdd:PRK13548 3 LEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AehvgfVF-QSFQLLDSLNALENVML---PMELEGRKDAREkARDLLERVG---LGKRLTHtprQLSGGEQQRVAIARAF 158
Cdd:PRK13548 79 A-----VLpQHSSLSFPFTVEEVVAMgraPHGLSRAEDDAL-VAAALAQVDlahLAGRDYP---QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 159 A------ADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA---PQE 226
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVAdgtPAE 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-222 |
6.68e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 115.18 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 8 AQNLSKVV-PSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVIL----------SGRNLSEL 76
Cdd:PRK13651 5 VKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkkTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DED--QRARVRA--------EHVGFVFQ--SFQLLDSlNALENVML-PMELEGRK-DAREKARDLLERVGLGKR-LTHTP 141
Cdd:PRK13651 85 EKLviQKTRFKKikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFgPVSMGVSKeEAKKRAAKYIELVGLDESyLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRLIRLEGGR 220
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDlDNVLEWTKRTIFFKDGK 242
|
..
gi 492156113 221 LV 222
Cdd:PRK13651 243 II 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-203 |
1.05e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 115.06 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVP------STEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLS 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 75 ELDEDQRARVRAEhVGFVFQSfqLLDSLNALENV--MLPMELE-----GRKDAREKARDLLERVGLgkRLTHT---PRQL 144
Cdd:PRK11308 81 KADPEAQKLLRQK-IQIVFQN--PYGSLNPRKKVgqILEEPLLintslSAAERREKALAMMAKVGL--RPEHYdryPHMF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 145 SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-226 |
1.31e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQ--SFQLLDSL 102
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVMLPMELE-GRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:PRK13634 103 VEKDICFGPMNFGvSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 181 RISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA---PQE 226
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVFLqgtPRE 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-221 |
1.36e-30 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 111.15 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvr 85
Cdd:cd03246 1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLD-SLNalENVmlpmelegrkdarekardllervglgkrlthtprqLSGGEQQRVAIARAFAADPHV 164
Cdd:cd03246 77 --HVGYLPQDDELFSgSIA--ENI-----------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 165 LFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-222 |
1.66e-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: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 11 LSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeldedqrARVRAEHVG 90
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 91 FVFQS--FQLLDSLNALEnvmLPMELEGRKDAREKARDLLERVGL-GKRLTHtPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:cd03226 75 YVMQDvdYQLFTDSVREE---LLLGLKELDAGNEQAETVLKDLDLyALKERH-PLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 168 DEPTGNLDSHTGERISDLLFELNKERNTTLVlVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-227 |
1.89e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.10 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR-----NLSE 75
Cdd:PRK11701 2 MDQPLLSVRGLTK----LYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 76 LDEDQRARVRAEHVGFVFQSFQ--LLDSLNALENVMLPMELEGRK---DAREKARDLLERVGLG-KRLTHTPRQLSGGEQ 149
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEIDaARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRLVA-- 223
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlavaRLLAH---RLLVMKQGRVVEsg 234
|
250
....*....|..
gi 492156113 224 --------PQEP 227
Cdd:PRK11701 235 ltdqvlddPQHP 246
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-204 |
1.98e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.80 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLP---SAGSVILSGRNLSELDEDQRarvraeHVGFVFQSF 96
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR------RIGILFQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 97 QLLDSLNALENVM--LPMELeGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:COG4136 86 LLFPHLSVGENLAfaLPPTI-GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|
gi 492156113 175 DSHTGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-226 |
3.07e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 112.52 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVR 85
Cdd:COG4559 2 LEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AehvgfVF-QSFQLLDSLNALENVML---PMELEGRKDAREkARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFA-- 159
Cdd:COG4559 78 A-----VLpQHSSLAFPFTVEEVVALgraPHGSSAAQDRQI-VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 160 -----ADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA---PQE 226
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAqgtPEE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-209 |
4.77e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.34 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKS-TLLGLLAGLDLPSA----GSVILSGRNLSE 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 76 LDEDQRARVRAEHVGFVFQsfQLLDSLNALEN-------VMLPMELEGRKDAREKARDLLERVGL---GKRLTHTPRQLS 145
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQ--EPMVSLNPLHTlekqlyeVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHR 209
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlsivRKLADR 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-203 |
5.08e-30 |
|
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: 111.02 E-value: 5.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehvgfVFQSFQLLDSLNA 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLP----MELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:TIGR01184 72 RENIALAvdrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|...
gi 492156113 181 RISDLLFELNKERNTTLVLVTHD 203
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHD 174
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-225 |
5.95e-30 |
|
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: 110.66 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQSFQLLDSLNALEN 107
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 108 VMLPME--LEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDL 185
Cdd:cd03298 91 VGLGLSpgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492156113 186 LFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAPQ 225
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-210 |
6.04e-30 |
|
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: 111.23 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTL-----LGLLAGLDLPSAGSVILSGRNLSELDED 79
Cdd:TIGR00972 1 AIEIENLNLFY----GEKEALKNINLDIPKNQVTALIGPSGCGKSTLlrslnRMNDLVPGVRIEGKVLFDGQDIYDKKID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRArVRaEHVGFVFQSFQLLdSLNALENVMLPMELEGRKD---AREKARDLLERVGL----GKRLTHTPRQLSGGEQQRV 152
Cdd:TIGR00972 77 VVE-LR-RRVGMVFQKPNPF-PMSIYDNIAYGPRLHGIKDkkeLDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKerNTTLVLVTHDERLAHRC 210
Cdd:TIGR00972 154 CIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKK--KYTIVIVTHNMQQAARI 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-216 |
1.52e-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: 115.08 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLLDSlNA 104
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD----QIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLpmeleGRKDAREKA-RDLLERVGLGKRL------THTP-----RQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:TIGR02857 413 AENIRL-----ARPDASDAEiREALERAGLDEFVaalpqgLDTPigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 173 NLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRL 216
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-222 |
1.57e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 109.77 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 26 HELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLP----SAGSVILSGRNLSELdedqraRVRAEHVGFVFQ----SFQ 97
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL------SIRGRHIATIMQnprtAFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLDSL--NALENVMLPMELEgrKDAREKARDLLERVGL--GKRLTHT-PRQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:TIGR02770 77 PLFTMgnHAIETLRSLGKLS--KQARALILEALEAVGLpdPEEVLKKyPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492156113 173 NLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRC-RRLIRLEGGRLV 222
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIaDEVAVMDDGRIV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-223 |
5.28e-29 |
|
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: 108.29 E-value: 5.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraEHVGFVFQSFQLL 99
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPmeleGRKDAREKARDLLERV-----GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:cd03224 88 PELTVEENLLLG----AYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 175 DSHTGERISDLLFELNKERnTTLVLVTHDERLA-HRCRRLIRLEGGRLVA 223
Cdd:cd03224 164 APKIVEEIFEAIRELRDEG-VTILLVEQNARFAlEIADRAYVLERGRVVL 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-223 |
6.10e-29 |
|
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: 108.23 E-value: 6.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 8 AQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGrnlseLDEDQRARVRAE 87
Cdd:cd03265 3 VENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG-----HDVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 88 HVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIIA 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-222 |
1.35e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 109.83 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTLLGLLAGLD----LPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQSfqLLDSLN 103
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD--PMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLP-MEL----EG--RKDAREKARDLLERVGL---GKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:PRK11022 104 PCYTVGFQiMEAikvhQGgnKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 174 LDSHTGERISDLLFELNKERNTTLVLVTHDERL-AHRCRRLIRLEGGRLV 222
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVV 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-222 |
1.58e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLS-KVVPSTEGDLTI-LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDED 79
Cdd:PRK13633 1 MNEMIKCKNVSyKYESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARVRAehvGFVFQS--FQLLDSLnALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIA 155
Cdd:PRK13633 81 WDIRNKA---GMVFQNpdNQIVATI-VEEDVAFGPENLGipPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-203 |
3.85e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.07 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvraehvgFVFQSFQLL 99
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---------LMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTG 179
Cdd:PRK11247 94 PWKKVIDNVGLGL----KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180
....*....|....*....|....
gi 492156113 180 ERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK11247 170 IEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-204 |
3.97e-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: 110.91 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVraehVGFVFQSFQL 98
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSlNALENVMLpmeleGRKDAR-EKARDLLERVGLGKRLTHTP-----------RQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:TIGR02868 421 FDT-TVRENLRL-----ARPDATdEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDE 204
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-227 |
4.64e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 109.35 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 29 SLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQSFQLLDSLNALENV 108
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 109 MLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLL 186
Cdd:PRK10070 128 AFGMELAGinAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492156113 187 FELNKERNTTLVLVTHDERLAHRC-RRLIRLEGGRLVAPQEP 227
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTP 249
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-223 |
4.79e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 108.65 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 39 AIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseLDEDQRARVRAE--HVGFVFQSFQLLDSLNALENVMLPMELEG 116
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLPPHrrRIGYVFQEARLFPHLSVRGNLLYGRKRAP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 117 RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTT 196
Cdd:COG4148 107 RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIP 186
|
170 180 190
....*....|....*....|....*....|.
gi 492156113 197 LVLVTHD----ERLAhrcRRLIRLEGGRLVA 223
Cdd:COG4148 187 ILYVSHSldevARLA---DHVVLLEQGRVVA 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-202 |
7.81e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 105.89 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTllgll--agldlPSA---GSVILSGRNLSEL 76
Cdd:COG1117 8 LEPKIEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndliPGArveGEILLDGEDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DEDQrARVRAeHVGFVFQSfqlldsLNAL-----ENVMLPMELEGRKDAR---EKARDLLERVGLGK----RLTHTPRQL 144
Cdd:COG1117 84 DVDV-VELRR-RVGMVFQK------PNPFpksiyDNVAYGLRLHGIKSKSeldEIVEESLRKAALWDevkdRLKKSALGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 145 SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERntTLVLVTH 202
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTH 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-222 |
8.01e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 8.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDL--PSA---GSVILSGRNLSELD-EDQRARVRaehvgFVF 93
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDvIELRRRVQ-----MVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 QSFQLLDSLNALENVMLPMEL----EGRKDAREKARDLLERVGL----GKRLTHTPRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHRCRRLIR-LEGGRLV 222
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAfLYKGQIV 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-223 |
1.13e-27 |
|
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: 104.67 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDqrarvr 85
Cdd:cd03269 1 LEVENVTK----RFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03269 71 --RIGYLPEERGLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVL 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-223 |
1.84e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.14 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrarVRAeHVGFVFQSFQL 98
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQ-AISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLNalENVMLpmeleGRKDAR-EKARDLLERVGLGKRLTHTP----------RQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:PRK11160 426 FsATLR--DNLLL-----AAPNASdEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-223 |
2.91e-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: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTegDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvr 85
Cdd:COG4618 331 LSVENLTVVPPGS--KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNAlENV-MLPmELEGRK--DAREKAR--DLLERV--GLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:COG4618 407 --HIGYLPQDVELFDGTIA-ENIaRFG-DADPEKvvAAAKLAGvhEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 159 AADPHVLFADEPTGNLDShTGER-----ISDLlfelnKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDD-EGEAalaaaIRAL-----KARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-223 |
1.78e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 103.26 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARV 84
Cdd:COG4152 1 MLELKGLTK----RFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raehvGFV------FQSFQLLDSLNALenvmlpMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIAR 156
Cdd:COG4152 74 -----GYLpeerglYPKMKVGEQLVYL------ARLKGlsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 157 AFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD----ERLahrCRRLIRLEGGRLVA 223
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQmelvEEL---CDRIVIINKGRKVL 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-227 |
1.97e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKvvpSTEGDLTIlHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArv 84
Cdd:PRK11607 19 LLEIRNLTK---SFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raehVGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:PRK11607 93 ----INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEP 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-207 |
2.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 2.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPStegDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARV 84
Cdd:PRK13639 1 ILETRDLKYSYPD---GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE---PIKYDKKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RA-EHVGFVFQSFQllDSLNA---LENVML-PMELEGRKDAREK-ARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:PRK13639 75 EVrKTVGIVFQNPD--DQLFAptvEEDVAFgPLNLGLSKEEVEKrVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERLA 207
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-203 |
2.98e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.22 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEG-----DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD 77
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARvraeHVGFVFQSFQllDSLNALENV--ML--PMELEGRKDARE---KARDLLERVGL-GKRLTHTPRQLSGGEQ 149
Cdd:COG4167 82 YKYRCK----HIRMIFQDPN--TSLNPRLNIgqILeePLRLNTDLTAEEreeRIFATLRLVGLlPEHANFYPHMLSSGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-223 |
4.05e-26 |
|
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: 101.31 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVI------LSGRNLSELdedqrarvRAeHVGFVF 93
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWEL--------RK-RIGLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 QSFQ--LLDSLNALENVM--------LPMELEgrKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:COG1119 85 PALQlrFPRDETVLDVVLsgffdsigLYREPT--DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRC-RRLIRLEGGRLVA 223
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-209 |
4.66e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTegdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD--ED 79
Cdd:COG1129 1 AEPLLEMRGISKSFGGV----KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARvraehVGFVFQSFQLLDSLNALENVMLPMELEG-----RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAI 154
Cdd:COG1129 77 QAAG-----IAIIHQELNLVPNLSVAENIFLGREPRRgglidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH--DE--RLAHR 209
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHrlDEvfEIADR 209
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-222 |
5.09e-26 |
|
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: 101.45 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRN-----LSELD 77
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARVRAEHVGFVFQSFQ--LLDSLNALENV-MLPMELEGRK--DAREKARDLLERVGLGK-RLTHTPRQLSGGEQQR 151
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRdgLRMRVSAGANIgERLMAIGARHygNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 152 VAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRLV 222
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlgvaRLLAQ---RLLVMQQGRVV 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-203 |
5.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.78 E-value: 5.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQ--SFQLLDSL 102
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVMLP----MELEgrkDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:PRK13646 103 VEREIIFGPknfkMNLD---EVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180
....*....|....*....|....*.
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-203 |
7.02e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.37 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILsgrNLSELDEDQRARVRaEHVGFVFQ--------SF 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFY---NNQAITDDNFEKLR-KHIGIVFQnpdnqfvgSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 97 QLLDSLNALENVMLPMElegrkDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:PRK13648 101 VKYDVAFGLENHAVPYD-----EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180
....*....|....*....|....*..
gi 492156113 177 HTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHD 202
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
24-222 |
7.23e-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: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLLDSlN 103
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEGRKDAREKAR-----DLLERV--GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAARaanahEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 177 HTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:cd03251 172 ESERLVQAALERLMKNR-TTFV-------IAHRlstienADRIVVLEDGKIV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-222 |
7.71e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 100.38 E-value: 7.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrarVRaEHVGFVFQSFQLLDSlN 103
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLpmeleGRKDARE-------KARDLLERVG---------LGKRLThtprQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:cd03253 91 IGYNIRY-----GRPDATDeevieaaKAAQIHDKIMrfpdgydtiVGERGL----KLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 168 DEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIV 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-209 |
1.80e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.92 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGL--LAGLDLPSA---GSVILSGRNLSELDEDQrARVRAEhVGFVFQ 94
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnRLLELNEEArveGEVRLFGRNIYSPDVDP-IEVRRE-VGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQLLDSLNALENVMLPMELEG----RKDAREKARDLLERVGL----GKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGlvksKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHR 209
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAAR 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-226 |
2.05e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQ--SFQLLDSl 102
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVML-PMELEGRKD-AREKARDLLERVGLGKRL-THTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTG 179
Cdd:PRK13641 102 TVLKDVEFgPKNFGFSEDeAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 492156113 180 ERISDLLFELNKERNtTLVLVTHD-ERLAHRCRRLIRLEGGRLV---APQE 226
Cdd:PRK13641 182 KEMMQLFKDYQKAGH-TVILVTHNmDDVAEYADDVLVLEHGKLIkhaSPKE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-222 |
3.16e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 98.45 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQLLdSLN 103
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFLF-SGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVML-----PMELEGRKDAREKARDLLERV--GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:cd03254 93 IMENIRLgrpnaTDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 177 HTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:cd03254 173 ETEKLIQEALEKLMKGR-TSII-------IAHRlstiknADKILVLDDGKII 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-223 |
3.46e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 98.05 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrARVRAEHVGFVFQSFQLL-DSLN 103
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQDVTLFyGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 alENVMLpmeleGRKDAREkaRDLLERV--------------GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADE 169
Cdd:cd03245 96 --DNITL-----GAPLADD--ERILRAAelagvtdfvnkhpnGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 170 PTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVA 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-223 |
3.83e-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: 98.56 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVraehvGFVF-QSFQLLDSLN 103
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI-----GVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEGRKDAREKAR-----DLLErvgLGkRLTHTP-RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRldelsELLD---LE-ELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDER-LAHRCRRLIRLEGGRLVA 223
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLY 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-204 |
4.70e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarvraeHVGFVFQSFQLL 99
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR------DICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVM--LPMELEGRKDAREKARDLLERV---GLGKRLTHtprQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:PRK11432 91 PHMSLGENVGygLKMLGVPKEERKQRVKEALELVdlaGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190
....*....|....*....|....*....|
gi 492156113 175 DSHTGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:PRK11432 168 DANLRRSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-227 |
8.23e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 98.72 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEgdLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGS---VILSGRNLSEld 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSK--KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 eDQRARVRaEHVGFVFQS--FQLL------DSLNALENVMLPmelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQ 149
Cdd:PRK13640 77 -KTVWDIR-EKVGIVFQNpdNQFVgatvgdDVAFGLENRAVP-----RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-209 |
8.58e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAG------LDLPSAGSVILSGRNLSELDEdqrARVRAEhVGFVFQ 94
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiydSKIKVDGKVLYFGKDIFQIDA---IKLRKE-VGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQLLDSLNALENVMLPMELEGRKDAREKAR---DLLERVGLGK----RLTHTPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKiveECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 492156113 168 DEPTGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHR 209
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVAR 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-223 |
9.20e-25 |
|
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: 95.84 E-value: 9.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDqrarvR 85
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQSFQLLDSlnalenvmlpmelegrkdarekarDLLERVGlgkrlthtpRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03247 74 SSLISVLNQRPYLFDT------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-222 |
9.46e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVV-PSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:COG1101 1 MLELKNLSKTFnPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 vraeHVGFVFQsfqllD-------SLNALENVMLPMeLEGR---------KDAREKARDLLERVGLG--KRLTHTPRQLS 145
Cdd:COG1101 81 ----YIGRVFQ-----DpmmgtapSMTIEENLALAY-RRGKrrglrrgltKKRRELFRELLATLGLGleNRLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRC-RRLIRLEGGRLV 222
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-222 |
9.80e-25 |
|
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: 96.88 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEgdltILHELSLELNKGdTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldedQRARVR 85
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AeHVGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARvdEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELNKERntTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-222 |
1.32e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 96.08 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPS--TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA--GSVILSGRNLSElded 79
Cdd:cd03213 2 VTLSFRNLTVTVKSspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 qraRVRAEHVGFVFQSFQLLDSLNALENVMLPMELegrkdarekardllervglgkrlthtpRQLSGGEQQRVAIARAFA 159
Cdd:cd03213 78 ---RSFRKIIGYVPQDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 160 ADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDER--LAHRCRRLIRLEGGRLV 222
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQGRVI 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-223 |
1.45e-24 |
|
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: 96.97 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraEHVGFVFQSFQLL 99
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIAR---LGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELegRKDAREKARDLlERVG-----LGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTgnl 174
Cdd:COG0410 91 PSLTVEENLLLGAYA--RRDRAEVRADL-ERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS--- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 175 dshTG------ERISDLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:COG0410 165 ---LGlaplivEEIFEIIRRLNRE-GVTILLVEQNARFALEiADRAYVLERGRIVL 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-221 |
1.81e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLA---GLDLPSAGSVILSGRNLS---EL 76
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTVQregRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DEDQRaRVRAeHVGFVFQSFQLLDSLNALENVML------PMELEG----RKDAREKARDLLERVGLGKRLTHTPRQLSG 146
Cdd:PRK09984 78 ARDIR-KSRA-NTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCfswfTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRL 221
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-222 |
4.00e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 97.67 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS----AGSVILSGRNLSELDEDQ 80
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQ-LLDS----LNALENVMLPMELEGR-----KDAREKARDLLERVGLGKR---LTHTPRQLSGG 147
Cdd:COG4170 83 RRKIIGREIAMIFQEPSsCLDPsakiGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHkdiMNSYPHELTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 148 EQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVLYCGQTV 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-227 |
5.43e-24 |
|
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: 99.11 E-value: 5.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTE-GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSV-ILSGR---NLSELD 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDewvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 EDQRARVRaEHVGFVFQSFQLLDSLNALENVM------LPMELegrkdAREKARDLLERVGLGKR-----LTHTPRQLSG 146
Cdd:TIGR03269 357 PDGRGRAK-RYIGILHQEYDLYPHRTVLDNLTeaigleLPDEL-----ARMKAVITLKMVGFDEEkaeeiLDKYPDELSE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAPQ 225
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIVKIG 510
|
..
gi 492156113 226 EP 227
Cdd:TIGR03269 511 DP 512
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-222 |
5.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 5.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKV-VPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeldeDQRAR---V 84
Cdd:PRK13637 6 ENLTHIyMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT----DKKVKlsdI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEhVGFVFQ--SFQLLDSLNALENVMLPMEL-EGRKDAREKARDLLERVGLGKR--LTHTPRQLSGGEQQRVAIARAFA 159
Cdd:PRK13637 82 RKK-VGLVFQypEYQLFEETIEKDIAFGPINLgLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 160 ADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-221 |
5.80e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.93 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 27 ELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQSFQLLDSLNALE 106
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 107 NVMLPME--LEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISD 184
Cdd:TIGR01277 90 NIGLGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 492156113 185 LLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRL 221
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-222 |
1.21e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILsGRNLseldedqrarv 84
Cdd:COG0488 315 VLELEGLSK----SYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raeHVGFVFQSFQLLD-SLNALENVMlpmelEGRKDAREK-ARDLLERVGLGKRLTHTP-RQLSGGEQQRVAIARAFAAD 161
Cdd:COG0488 379 ---KIGYFDQHQEELDpDKTVLDELR-----DGAPGGTEQeVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLL--FElnkernTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALddFP------GTVLLVSHDRYFLDRvATRILEFEDGGVR 508
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-216 |
1.25e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.45 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVilsgrnlseldedqrARVRAEHVGFVFQSFQLL 99
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNA--LENVML----PMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:NF040873 68 DSLPLtvRDLVAMgrwaRRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 172 GNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHRCRRLIRL 216
Cdd:NF040873 148 TGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-221 |
1.36e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.02 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQSFQLL 99
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRvnQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDE----RLAHrcrRLIRLEGGRL 221
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQveamTLAD---KIVVLDAGRV 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-216 |
2.31e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRarvraEHVGFVFQSFQL 98
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYR-----QQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLnaLENVMLPMELEGRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:PRK10247 93 FgDTV--YDNLIFPWQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492156113 177 HTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRL 216
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-227 |
2.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraEHVGFVFQS--FQLL--- 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIR---KLVGIVFQNpeTQFVgrt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 ---DSLNALENVMLP-MELEGRKDarekaRDLLErVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:PRK13644 95 veeDLAFGPENLCLPpIEIRKRVD-----RALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 176 SHTGERISDLLFELNkERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13644 169 PDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-227 |
3.43e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPstegDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQR 81
Cdd:PRK10575 8 SDTTFALRNVSFRVP----GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARvraeHVGFVFQSFQLLDSLNALENVML-------PMELEGRKDaREKARDLLERVGL---GKRLTHTprqLSGGEQQR 151
Cdd:PRK10575 84 AR----KVAYLPQQLPAAEGMTVRELVAIgrypwhgALGRFGAAD-REKVEEAISLVGLkplAHRLVDS---LSGGERQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 152 VAIARAFAADPHVLFADEPTGNLD-SHTGERISdLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLA-LVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTP 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-222 |
3.99e-23 |
|
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: 93.37 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrARVRAEHVGFVFQSFQLLD 100
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWLRSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 -SLnaLENVML---PMELEGRKDAREKA------RDLLERVG--LGKRLThtprQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:cd03249 91 gTI--AENIRYgkpDATDEEVEEAAKKAnihdfiMSLPDGYDtlVGERGS----QLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 169 EPTGNLDSHTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMKGR-TTIV-------IAHRlstirnADLIAVLQNGQVV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-209 |
5.07e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTEGDLT-------ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLS 74
Cdd:PRK10261 310 GEPILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 75 ELDEDQRARVRAEhVGFVFQS-FQLLDSLNAL-ENVMLPMELEGR---KDAREKARDLLERVGLgkRLTHT---PRQLSG 146
Cdd:PRK10261 390 TLSPGKLQALRRD-IQFIFQDpYASLDPRQTVgDSIMEPLRVHGLlpgKAAAARVAWLLERVGL--LPEHAwryPHEFSG 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHR 209
Cdd:PRK10261 467 GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDmavvERISHR 533
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-203 |
7.44e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.08 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSV-----ILSGRN---- 72
Cdd:PRK10261 9 ARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSrqvi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 73 -LSELDEDQRARVRAEHVGFVFQsfQLLDSLNAL--------ENVMLPMELeGRKDAREKARDLLERVGLGKR---LTHT 140
Cdd:PRK10261 89 eLSEQSAAQMRHVRGADMAMIFQ--EPMTSLNPVftvgeqiaESIRLHQGA-SREEAMVEAKRMLDQVRIPEAqtiLSRY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 141 PRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-203 |
1.02e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.00 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 29 SLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEhVGFVFQSfqLLDSLNALENV 108
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQD--PLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 109 --MLPMELE------GRKDAREKARDLLERVGLGKRLTHT-PRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTG 179
Cdd:PRK15079 118 geIIAEPLRtyhpklSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180
....*....|....*....|....
gi 492156113 180 ERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-221 |
1.34e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 8 AQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRN----LS---ELDEDQ 80
Cdd:COG0488 1 LENLSKSF----GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPqepPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARvraehvGFVFQSF----QLLDSLNALENVMLPMELEGRK--------------DAREKARDLLERVGLGKRLTHTP- 141
Cdd:COG0488 77 TVL------DTVLDGDaelrALEAELEELEAKLAEPDEDLERlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLfelnKERNTTLVLVTHDeR--LAHRCRRLIRLEGG 219
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHD-RyfLDRVATRILELDRG 225
|
..
gi 492156113 220 RL 221
Cdd:COG0488 226 KL 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-222 |
1.82e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.68 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLP----SAGSVILSGRNLSEldedqrARVRAEHVGFVFQ 94
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP------CALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQllDSLNALENvMLPMELE-----GRKDAREKARDLLERVGLGKR---LTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:PRK10418 87 NPR--SAFNPLHT-MHTHAREtclalGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD----ERLAHrcrRLIRLEGGRLV 222
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmgvvARLAD---DVAVMSHGRIV 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-209 |
2.69e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLD--LPS---AGSVILSGRNLSE 75
Cdd:PRK14239 1 MTEPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEvtiTGSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 76 LDEDQrARVRAEhVGFVFQS---FqlldSLNALENVMLPMELEGRKDaREKARDLLERVGLG--------KRLTHTPRQL 144
Cdd:PRK14239 77 PRTDT-VDLRKE-IGMVFQQpnpF----PMSIYENVVYGLRLKGIKD-KQVLDEAVEKSLKGasiwdevkDRLHDSALGL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 145 SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHR 209
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASR 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-222 |
2.91e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.42 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQLLDSlN 103
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR-QFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEGRKDAREKARDLLE--------RVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:TIGR01193 564 ILENLLLGAKENVSQDEIWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492156113 176 SHTGERISDLLFELNKErntTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-222 |
6.20e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.69 E-value: 6.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldeDQRARVRaeHVGFVF-QSFQLLDSLN 103
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK---RRKEFAR--RIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEG--RKDAREKARDLLERVGLGKrLTHTP-RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:COG4586 113 AIDSFRLLKAIYRipDAEYKKRLDELVELLDLGE-LLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 181 RISDLLFELNKERNTTLVLVTHD----ERLahrCRRLIRLEGGRLV 222
Cdd:COG4586 192 AIREFLKEYNRERGTTILLTSHDmddiEAL---CDRVIVIDHGRII 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-222 |
7.27e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.10 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQLLDSLNA 104
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 lENVMLpmeleGRKDA----------REKARDLLER--VGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:PRK13657 427 -DNIRV-----GRPDAtdeemraaaeRAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 173 NLDSHTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKGR-TTFI-------IAHRlstvrnADRILVFDNGRVV 548
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-227 |
9.40e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.07 E-value: 9.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPS-TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSV----ILSGRNLSELDED 79
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRARVRA--------EHVGFVFQ--SFQLL-DSLNalENVML-PMELEGRK-DAREKARDLLERVGLGKR-LTHTPRQLS 145
Cdd:PRK13631 101 TNPYSKKiknfkelrRRVSMVFQfpEYQLFkDTIE--KDIMFgPVALGVKKsEAKKLAKFYLNKMGLDDSyLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPTGNLDShTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAP 224
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKILKT 257
|
...
gi 492156113 225 QEP 227
Cdd:PRK13631 258 GTP 260
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-223 |
1.24e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 89.12 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraEHVGFVFQSFQLL 99
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDAREKA---------RDLLERVGlGkrlthtprQLSGGEQQRVAIARAFAADPHVLFADEP 170
Cdd:TIGR03410 88 PRLTVEENLLTGLAALPRRSRKIPDeiyelfpvlKEMLGRRG-G--------DLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 171 TGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRC-RRLIRLEGGRLVA 223
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVVA 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
1.36e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPStegdLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLsELDEDQ 80
Cdd:COG3845 1 MMPPALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RArvRAEHVGFVFQSFQLLDSLNALENVMLPME-----LEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIA 155
Cdd:COG3845 76 DA--IALGIGMVHQHFMLVPNLTVAENIVLGLEptkggRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 156 RAFAADPHVLFADEPTGNLdshTGERISDLLFELN--KERNTTLVLVTH--DE--RLAHRC---RRlirlegGRLVA 223
Cdd:COG3845 154 KALYRGARILILDEPTAVL---TPQEADELFEILRrlAAEGKSIIFITHklREvmAIADRVtvlRR------GKVVG 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-175 |
1.70e-21 |
|
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: 88.75 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTegdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVr 85
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPH 163
Cdd:cd03218 76 --GIGYLPQEASIFRKLTVEENILAVLEIRGlsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170
....*....|..
gi 492156113 164 VLFADEPTGNLD 175
Cdd:cd03218 154 FLLLDEPFAGVD 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
1.75e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.91 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVR-AEHVGFVFQS--FQLLdS 101
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK---PIDYSRKGLMKlRESVGMVFQDpdNQLF-S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 102 LNALENVML-PMELE-GRKDAREKARDLLERVGLgKRLTHTPRQ-LSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHT 178
Cdd:PRK13636 98 ASVYQDVSFgAVNLKlPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 179 GERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVI 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-222 |
1.82e-21 |
|
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: 92.19 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELdedQRARVRAeHVGFVFQSFQL 98
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV---TQASLRA-AIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLnaLENVmlpmeLEGRKDA-REKARDLLERVGLGKRLTHTPRQ-----------LSGGEQQRVAIARAFAADPHVL 165
Cdd:COG5265 444 FnDTI--AYNI-----AYGRPDAsEEEVEAAARAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVARGR-TTLV-------IAHRlstivdADEILVLEAGRIV 571
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-221 |
2.33e-21 |
|
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: 91.64 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvr 85
Cdd:TIGR01842 317 LSVENVTIVPP--GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLDSLNAlENVMlpmELEGRKDAR---EKAR-----DLLERVGLGKRLTHTPR--QLSGGEQQRVAIA 155
Cdd:TIGR01842 393 --HIGYLPQDVELFPGTVA-ENIA---RFGENADPEkiiEAAKlagvhELILRLPDGYDTVIGPGgaTLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-223 |
2.47e-21 |
|
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: 90.56 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 27 ELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSE------LDEDQRArvraehVGFVFQSFQLLD 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR------IGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVmlpmeLEGRKDAREKARD-----LLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:TIGR02142 89 HLSVRGNL-----RYGMKRARPSERRisferVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 176 SHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGRVAA 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-222 |
3.09e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHE-----LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehVGFVFQS 95
Cdd:PRK10771 6 DITWLYHhlpmrFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 96 FQLLDSLNALENVMLPME--LEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:PRK10771 80 NNLFSHLTVAQNIGLGLNpgLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 174 LDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIA 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-226 |
3.32e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSkvvpSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:PRK11231 1 MTLRTENLT----VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 vraeHVGFVFQSFQLLDSLNALENVML---P-MELEGRKDAREKAR--DLLERVGLG----KRLThtprQLSGGEQQRVA 153
Cdd:PRK11231 77 ----RLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARvnQAMEQTRINhladRRLT----DLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 154 IARAFAADPHVLFADEPTGNLD-SHTGErISDLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA---PQE 226
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDiNHQVE-LMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHVMAqgtPEE 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-227 |
3.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQ--SFQLLDSl 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVMLPMELEG--RKDAREKARDLLERVGLGKRL-THTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTG 179
Cdd:PRK13649 102 TVLKDVAFGPQNFGvsQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 180 ERISDLLFELNkERNTTLVLVTH--DErLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13649 182 KELMTLFKKLH-QSGMTIVLVTHlmDD-VANYADFVYVLEKGKLVLSGKP 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-227 |
3.56e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSG----RNLSELDEDQRARvraEHVGFVFQ--SFQL 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLR---KEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSLNALENVMLPMEL-EGRKDAREKARDLLERVGLGKR-LTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:PRK13645 104 FQETIEKDIAFGPVNLgENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 177 HTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-223 |
4.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrarVRAEhVGFVFQS--FQLLdSL 102
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VRSK-VGLVFQDpdDQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVML-PMELE-GRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:PRK13647 96 TVWDDVAFgPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 181 RISDLLFELNKErNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVLA 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-227 |
4.95e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.09 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldedq 80
Cdd:PRK13537 3 MSVAPIDFRNVEK----RYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:PRK13537 74 RARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGlsAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 159 AADPHVLFADEPTGNLDSHTG----ERISDLLfelnkERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARhlmwERLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAP 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-221 |
5.25e-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: 87.53 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRA 82
Cdd:cd03248 9 KGIVKFQNVTFAYP-TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 RVraehVGFVFQSFQLLdSLNALENV---MLPMELEGRKDAREK--ARDLLERVGLGKRLTHTPR--QLSGGEQQRVAIA 155
Cdd:cd03248 88 SK----VSLVGQEPVLF-ARSLQDNIaygLQSCSFECVKEAAQKahAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDLLFELNkeRNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-203 |
5.60e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 18 TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRaEHVGFVFQSFQ 97
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLDSLNALENVMLPMELEGRKDA---REKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:PRK11831 95 LFTDMNVFDNVAYPLREHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180
....*....|....*....|....*....
gi 492156113 175 DSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-205 |
6.09e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 87.33 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLpsaGSVILSGRNLSELDEDQRARVRaEHVGFVFQSFQLLDSLN 103
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE---GGGTTSGQILFNGQPRKPDQFQ-KCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEGRKDAREKARDLLERVGLGKRLTHTP------RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRiggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....*...
gi 492156113 178 TGERISDLLFELNKeRNTTLVLVTHDER 205
Cdd:cd03234 178 TALNLVSTLSQLAR-RNRIVILTIHQPR 204
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-205 |
7.79e-21 |
|
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: 87.33 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARV 84
Cdd:TIGR04406 1 TLVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raeHVGFVFQSFQLLDSLNALENVMLPMELEGRKDA---REKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAAD 161
Cdd:TIGR04406 77 ---GIGYLPQEASIFRKLTVEENIMAVLEIRKDLDRaerEERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDER 205
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVR 196
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-222 |
1.09e-20 |
|
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: 86.77 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRAEhVGFVFQSfQLLDSLN 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLRRQ-VGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVML-----PME--LEGRK--DAREKARDLLErvGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:cd03252 92 IRDNIALadpgmSMErvIEAAKlaGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492156113 175 DSHTGERISDLLFELNKERntTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:cd03252 170 DYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-223 |
1.21e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.43 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELdedqrarvrAEHVGFvfqsfqlL 99
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL---------GLGGGF-------N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLtHTP-RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:cd03220 97 PELTGRENIYLNGRLLGlsRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492156113 177 HTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVA 223
Cdd:cd03220 176 AFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-206 |
1.25e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RAR---VRAehvgfvFQSFQLLDSLNALENVML-----------------PMELEGRKDAREKARDLLERVGLGKRLTHT 140
Cdd:PRK11300 77 IARmgvVRT------FQHVRLFREMTVIENLLVaqhqqlktglfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 141 PRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERL 206
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-227 |
1.31e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHVGFVFQ--SFQLLDSL 102
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVMLPMELEGRKDAREK-ARDLLERVGLGKRL-THTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTge 180
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA-- 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 181 RISDL-LFELNKERNTTLVLVTH-DERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13643 180 RIEMMqLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-227 |
1.52e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.48 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTllgllagldlpsagsvILsgRNLSELDEDQRARVR---AEHVGFVFQ-SFQL 98
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKST----------------LL--RAIAGLWPYGSGRIArpaGARVLFLPQrPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSLnaLENVMLPMELEGRKDARekARDLLERVGLGK---RL---THTPRQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:COG4178 439 LGTL--REALLYPATAEAFSDAE--LREALEAVGLGHlaeRLdeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 173 NLDSHTGERISDLLfeLNKERNTTLVLVTHDERLAHRCRRLIRLEG---GRLVAPQEP 227
Cdd:COG4178 515 ALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLELTGdgsWQLLPAEAP 570
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-223 |
2.33e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESIlSAQNLSK------------------VVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS 62
Cdd:COG1134 1 MSSMI-EVENVSKsyrlyhepsrslkelllrRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 63 AGSVILSGRNLSELDedqrarvraehVGFVFQSfqlldSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLtHT 140
Cdd:COG1134 80 SGRVEVNGRVSALLE-----------LGAGFHP-----ELTGRENIYLNGRLLGlsRKEIDEKFDEIVEFAELGDFI-DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 141 P-RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDER-LAHRCRRLIRLEG 218
Cdd:COG1134 143 PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGaVRRLCDRAIWLEK 221
|
....*
gi 492156113 219 GRLVA 223
Cdd:COG1134 222 GRLVM 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-222 |
2.69e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLskVVPSTEGDlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDlPSAGSVILSGRNLSELDEDQRARvr 85
Cdd:PRK11174 350 IEAEDL--EILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRK-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVFQSFQLLD-SLnaLENVMLpmeleGRKDAR-EKARDLLERVGLG---KRLTH---TPRQ-----LSGGEQQRV 152
Cdd:PRK11174 424 --HLSWVGQNPQLPHgTL--RDNVLL-----GNPDASdEQLQQALENAWVSeflPLLPQgldTPIGdqaagLSVGQAQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNkeRNTTLVLVTHdeRLA--HRCRRLIRLEGGRLV 222
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTH--QLEdlAQWDQIWVMQDGQIV 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-222 |
5.20e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLLd 100
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR----QVALVGQEPVLF- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVML-----PMElEGRKDAREK-ARDLLERV--GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:TIGR00958 568 SGSVRENIAYgltdtPDE-EIMAAAKAAnAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 173 NLDShtgeRISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:TIGR00958 647 ALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-205 |
9.03e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 84.31 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRA 82
Cdd:COG1137 1 MMTLEAENLVK----SYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 RvraEHVGF------VFQSfqlldsLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAI 154
Cdd:COG1137 77 R---LGIGYlpqeasIFRK------LTVEDNILAVLELRKlsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTlVLVT-HDER 205
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIG-VLITdHNVR 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-223 |
1.06e-19 |
|
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: 83.57 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARV 84
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raehvGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:cd03266 81 -----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 163 HVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD----ERLahrCRRLIRLEGGRLVA 223
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImqevERL---CDRVVVLHRGRVVY 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-202 |
1.33e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS---AGSVILSGRNLsELDEdQRARVraehvGFVFQSFQLL 99
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKE-MRAIS-----AYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELE-----GRKDAREKARDLLERVGLGK---RLTHTP---RQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRmprrvTKKEKRERVDEVLQALGLRKcanTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 169 EPTGNLDSHTGERISDLLFELnKERNTTLVLVTH 202
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIH 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-227 |
1.88e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQSFQLL 99
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVM------LPMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:PRK10253 94 GDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 174 LDSHTGERISDLLFELNKERNTTLVLVTHDerLAHRCR---RLIRLEGGRLVAPQEP 227
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYTLAAVLHD--LNQACRyasHLIALREGKIVAQGAP 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-223 |
3.00e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTlLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRAEHV-----GFVFQSFQLLDsl 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST-LLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSqqqspPFAMPVFQYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 nalenvmLPMELEGRKDAREKA-RDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF-----AADPH--VLFADEPTGNL 174
Cdd:COG4138 92 -------LHQPAGASSEAVEQLlAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 175 DSHTGERISDLLFELnKERNTTLVLVTHDerLAHRCR---RLIRLEGGRLVA 223
Cdd:COG4138 165 DVAQQAALDRLLREL-CQQGITVVMSSHD--LNHTLRhadRVWLLKQGKLVA 213
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-222 |
3.51e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.54 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTEGDltILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldEDQRARVR 85
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL----ADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQSFQLLDSLNAlENVML-PMELEGRKDAREKAR-----DLLERVGLGkrlTHTP-----RQLSGGEQQRVAI 154
Cdd:TIGR02203 405 RRQVALVSQDVVLFNDTIA-NNIAYgRTEQADRAEIERALAaayaqDFVDKLPLG---LDTPigengVLLSGGQRQRLAI 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 155 ARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERnTTLVlvthderLAHR------CRRLIRLEGGRLV 222
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGR-TTLV-------IAHRlstiekADRIVVMDDGRIV 546
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-227 |
9.98e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrARVRAEHVGFVFQSFQLl 99
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----ARAASRRVASVPQDTSL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 dSLNALENVMLPM-------ELEGRKDAREKA-RDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:PRK09536 89 -SFEFDVRQVVEMgrtphrsRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 172 GNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK09536 168 ASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPP 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-227 |
1.34e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 15 VPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGrnlseLDEDQRARVRAEHVGFVFQ 94
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG-----VPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQLLDSLNALENVMLpmelEGRKdAREKARD-------LLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:PRK13536 122 FDNLDLEFTVRENLLV----FGRY-FGMSTREieavipsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 168 DEPTGNLDSHTG----ERISDLLfelnkERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK13536 197 DEPTTGLDPHARhliwERLRSLL-----ARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRP 256
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-222 |
1.93e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGL----LAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAicgvTKDNWRVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQllDSLNALENVMLPM-------ELEGRKDAR-----EKARDLLERVGLG--KRLTHT-PRQLS 145
Cdd:PRK15093 83 RRKLVGHNVSMIFQEPQ--SCLDPSERVGRQLmqnipgwTYKGRWWQRfgwrkRRAIELLHRVGIKdhKDAMRSfPYELT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYCGQTV 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-223 |
2.78e-18 |
|
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: 78.62 E-value: 2.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVPSTegdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldedqrarvr 85
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aehvgfvfqsfqlldslnalenvmlPMELEGRKDAREkardllervgLGKRLTHtprQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03216 63 -------------------------EVSFASPRDARR----------AGIAMVY---QLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH--DERLAHrCRRLIRLEGGRLVA 223
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEVFEI-ADRVTVLRDGRVVG 162
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-222 |
6.92e-18 |
|
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: 78.41 E-value: 6.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDqrarvr 85
Cdd:cd03268 1 LKTNDLTK----TYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQSFQLLDSLNALENVMLPMELEGRKDARekARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR--IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRLIRLEGGRLV 222
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADRIGIINKGKLI 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-203 |
8.26e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.78 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVRaEHVGFVFQS--FQLL-- 99
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIR-HKIGMVFQNpdNQFVga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 ----DSLNALENVMLPmelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:PRK13650 98 tvedDVAFGLENKGIP-----HEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180
....*....|....*....|....*...
gi 492156113 176 SHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHD 200
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-223 |
8.34e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 8.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELN-----KGDTlAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSelDEDQRARVRAE--HVGFVFQSFQ 97
Cdd:PRK11144 10 LGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEKGICLPPEkrRIGYVFQDAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLDSLNALENVMLPMelegRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:PRK11144 87 LFPHYKVRGNLRYGM----AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTH--DE--RLAHrcrRLIRLEGGRLVA 223
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHslDEilRLAD---RVVVLEQGKVKA 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-220 |
9.11e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 76.72 E-value: 9.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNlseldedqrarvr 85
Cdd:cd03221 1 IELENLSK----TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aeHVGFVfqsfqlldslnalenvmlpmelegrkdarekardllervglgkrlthtpRQLSGGEQQRVAIARAFAADPHVL 165
Cdd:cd03221 64 --KIGYF-------------------------------------------------EQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 166 FADEPTGNLDSHTGERISDLLfelnKERNTTLVLVTHDER-LAHRCRRLIRLEGGR 220
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-222 |
1.13e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAG-----SVILSGRNLSELDEDQRARVRaehVGFVFQSFQ 97
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRR---VGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 98 LLdSLNALENVMLPM---ELEGRKDAREKARDLLERVGL----GKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEP 170
Cdd:PRK14271 112 PF-PMSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 171 TGNLDSHTGERISDLLFELNKErnTTLVLVTHDERLAHRCR-RLIRLEGGRLV 222
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISdRAALFFDGRLV 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-220 |
1.22e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.27 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 10 NLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraehV 89
Cdd:PRK11650 5 KLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD------I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 90 GFVFQSFQLLDSLNALENvmlpME--LEGRK------DAR-EKARDLLErvgLGKRLTHTPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN----MAygLKIRGmpkaeiEERvAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 161 DPHVLFADEPTGNLDSHTgeRISDLL--FELNKERNTTLVLVTHDE----RLAHrcrRLIRLEGGR 220
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKL--RVQMRLeiQRLHRRLKTTSLYVTHDQveamTLAD---RVVVMNGGV 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-202 |
1.45e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ 80
Cdd:PRK09700 1 MATPYISMAGIGK----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVraeHVGFVFQSFQLLDSLNALENVMLpmeleGR--------------KDAREKARDLLERVGLGKRLTHTPRQLSG 146
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYI-----GRhltkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLdshTGERISDLLFELNKERN--TTLVLVTH 202
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQLRKegTAIVYISH 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-201 |
1.94e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.68 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEG-----DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD 77
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 78 edqrARVRAEHVGFVFQSFQllDSLNALENVM----LPMEL--EGRKDAREKA-RDLLERVGL-GKRLTHTPRQLSGGEQ 149
Cdd:PRK15112 82 ----YSYRSQRIRMIFQDPS--TSLNPRQRISqildFPLRLntDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVT 201
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-222 |
2.19e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTEGDL-------TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDlPSAGSVILSGRNLS 74
Cdd:PRK15134 272 ASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLH 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 75 ELDEDQRARVRaEHVGFVFQSFQllDSLNALENVMLPMElEG--------RKDARE-KARDLLERVGLGKRLTHT-PRQL 144
Cdd:PRK15134 351 NLNRRQLLPVR-HRIQVVFQDPN--SSLNPRLNVLQIIE-EGlrvhqptlSAAQREqQVIAVMEEVGLDPETRHRyPAEF 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 145 SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVV 505
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-209 |
2.59e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLG--LLAGLDLPSA---GSVILSGRNLSEL 76
Cdd:PRK14243 7 TETVLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfNRLNDLIPGFrveGKVTFHGKNLYAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DEDQrARVRaEHVGFVFQS---FqlldSLNALENVMLPMELEGRK-DAREKARDLLERVGLGKRLTHTPRQ----LSGGE 148
Cdd:PRK14243 83 DVDP-VEVR-RRIGMVFQKpnpF----PKSIYDNIAYGARINGYKgDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 149 QQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERnTTLVLVTHDERLAHR 209
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQ-YTIIIVTHNMQQAAR 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-202 |
3.87e-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: 80.06 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNL-SELDEdqrarVRaEHVGFVFQSFQLLDSLNALE 106
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA-----VR-QSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 107 NVMLPMELEGR--KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISD 184
Cdd:TIGR01257 1023 HILFYAQLKGRswEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170
....*....|....*...
gi 492156113 185 LLFELNKERntTLVLVTH 202
Cdd:TIGR01257 1103 LLLKYRSGR--TIIMSTH 1118
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
4.26e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSkvvpSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELdedQ 80
Cdd:PRK11614 1 MEKVMLSFDKVS----AHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAEHVGFVFQSFQLLDSLNALENVMLPMELEGRKDAREKAR---DLLERvgLGKRLTHTPRQLSGGEQQRVAIARA 157
Cdd:PRK11614 74 TAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKwvyELFPR--LHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 158 FAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-218 |
6.70e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVvpstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNlselDEDQRARVR 85
Cdd:PRK13539 3 LEGEDLACV----RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD----IDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGfvFQSFqLLDSLNALENVMLPMELEGRKDARekARDLLERVGLGkRLTHTP-RQLSGGEQQRVAIARAFAADPHV 164
Cdd:PRK13539 75 CHYLG--HRNA-MKPALTVAENLEFWAAFLGGEELD--IAAALEAVGLA-PLAHLPfGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 165 LFADEPTGNLDSHTGERISDLLFElNKERNTTLVLVTHDErLAHRCRRLIRLEG 218
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHIP-LGLPGARELDLGP 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-221 |
1.10e-16 |
|
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: 74.78 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSkvVPSTegdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRarv 84
Cdd:cd03215 4 VLEVRGLS--VKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEHVGFV---FQSFQLLDSLNALENVMLPmelegrkdarekardllervglgkrlthtpRQLSGGEQQRVAIARAFAAD 161
Cdd:cd03215 73 IRAGIAYVpedRKREGLVLDLSVAENIALS------------------------------SLLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-220 |
1.58e-16 |
|
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: 74.81 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldedqrarvraehVGFVFQSFQLLdslN 103
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-----------------IAYVSQEPWIQ---N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 A--LENVMLPMELEgrkdaREKARDLLERVGLGKRLTHTPRQ-----------LSGGEQQRVAIARAFAADPHVLFADEP 170
Cdd:cd03250 80 GtiRENILFGKPFD-----EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 171 TGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGR 220
Cdd:cd03250 155 LSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-209 |
1.73e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldEDQRARVRAEHVGFVFQSFQLLDSLNA 104
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL----RDYTLASLRNQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 lENVMLPMELE-GRKDAREKAR-----DLLERV--GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDS 176
Cdd:PRK11176 435 -NNIAYARTEQySREQIEEAARmayamDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190
....*....|....*....|....*....|...
gi 492156113 177 HTGERISDLLFELNKERnTTLVlvthderLAHR 209
Cdd:PRK11176 514 ESERAIQAALDELQKNR-TSLV-------IAHR 538
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-207 |
1.78e-16 |
|
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: 74.49 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLL--AGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 vraehVGfVFQSFQlldslnalenvmLPMELEGRKDArekarDLLERVGLGkrlthtprqLSGGEQQRVAIARAFAADPH 163
Cdd:cd03217 77 -----LG-IFLAFQ------------YPPEIPGVKNA-----DFLRYVNEG---------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 164 VLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERLA 207
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLL 167
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-227 |
2.57e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPSTegdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:PRK10895 2 ATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 vraEHVGFVFQSFQLLDSLNALENVMLPMELegRKD-----AREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:PRK10895 78 ---RGIGYLPQEASIFRRLSVYDNLMAVLQI--RDDlsaeqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELnkeRNTTL-VLVT-HDER-LAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL---RDSGLgVLITdHNVReTLAVCERAYIVSQGHLIAHGTP 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-202 |
3.26e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEdqraRVRAEHVGFVFQSFQLL 99
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH----SVLRQGVAMVQQDPVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 -DSLNAleNVMLpmeleGRKDAREKARDLLERV-----------GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:PRK10790 428 aDTFLA--NVTL-----GRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190
....*....|....*....|....*....|....*
gi 492156113 168 DEPTGNLDSHTGERISDLLFELNKerNTTLVLVTH 202
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALAAVRE--HTTLVVIAH 533
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-213 |
3.52e-16 |
|
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: 73.93 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVvpstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDqrarvR 85
Cdd:TIGR01189 1 LAARNLACS----RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQSFQLLDSLNALENVMLPMELEGrkDAREKARDLLERVGLgKRLTHTP-RQLSGGEQQRVAIARAFAADPHV 164
Cdd:TIGR01189 72 HENILYLGHLPGLKPELSALENLHFWAAIHG--GAQRTIEDALAAVGL-TGFEDLPaAQLSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 492156113 165 LFADEPTGNLDShTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRL 213
Cdd:TIGR01189 149 WILDEPTTALDK-AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEAREL 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-203 |
4.03e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.73 E-value: 4.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 9 QNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeH 88
Cdd:COG4604 5 KNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 89 VGFVFQSFQLLDSLNALENVMLpmeleGR---------KDAREKARDLLERVGL----GKRLThtprQLSGGEQQRVAIA 155
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAF-----GRfpyskgrltAEDREIIDEAIAYLDLedlaDRYLD----ELSGGQRQRAFIA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-206 |
5.76e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.95 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLL--AGLDLPSAGSVILSGRNLSELDEDQRAR 83
Cdd:COG0396 1 LEIKNLHVSV----EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 VraehvGfVFQSFQ---------LLDSLNALENVMLPMELEGRkDAREKARDLLERVGLGKRLTHtpRQL----SGGEQQ 150
Cdd:COG0396 77 A-----G-IFLAFQypveipgvsVSNFLRTALNARRGEELSAR-EFLKLLKEKMKELGLDEDFLD--RYVnegfSGGEKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 151 RVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHDERL 206
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYQRI 202
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-203 |
6.06e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA-----GSVILSGRNLSELDEDQRaRVRAEhVGFVFQSFQL 98
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLN-RLRRQ-VSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LdSLNALENVML---------PMELEGRKDAREKARDLLERVGlgKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADE 169
Cdd:PRK14258 100 F-PMSVYDNVAYgvkivgwrpKLEIDDIVESALKDADLWDEIK--HKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 170 PTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-227 |
1.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARvraeHVGFVFQS--F 96
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR----KIGMVFQNpdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 97 QLLDSlNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:PRK13642 93 QFVGA-TVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 175 DSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-202 |
4.11e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKVvpstEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvr 85
Cdd:PRK13538 2 LEARNLACE----RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 aehvgfvfqsfQLL---------DSLNALENVMLPMELEGRKDaREKARDLLERVGLGKRLtHTP-RQLSGGEQQRVAIA 155
Cdd:PRK13538 75 -----------DLLylghqpgikTELTALENLRFYQRLHGPGD-DEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492156113 156 RAFAADPHVLFADEPTGNLDSHTGERISDlLFELNKERNTTLVLVTH 202
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEA-LLAQHAEQGGMVILTTH 187
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-223 |
9.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKvvpSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEldedQRARV 84
Cdd:PRK13652 3 LIETRDLCY---SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK----ENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 RAEHVGFVFQSF--QLLDSLNALENVMLPMELeGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAA 160
Cdd:PRK13652 76 VRKFVGLVFQNPddQIFSPTVEQDIAFGPINL-GLDEETVAHRvsSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492156113 161 DPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-203 |
9.90e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 34 KGDTLAIVGASGSGKSTLLGllagldlpsagsvILSGR---NLSELDEDqrarVRAEHVGFVFQSFQLLDSLNALEN--- 107
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVK-------------ILSGElipNLGDYEEE----PSWDEVLKRFRGTELQNYFKKLYNgei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 108 --------V-MLPMELEG-------RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:PRK13409 161 kvvhkpqyVdLIPKVFKGkvrellkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 172 GNLDshTGERI--SDLLFELNKERntTLVLVTHD 203
Cdd:PRK13409 241 SYLD--IRQRLnvARLIRELAEGK--YVLVVEHD 270
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-224 |
1.13e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSkvVPSTEGdLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRA 82
Cdd:COG3845 255 EVVLEVENLS--VRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 RVRAEHVGFV---FQSFQLLDSLNALENVML------PMELEG---RKDAREKARDLLERVGLGKRLTHTP-RQLSGGEQ 149
Cdd:COG3845 329 ERRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrpPFSRGGfldRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH--DERLAHrCRRLIRLEGGRLVAP 224
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEdlDEILAL-SDRIAVMYEGRIVGE 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-204 |
1.96e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKST--LLGLLAGLDLPSAGSVilsgrnlsELDEDQRARVRAehvgfvfqsfqLLD 100
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTllRLLAGALKGTPVAGCV--------DVPDNQFGREAS-----------LID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVMLPMELegrkdarekardlLERVGLG-----KRlthTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:COG2401 105 AIGRKGDFKDAVEL-------------LNAVGLSdavlwLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*....
gi 492156113 176 SHTGERISDLLFELNKERNTTLVLVTHDE 204
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-223 |
2.37e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTlLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVRA-----EHVGFVFQSFQLLDsl 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST-LLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAylsqqQTPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 nalenvmLPMELEGRKDAREKA-RDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF-----AADPH--VLFADEPTGNL 174
Cdd:PRK03695 92 -------LHQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 175 DShTGERISDLLFELNKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVA 223
Cdd:PRK03695 165 DV-AQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLA 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-222 |
2.66e-14 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 69.06 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqRARVRaEHVGFVFQSFQL----- 98
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLR-SRISIIPQDPVLfsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 ---LDSLN---------ALENVMLpmelegrkdareKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:cd03244 95 rsnLDPFGeysdeelwqALERVGL------------KEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 167 ADEPTGNLDSHTGERISDLLFElnKERNTTLVLVTHdeRLAH--RCRRLIRLEGGRLV 222
Cdd:cd03244 163 LDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH--RLDTiiDSDRILVLDKGRVV 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-206 |
2.90e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.76 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVIlsgrnlseldedqraRVRAEHVGFVFQSFQLl 99
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYVPQKLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 dslnaleNVMLPMELEGRKDAREKARD-----LLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNL 174
Cdd:PRK09544 79 -------DTTLPLTVNRFLRLRPGTKKedilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190
....*....|....*....|....*....|..
gi 492156113 175 DSHTGERISDLLFELNKERNTTLVLVTHDERL 206
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-227 |
3.23e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.98 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVRaEHVGFVFQSFQLLDSLNALEN 107
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYR-QLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 108 VMLPmelegrkdarEKARDLLERVGLGKRLTH-----TPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTgERI 182
Cdd:COG4615 427 EADP----------ARARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF-RRV 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492156113 183 --SDLLFELnKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:COG4615 496 fyTELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGP 541
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-203 |
5.33e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAgldlpsaGSVILSGRNLSELDEDQRARVRAEHVGFVFQSFQLLDSL 102
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NAL-ENVML-----PMELEGRKDAREKAR--DLLERVGLgkrLTHTPRQ---LSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:PRK15056 94 PVLvEDVVMmgrygHMGWLRRAKKRDRQIvtAALARVDM---VEFRHRQigeLSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190
....*....|....*....|....*....|..
gi 492156113 172 GNLDSHTGERISDLLFELNKERNTTLVlVTHD 203
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLV-STHN 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-203 |
1.07e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 34 KGDTLAIVGASGSGKSTLLGllagldlpsagsvILSGR---NLSELDEDqrarVRAEHVGFVFQSFQLLDSLNALEN--- 107
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK-------------ILSGElkpNLGDYDEE----PSWDEVLKRFRGTELQDYFKKLANgei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 108 --------V-MLPMELEG-------RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:COG1245 161 kvahkpqyVdLIPKVFKGtvrelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 172 GNLDshTGERI--SDLLFELNKERNTTLVlVTHD 203
Cdd:COG1245 241 SYLD--IYQRLnvARLIRELAEEGKYVLV-VEHD 271
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-203 |
2.50e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 29 SLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILS-GRNLSELDEDQrarvraehvgFVFQSFQLLDSL----N 103
Cdd:PRK15064 21 SVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQ----------FAFEEFTVLDTVimghT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVM--------LP-------M---ELEGR------KDAREKARDLLERVGLGKRLTHTP-RQLSGGEQQRVAIARAF 158
Cdd:PRK15064 91 ELWEVKqerdriyaLPemseedgMkvaDLEVKfaemdgYTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 159 AADPHVLFADEPTGNLDSHTgerISDLLFELNkERNTTLVLVTHD 203
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINT---IRWLEDVLN-ERNSTMIIISHD 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-203 |
5.86e-13 |
|
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: 65.85 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 35 GDTLAIVGASGSGKSTLLGLLAGLDLPSAGSV--------ILSGRNLSEL--------DEDQRARVRAEHVGFVFQSFQl 98
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELqnyftkllEGDVKVIVKPQYVDLIPKAVK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 ldslnalENVmlpMELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDshT 178
Cdd:cd03236 105 -------GKV---GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD--I 172
|
170 180
....*....|....*....|....*..
gi 492156113 179 GERIS--DLLFELNKERNTTLVlVTHD 203
Cdd:cd03236 173 KQRLNaaRLIRELAEDDNYVLV-VEHD 198
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-227 |
5.89e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.39 E-value: 5.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA--------GSVILSGRNLSELDEDQRARVRAehvgFVFQ 94
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRA----VLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 SFQLLDSLNALENVMLPMELEGRKDAREKARD------LLERVGLGKRLTHTPRQLSGGEQQRVAIARAFA--------- 159
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHARRAGALTHRDgeiawqALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 160 ADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHR-CRRLIRLEGGRLVAPQEP 227
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAP 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-223 |
6.02e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPSTEGdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldEDQR 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKA----LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARVRA---EHVGFVFQSFQLLDSLNALENVML---P--MELEGRKDAREKARDLLERVGLgKRLTHTP-RQLSGGEQQRV 152
Cdd:PRK11288 71 ASTTAalaAGVAIIYQELHLVPEMTVAENLYLgqlPhkGGIVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTH--DE--RLahrCRRLIRLEGGRLVA 223
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHrmEEifAL---CDAITVFKDGRYVA 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-216 |
8.50e-13 |
|
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: 64.82 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSEL-DEDQRARVRAEHVGfvfqsfQL 98
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAP------GI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSLNALENvmlpMELEGRKDAREKARDLLERVGLGKrLTHTP-RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03231 85 KTTLSVLEN----LRFWHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492156113 178 TGERISDlLFELNKERNTTLVLVTH-DERLAHRCRRLIRL 216
Cdd:cd03231 160 GVARFAE-AMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-202 |
1.80e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTllgllaGLDLPSA--------GSVILSGrn 72
Cdd:PRK13549 1 MMEYLLEMKNITK----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKST------LMKVLSGvyphgtyeGEIIFEG-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 73 lseldEDQRAR-VR-AEHVGFV--FQSFQLLDSLNALENVMLPMELE--GRKDARE---KARDLLERVGLGKRlTHTP-R 142
Cdd:PRK13549 69 -----EELQASnIRdTERAGIAiiHQELALVKELSVLENIFLGNEITpgGIMDYDAmylRAQKLLAQLKLDIN-PATPvG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 143 QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH 202
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-203 |
2.11e-12 |
|
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: 64.35 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 31 ELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLS----ELDEDQRARVRAehvgFVFQSFQLLDSLNALE 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD----LLSSITKDFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 107 N-VMLPMELEgrkdarekarDLLERvglgkRLThtprQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDL 185
Cdd:cd03237 97 TeIAKPLQIE----------QILDR-----EVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180
....*....|....*....|
gi 492156113 186 L--FELNKERntTLVLVTHD 203
Cdd:cd03237 158 IrrFAENNEK--TAFVVEHD 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-209 |
2.86e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 27 ELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRArvraeHVGFVF------QSFQLLD 100
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL-----ARGLVYlpedrqSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVMLPMELEG--RKDAREKARdlLERV--GLGKRLTH---TPRQLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:PRK15439 356 APLAWNVCALTHNRRGfwIKPARENAV--LERYrrALNIKFNHaeqAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492156113 174 LDSHTGERISDLLFELNKErNTTLVLVTHD----ERLAHR 209
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDleeiEQMADR 472
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-221 |
3.54e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 28 LSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVRAeHVGFVFQSFQLLDSLnalen 107
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRK-LFSAVFTDFHLFDQL----- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 108 vmlpMELEGRKDAREKARDLLERVGLGKRLTH-----TPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:PRK10522 413 ----LGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 492156113 183 SDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-227 |
4.41e-12 |
|
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: 62.81 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARvraehVGFVFQSFQLLDSl 102
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRSS-----LTIIPQDPTLFSG- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 naleNVMLPMELEGRKDAREKARDLlervglgkRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:cd03369 97 ----TIRSNLDPFDEYSDEEIYGAL--------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 492156113 183 SDLLFELNKerNTTLVLVTHDERLAHRCRRLIRLEGGRLVAPQEP 227
Cdd:cd03369 165 QKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-206 |
9.24e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPSTEgdltILHELSLELNKGDTLAIVGASGSGKSTllGLLAGLDLPS----AGSVILSGRNLSEL 76
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKST--LSKVIAGHPAykilEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 77 DEDQRArvraeHVGfVFQSFQLLDSLNALENVMLpmeLEGRKDAREKARDL---------------LERVGLGKRLTHtp 141
Cdd:CHL00131 77 EPEERA-----HLG-IFLAFQYPIEIPGVSNADF---LRLAYNSKRKFQGLpeldplefleiinekLKLVGMDPSFLS-- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 142 RQL----SGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDllfELNKERNTT--LVLVTHDERL 206
Cdd:CHL00131 146 RNVnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAE---GINKLMTSEnsIILITHYQRL 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-171 |
1.55e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSkvvpstegDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEdqRA 82
Cdd:COG1129 254 EVVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSP--RD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 RVRAehvGFVF-----QSFQLLDSLNALENVMLPMeLEG--------RKDAREKARDLLERVGLgKrlTHTPRQ----LS 145
Cdd:COG1129 324 AIRA---GIAYvpedrKGEGLVLDLSIRENITLAS-LDRlsrgglldRRRERALAEEYIKRLRI-K--TPSPEQpvgnLS 396
|
170 180
....*....|....*....|....*.
gi 492156113 146 GGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-202 |
1.55e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.58 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARVRAEhVGFVFQSFQLL 99
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfEATRSRNRYS-VAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSlNALENVML--PMELEGRKDAREKAR-----DLL---ERVGLGKRLTHtprqLSGGEQQRVAIARAFAADPHVLFADE 169
Cdd:cd03290 92 NA-TVEENITFgsPFNKQRYKAVTDACSlqpdiDLLpfgDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 170 PTGNLDSHTGERI-SDLLFELNKERNTTLVLVTH 202
Cdd:cd03290 167 PFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTH 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-222 |
1.63e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTllgllagldlpsagsviLSGRNLSELdEDQRARVRAEH-VGFVFQSFQLLDSl 102
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKST-----------------LLQSLLSQF-EISEGRVWAERsIAYVPQQAWIMNA- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NALENVMLPMElegrkdarEKARDLLERV--------------GLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:PTZ00243 736 TVRGNILFFDE--------EDAARLADAVrvsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 492156113 169 EPTGNLDSHTGERISDLLFeLNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLV 222
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
142-218 |
1.70e-11 |
|
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: 60.25 E-value: 1.70e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLfelnKERNTTLVLVTHDERLAHRCRRLIRLEG 218
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
100-223 |
2.44e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENV-MLPMELE-GRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:NF000106 99 ESFSGRENLyMIGR*LDlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRLVA 223
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-202 |
5.46e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSG--RNLSELDEDQ 80
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKA----LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RArvraeHVGFVFQSFQLLDSLNALENVMLPMELEGR------KDAREKARDLLERVGLgkrlTHTPRQLSG----GEQQ 150
Cdd:PRK10762 78 EA-----GIGIIHQELNLIPQLTIAENIFLGREFVNRfgridwKKMYAEADKLLARLNL----RFSSDKLVGelsiGEQQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 492156113 151 RVAIARAFAADPHVLFADEPTGNL-DSHTgERISDLLFELnKERNTTLVLVTH 202
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIREL-KSQGRGIVYISH 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-202 |
1.41e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 18 TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA--GSVILSGRNL--SELDEDQRARVRAEHvgfvf 93
Cdd:TIGR02633 10 TFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkaSNIRDTERAGIVIIH----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 QSFQLLDSLNALENVMLPMELE---GRKDARE---KARDLLERVGL-GKRLTHTPRQLSGGEQQRVAIARAFAADPHVLF 166
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNEITlpgGRMAYNAmylRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 492156113 167 ADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH 202
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISH 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-203 |
1.93e-10 |
|
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: 59.95 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 2 SESILSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGllagldlpsagsvILSGrnlseLDEDQR 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVP---PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAG-----VDKDFN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARVRAE---HVGFVFQSFQLLDSLNALENVMLPM--------------------------------ELEGRKDAReKARD 126
Cdd:TIGR03719 60 GEARPQpgiKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneisakyaepdadfdklaaeqaELQEIIDAA-DAWD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 127 L---LERVGLGKRL-------THtprqLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLfelnKERNTT 196
Cdd:TIGR03719 139 LdsqLEIAMDALRCppwdadvTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGT 210
|
....*..
gi 492156113 197 LVLVTHD 203
Cdd:TIGR03719 211 VVAVTHD 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-175 |
2.70e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDedqrarvRAEHVGFVFQSFQLLD 100
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 101 SLNALENVMLPMELEGRKdAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLD 175
Cdd:PRK13543 96 DLSTLENLHFLCGLHGRR-AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-217 |
2.89e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 57.62 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 31 ELNKGDTLaIVGASGSGKSTLLGLLAGLDLpsaGSVILSGRNLSELDEDQR-ARVRAEhVGFVFQSFQ-----LLDSLNA 104
Cdd:cd03240 19 EFFSPLTL-IVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHDPKLIReGEVRAQ-VKLAFENANgkkytITRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENV-MLPmelegrkdaREKARDLLERvglgkrlthTPRQLSGGEQQ------RVAIARAFAADPHVLFADEPTGNLDS- 176
Cdd:cd03240 94 LENViFCH---------QGESNWPLLD---------MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEe 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492156113 177 HTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:cd03240 156 NIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-221 |
3.08e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.29 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGsvilsgrnlsELDEDQRARVRAEHVGFVFQsfqlldsLNA 104
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG----------KVDRNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:PRK13546 103 IENIEFKMLCMGfkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 492156113 183 SDLLFELnKERNTTLVLVTHDERLAHR-CRRLIRLEGGRL 221
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKL 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-221 |
6.10e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 19 EGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldedqrarvraehVGFVFQSFQL 98
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 L-DSLNalENVMLPMELEgrkdaREKARDLLERVGLGKRLTHTPR-----------QLSGGEQQRVAIARAFAADPHVLF 166
Cdd:TIGR00957 711 QnDSLR--ENILFGKALN-----EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 167 ADEPTGNLDSHTGERISD-LLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-175 |
8.82e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 8.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVR-AEHVGFVFQS---- 95
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLAlRQQVATVFQDpeqq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 96 --FQLLDSLNA--LENVMLPMElegrkdarEKARDLLERVGL--GKRLTHTPRQ-LSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:PRK13638 90 ifYTDIDSDIAfsLRNLGVPEA--------EITRRVDEALTLvdAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
....*..
gi 492156113 169 EPTGNLD 175
Cdd:PRK13638 162 EPTAGLD 168
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-186 |
8.89e-10 |
|
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: 56.10 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 4 SILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS--AGSVILSGRnlsELDEDQR 81
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARvraehVGFVFQSFQLLDSLNALENVMLPMELegrkdarekardllervglgkrlthtpRQLSGGEQQRVAIARAFAAD 161
Cdd:cd03232 79 RS-----TGYVEQQDVHSPNLTVREALRFSALL---------------------------RGLSVEQRKRLTIGVELAAK 126
|
170 180
....*....|....*....|....*
gi 492156113 162 PHVLFADEPTGNLDSHTGERISDLL 186
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-210 |
1.09e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS-AGSVILSGRnlseldedQRARVRA-----EHVGFVF 93
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGR--------RRGSGETiwdikKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 QSFQLLDSLNA-LENVMLpmelEGRKDA-----------REKARDLLERVGLGKRLTHTP-RQLSGGEQQRVAIARAFAA 160
Cdd:PRK10938 343 SSLHLDYRVSTsVRNVIL----SGFFDSigiyqavsdrqQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVK 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 492156113 161 DPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRC 210
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAC 468
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-202 |
1.33e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS--AGSVILSGRNLseldedqrARVRAEHVGFVFQSFQLLD 100
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP--------TKQILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVM------LPMELEgRKDAREKARDLLERVGLGKrLTHTP------RQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:PLN03211 154 HLTVRETLVfcsllrLPKSLT-KQEKILVAESVISELGLTK-CENTIignsfiRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|....
gi 492156113 169 EPTGNLDSHTGERISDLLFELnKERNTTLVLVTH 202
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-206 |
2.99e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILS-GRNLSELDEDQRARVRAEHvgfvfQSFQL 98
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE-----SPLQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSLnalenvmLPMELEgrkdarEKARDLLERVGL-GKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:PRK10636 398 LARL-------APQELE------QKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|....*....
gi 492156113 178 TGERISDLLFELNKerntTLVLVTHDERL 206
Cdd:PRK10636 465 MRQALTEALIDFEG----ALVVVSHDRHL 489
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-216 |
4.86e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.52 E-value: 4.86e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 143 QLSGGEQQRVAIARAFA-----ADPHVLFaDEPTGNLDSHTGERISDLLFELNKERNTTLVlVTHDERLAHRCRRLIRL 216
Cdd:cd03227 77 QLSGGEKELSALALILAlaslkPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-202 |
5.11e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 18 TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILsgrNLSELDEDQRARVRAEHVGFVFQ--- 94
Cdd:PTZ00265 394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII---NDSHNLKDINLKWWRSKIGVVSQdpl 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 95 ------------SFQLLDSLNALENVM------LPMELEGRKDAREKARDLL-------------------------ERV 131
Cdd:PTZ00265 471 lfsnsiknnikySLYSLKDLEALSNYYnedgndSQENKNKRNSCRAKCAGDLndmsnttdsneliemrknyqtikdsEVV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 132 GLGKR-LTH----------------TPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERN 194
Cdd:PTZ00265 551 DVSKKvLIHdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
....*...
gi 492156113 195 TTLVLVTH 202
Cdd:PTZ00265 631 RITIIIAH 638
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-202 |
5.11e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 5.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTH 202
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
126-222 |
9.00e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 126 DLLERVGLG--KRLThtprQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLfelnKERNTTLVLVTHD 203
Cdd:PRK11147 141 EVLAQLGLDpdAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHD 212
|
90 100
....*....|....*....|
gi 492156113 204 ERLAHR-CRRLIRLEGGRLV 222
Cdd:PRK11147 213 RSFIRNmATRIVDLDRGKLV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-182 |
1.15e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEgdltILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQrarv 84
Cdd:PRK15439 11 LLCARSISKQYSGVE----VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 rAEHVG--FVFQSFQLLDSLNALENVMLpmELEGRKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADP 162
Cdd:PRK15439 83 -AHQLGiyLVPQEPLLFPNLSVKENILF--GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180
....*....|....*....|
gi 492156113 163 HVLFADEPTGNLDSHTGERI 182
Cdd:PRK15439 160 RILILDEPTASLTPAETERL 179
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-206 |
1.56e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEgdltILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLD--LPSAGSVILSGRNLSELDEDQRA 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 83 rvrAEHVGFVFQ----------SFQLLDSLNALENVMLPMELEgRKD----AREKAR------DLLER-VGLGkrlthtp 141
Cdd:PRK09580 77 ---GEGIFMAFQypveipgvsnQFFLQTALNAVRSYRGQEPLD-RFDfqdlMEEKIAllkmpeDLLTRsVNVG------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 142 rqLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHDERL 206
Cdd:PRK09580 146 --FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRI 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-221 |
1.88e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLskvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNL---SELDED 79
Cdd:PRK09700 263 ETVFEVRNV------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAV 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRA-----RVRAEHvGFvFQSF---QLLDSLNALEN------VMLPMELEGRKDArEKARDLLER--VGLGKRLThtprQ 143
Cdd:PRK09700 337 KKGmayitESRRDN-GF-FPNFsiaQNMAISRSLKDggykgaMGLFHEVDEQRTA-ENQRELLALkcHSVNQNIT----E 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 144 LSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEGGRL 221
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-202 |
2.07e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGllagldlpsagsvILSG------RNLSELDEDQRARVR----AEHVGFVF- 93
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMK-------------VLSGvyphgsYEGEILFDGEVCRFKdirdSEALGIVIi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 -QSFQLLDSLNALENVMLPMELEGR-----KDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFA 167
Cdd:NF040905 84 hQELALIPYLSIAENIFLGNERAKRgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 492156113 168 DEPTGNLDSHTGERISDLLFELnKERNTTLVLVTH 202
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-198 |
7.39e-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: 50.72 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA---GSVILSGRNLSELDED 79
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 QRAR---VRAEHVGF----VFQSFQLLDSLNALENVmlpmelegrkdarekardllervglgkrlthtpRQLSGGEQQRV 152
Cdd:cd03233 81 YPGEiiyVSEEDVHFptltVRETLDFALRCKGNEFV---------------------------------RGISGGERKRV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 153 AIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLV 198
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-203 |
8.31e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSKvvpsTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVilsgrNLSEldedqrarvr 85
Cdd:PRK15064 320 LEVENLTK----GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSE---------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 86 AEHVGFVFQsfqllDSLNALENVMLPMELEGrKDAREKARDLLERVGLGKRL------THTPRQLSGGEQQRVAIARAFA 159
Cdd:PRK15064 381 NANIGYYAQ-----DHAYDFENDLTLFDWMS-QWRQEGDDEQAVRGTLGRLLfsqddiKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 492156113 160 ADPHVLFADEPTGNLDShtgERISDLLFELNKERNtTLVLVTHD 203
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSHD 494
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-212 |
9.27e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQRARVraehvGFVFQSFQLL 99
Cdd:NF033858 277 GDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRV-----GYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLPMELEGRKDAREKAR--DLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARvaEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190
....*....|....*....|....*....|....*..
gi 492156113 178 TGERISDLLFELNKERNTTLVLVTH--DErlAHRCRR 212
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHfmNE--AERCDR 466
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-201 |
9.38e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.05 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 18 TEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLP-SAGSVILSGRnlseldedqrarvraehVGFVFQSF 96
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGT-----------------VAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 97 QLLDSlNALENVMLPMELEGRK-----DAREKARDLLERVG-----LGKRLTHtprqLSGGEQQRVAIARAFAADPHVLF 166
Cdd:PLN03130 689 WIFNA-TVRDNILFGSPFDPERyeraiDVTALQHDLDLLPGgdlteIGERGVN----ISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190
....*....|....*....|....*....|....*..
gi 492156113 167 ADEPTGNLDSHTGERISD--LLFELnkeRNTTLVLVT 201
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFDkcIKDEL---RGKTRVLVT 797
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-219 |
9.40e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPS-AGSVILSGrnlseldedqrARVRAEHVGFVFQSfqlldslN 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRG-----------SVAYVPQVSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMELEGRK-------DAREKARDLL---ERVGLGKRLTHtprqLSGGEQQRVAIARAFAADPHVLFADEPTGN 173
Cdd:PLN03232 695 VRENILFGSDFESERywraidvTALQHDLDLLpgrDLTEIGERGVN----ISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 174 LDSHTGERISDLLFElNKERNTTLVLVTHDERLAHRCRRLIRLEGG 219
Cdd:PLN03232 771 LDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
38-206 |
9.80e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 38 LAIVGASGSGKSTLLGLLAGLDLPSAGSVILSgrnlseldedqrARVRAEhvgfVFqSFQLLDSLNALENVMLPMELEGR 117
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRS------------AKVRMA----VF-SQHHVDGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 118 KDAREKARDLLERVGLGKRLTHTPR-QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISD--LLFElnkern 194
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQglVLFQ------ 674
|
170
....*....|..
gi 492156113 195 TTLVLVTHDERL 206
Cdd:PLN03073 675 GGVLMVSHDEHL 686
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-203 |
1.51e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSViLSGRNLSELDEDQRarvRAEhvgfvfqsfqlL 99
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEVAYFDQH---RAE-----------L 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 D-SLNALENVMlpmelEGRKDAREKARDlleRVGLG---------KRlTHTP-RQLSGGEQQRVAIARAFAADPHVLFAD 168
Cdd:PRK11147 395 DpEKTVMDNLA-----EGKQEVMVNGRP---RHVLGylqdflfhpKR-AMTPvKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*
gi 492156113 169 EPTGNLDSHTGErisdLLFELNKERNTTLVLVTHD 203
Cdd:PRK11147 466 EPTNDLDVETLE----LLEELLDSYQGTVLLVSHD 496
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-200 |
1.59e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARVRAEhvgfvfqsFQLL--DS 101
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfEQLQKLVSDE--------WQRNntDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 102 LNALEN----VMLPMELEGRKDArEKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:PRK10938 91 LSPGEDdtgrTTAEIIQDEVKDP-ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|...
gi 492156113 178 TGERISDLLFELNKErNTTLVLV 200
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-203 |
2.43e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 31 ELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnLS----ELDEDQRARVRAehvgFVFQSFQLLDSLNALE 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISykpqYIKPDYDGTVED----LLRSITDDLGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 107 NVMLPMELEgrkdarekarDLLERvglgkRLTHtprqLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHtgERI--SD 184
Cdd:PRK13409 436 EIIKPLQLE----------RLLDK-----NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLavAK 494
|
170
....*....|....*....
gi 492156113 185 LLFELNKERNTTLVLVTHD 203
Cdd:PRK13409 495 AIRRIAEEREATALVVDHD 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-182 |
4.35e-07 |
|
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: 50.29 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldedqrarvraehVGFVFQSFQLLDSlN 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMEL-EGRKDAREKARDLLERVGLGKRLTHTPR-----QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:TIGR01271 503 IKDNIIFGLSYdEYRYTSVIKACQLEEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*
gi 492156113 178 TGERI 182
Cdd:TIGR01271 583 TEKEI 587
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-201 |
4.57e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 23 TILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSA----GSVILSGRNLSELDEDQRARV--RAE---HVGfVF 93
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHYRGDVvyNAEtdvHFP-HL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 QSFQLLDSLNALENVMLPMELEGRKDAREKARDLLERVgLGkrLTHTP---------RQLSGGEQQRVAIARAFAADPHV 164
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAT-YG--LSHTRntkvgndfvRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190
....*....|....*....|....*....|....*..
gi 492156113 165 LFADEPTGNLDSHTGERISDLLFELNKERNTTlVLVT 201
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTT-PLVA 266
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-203 |
6.89e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 1 MSESILSAQNLSKVVPsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGllagldlpsagsvILSGrnlseLDEDQ 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVP---PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAG-----VDKEF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 RARVRAE---HVGFVFQSFQLLDSLNALENVML---------------------PM-----------ELEGRKDAREkAR 125
Cdd:PRK11819 61 EGEARPApgiKVGYLPQEPQLDPEKTVRENVEEgvaevkaaldrfneiyaayaePDadfdalaaeqgELQEIIDAAD-AW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 126 DL---LERVGLGKRL-------THtprqLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLfelnKERNT 195
Cdd:PRK11819 140 DLdsqLEIAMDALRCppwdakvTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPG 211
|
....*...
gi 492156113 196 TLVLVTHD 203
Cdd:PRK11819 212 TVVAVTHD 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-202 |
7.87e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.94 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELDEDQ-RARvraehVGFVFQS-FQL 98
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSR-----LAVVSQTpFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 LDSLNAleNVMLpmeleGRKDA-----REKAR------DLLeRVGLGKRLTHTPR--QLSGGEQQRVAIARAFAADPHVL 165
Cdd:PRK10789 402 SDTVAN--NIAL-----GRPDAtqqeiEHVARlasvhdDIL-RLPQGYDTEVGERgvMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|....*..
gi 492156113 166 FADEPTGNLDSHTGERISDLLFELNKERntTLVLVTH 202
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAH 508
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-184 |
1.12e-06 |
|
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: 48.31 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlseldedqrarvraehVGFVFQsFQLLDSLN 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQ-FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 104 ALENVMLPMEL-EGRKDAREKARDLLERVGLGKRLTHTPR-----QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:cd03291 114 IKENIIFGVSYdEYRYKSVVKACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
....*..
gi 492156113 178 TGERISD 184
Cdd:cd03291 194 TEKEIFE 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-178 |
1.17e-06 |
|
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: 48.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVpsteGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILsGRNLseldedqrarv 84
Cdd:TIGR03719 322 VIEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 85 raeHVGFVFQSfqlLDSLNALENVMLP-------MELEGRK-DARE-------KARDLLERVGlgkrlthtprQLSGGEQ 149
Cdd:TIGR03719 386 ---KLAYVDQS---RDALDPNKTVWEEisggldiIKLGKREiPSRAyvgrfnfKGSDQQKKVG----------QLSGGER 449
|
170 180
....*....|....*....|....*....
gi 492156113 150 QRVAIARAFAADPHVLFADEPTGNLDSHT 178
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-223 |
1.18e-06 |
|
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: 47.64 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 126 DLLERVGLGK-RLTHTPRQLSGGEQQRVAIARAFAAD-PHVLFA-DEPTGNLDSHTGERISDLLFELNKERNtTLVLVTH 202
Cdd:cd03270 119 GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEH 197
|
90 100
....*....|....*....|....*..
gi 492156113 203 DERLAHRCRRLIRL------EGGRLVA 223
Cdd:cd03270 198 DEDTIRAADHVIDIgpgagvHGGEIVA 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-203 |
1.28e-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: 48.63 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 31 ELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnLS----ELDEDQRARVRaehvgfvfqsfQLLDSLN--A 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISykpqYISPDYDGTVE-----------EFLRSANtdD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELegrkdarekardlLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHtgERIS- 183
Cdd:COG1245 430 FGSSYYKTEI-------------IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE--QRLAv 494
|
170 180
....*....|....*....|.
gi 492156113 184 -DLLFELNKERNTTLVLVTHD 203
Cdd:COG1245 495 aKAIRRFAENRGKTAMVVDHD 515
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-213 |
2.33e-06 |
|
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: 48.09 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 5 ILSAQNLSKVVPSTEGdlTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR----NLSELDEDq 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSS--PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQN- 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 81 rarvraehVGFVFQSFQLLDSLNALENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAF 158
Cdd:TIGR01257 2014 --------MGYCPQFDAIDDLLTGREHLYLYARLRGvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 492156113 159 AADPHVLFADEPTGNLDSHTGERISDLLFELNKErNTTLVLVTHD-ERLAHRCRRL 213
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSmEECEALCTRL 2140
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-226 |
3.40e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARvraehVGFVFQSFQL---- 98
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKV-----LGIIPQAPVLfsgt 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 99 ----LDSLNALENVMLPMELEgrkdaREKARDLLER--VGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTG 172
Cdd:PLN03130 1329 vrfnLDPFNEHNDADLWESLE-----RAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492156113 173 NLDSHTGERISDLLFElnkERNTTLVLVthderLAHR------CRRLIRLEGGRLV---APQE 226
Cdd:PLN03130 1404 AVDVRTDALIQKTIRE---EFKSCTMLI-----IAHRlntiidCDRILVLDAGRVVefdTPEN 1458
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-203 |
3.46e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSeldedQRARVRAEHVGFVFQSFQ-----LL 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV-----TRSPQDGLANGIVYISEDrkrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 100 DSLNALENVMLP-MELEGRKDAREKARDLLERVGLGKRL--THTPRQ------LSGGEQQRVAIARAFAADPHVLFADEP 170
Cdd:PRK10762 343 LGMSVKENMSLTaLRYFSRAGGSLKHADEQQAVSDFIRLfnIKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190
....*....|....*....|....*....|...
gi 492156113 171 TGNLDSHTGERISDLLFELNKErNTTLVLVTHD 203
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAE-GLSIILVSSE 454
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
151-217 |
5.60e-06 |
|
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: 46.58 E-value: 5.60e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492156113 151 RVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKE----RNTTLVLVTHDERLAHRCRRLIRLE 217
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqRNFQLLVITHDEDFVELLGRSEYVE 1283
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-202 |
6.10e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGrnlseldedqRARVRAEHVGfvfqsfqLLDSLNA 104
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------SAALIAISSG-------LNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLPMELEG--RKDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI 182
Cdd:PRK13545 103 IENIELKGLMMGltKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180
....*....|....*....|
gi 492156113 183 SDLLFELnKERNTTLVLVTH 202
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISH 201
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-182 |
7.46e-06 |
|
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: 46.48 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 24 ILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLSELD-EDQRARVRAEHVGFVFQSFQLLDSL 102
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 103 NAL-----ENVMLPMELEGRKDAREKARDllervGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSH 177
Cdd:TIGR00957 1381 DPFsqysdEEVWWALELAHLKTFVSALPD-----KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
....*
gi 492156113 178 TGERI 182
Cdd:TIGR00957 1456 TDNLI 1460
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-223 |
1.59e-05 |
|
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: 43.85 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 25 LHELSLELNKGDTLAIVGASGSGKSTllgllagldlpsagsVILSGRNLSELDEDQRARVRAEHVGFVFqsfqlLDSLNA 104
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLYASGKARLISFLPKFSRNKLIF-----IDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 105 LENVMLpmelegrkdarekardllERVGLGKRLThtprQLSGGEQQRVAIAR-AFAADPHVLFA-DEPTGNLDSHTGERI 182
Cdd:cd03238 71 LIDVGL------------------GYLTLGQKLS----TLSGGELQRVKLASeLFSEPPGTLFIlDEPSTGLHQQDINQL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 492156113 183 SDLLFELNKERNtTLVLVTHDERLAHRCRRLIRL------EGGRLVA 223
Cdd:cd03238 129 LEVIKGLIDLGN-TVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVF 174
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-214 |
1.97e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 144 LSGGEQQRVAIARAFAAD----PHVLfaDEPTGNLDSHTGERISDLLFELNKERNTTLvLVTHDERLAHRCRRLI 214
Cdd:PRK00635 477 LSGGEQERTALAKHLGAEligiTYIL--DEPSIGLHPQDTHKLINVIKKLRDQGNTVL-LVEHDEQMISLADRII 548
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-192 |
2.94e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNL-SKVVPStegdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNLseldeDQR 81
Cdd:PRK10982 248 EVILEVRNLtSLRQPS-------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-----NNH 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 82 ARVRAEHVGFVFQS--------FQLLD-SLNAL----ENVMLPMELEGRKDAREKARDLLE--RVGLGKRLTHTPrQLSG 146
Cdd:PRK10982 316 NANEAINHGFALVTeerrstgiYAYLDiGFNSLisniRNYKNKVGLLDNSRMKSDTQWVIDsmRVKTPGHRTQIG-SLSG 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 492156113 147 GEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKE 192
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK 440
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
144-203 |
3.18e-05 |
|
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: 42.94 E-value: 3.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 144 LSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKERNTTLVLVTHD 203
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
143-192 |
3.28e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 3.28e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 492156113 143 QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKE 192
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ 454
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
144-218 |
3.81e-05 |
|
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: 43.97 E-value: 3.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 144 LSGGEQQRVAIARAFAADPHVLFADEPTgnldSHTGERISDLLFELNKERNTTLVLVTHDERLAHRCRRLIRLEG 218
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
142-223 |
6.05e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKerntTLVLVTH-DERLAHRCRRLIRLEGGR 220
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHaREFLNTVVTDILHLHGQK 418
|
...
gi 492156113 221 LVA 223
Cdd:PLN03073 419 LVT 421
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
122-220 |
6.95e-05 |
|
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: 41.59 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 122 EKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERI-----SDLLFELNKERNTT 196
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleeLRLLLLLKSEKNLT 118
|
90 100 110
....*....|....*....|....*....|
gi 492156113 197 LVLVTHDER------LAHRCRRLIRLEGGR 220
Cdd:smart00382 119 VILTTNDEKdlgpalLRRRFDRRIVLLLIL 148
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
117-171 |
2.76e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 2.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 492156113 117 RKDAREKARDLLERVGlgkrlthtprQLSGGEQQRVAIARAFAADPHVLFADEPT 171
Cdd:NF040905 388 RKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-204 |
3.44e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 21 DLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRNlseLDEDQRArvRAEHVGFVFQSFQLLD 100
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS---IKKDLCT--YQKQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 101 SLNALENVMLPMELEgrkDAREKARDLLERVGLGKRLTHTPRQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGE 180
Cdd:PRK13540 88 YLTLRENCLYDIHFS---PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|....
gi 492156113 181 RISDLLfELNKERNTTLVLVTHDE 204
Cdd:PRK13540 165 TIITKI-QEHRAKGGAVLLTSHQD 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
142-203 |
3.63e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 3.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492156113 142 RQLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD 203
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSD 455
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
61-223 |
4.88e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 61 PSAGSVILSGRNLSEldedqrarvraehvgfvFQSFQLLDSLNALENVMLPMEleGRKDAREKARDLLER------VGLG 134
Cdd:TIGR00630 418 PEALAVTVGGKSIAD-----------------VSELSIREAHEFFNQLTLTPE--EKKIAEEVLKEIRERlgflidVGLD 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 135 K-RLTHTPRQLSGGEQQRVAIARAFAAD-PHVLFA-DEPTGNLDSHTGERISDLLFELNKERNTTLVlVTHDERLAHRCR 211
Cdd:TIGR00630 479 YlSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV-VEHDEDTIRAAD 557
|
170
....*....|....*...
gi 492156113 212 RLIRL------EGGRLVA 223
Cdd:TIGR00630 558 YVIDIgpgageHGGEVVA 575
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
144-192 |
5.09e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 5.09e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 492156113 144 LSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELNKE 192
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE 452
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-189 |
7.73e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 3 ESILSAQNLSKVVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLpsaGSVILSGRNLS---ELDED 79
Cdd:TIGR00956 757 EDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVngrPLDSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 80 -QRArvraehVGFVFQSFQLLDSLNALENVM------LPMEL--EGRKDAREKARDLLERVGLGKRLTHTPRQ-LSGGEQ 149
Cdd:TIGR00956 834 fQRS------IGYVQQQDLHLPTSTVRESLRfsaylrQPKSVskSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQR 907
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 492156113 150 QRVAIARAFAADPHVL-FADEPTGNLDSHTGERISDLLFEL 189
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-218 |
1.01e-03 |
|
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: 39.89 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 6 LSAQNLSkvVPSTEGDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLpSAGSVILSGR--NLSELDEDQRAR 83
Cdd:TIGR01271 1218 MDVQGLT--AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVswNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 84 VRAEHVGFVFQ-SFQL-LDslnalenvmlPMElegrKDAREKARDLLERVGLGKRLTHTPRQ-----------LSGGEQQ 150
Cdd:TIGR01271 1295 GVIPQKVFIFSgTFRKnLD----------PYE----QWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQ 1360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492156113 151 RVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFElnKERNTTLVLVTHDERLAHRCRRLIRLEG 218
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ--SFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-203 |
1.12e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 26 HELSLELNKGDTLaIVGASGSGKST-----------------LLGLLAGLDLPSAGSVILS----------GRNLSELDE 78
Cdd:COG0419 15 DTETIDFDDGLNL-IVGPNGAGKSTileairyalygkarsrsKLRSDLINVGSEEASVELEfehggkryriERRQGEFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 79 DQRA--RVRAEHVGFVFQ---SFQLLDSLNALENvmlpmELEGRKDAREKARDLLERvgLGKRLT--HTPRQLSGGEQQR 151
Cdd:COG0419 94 FLEAkpSERKEALKRLLGleiYEELKERLKELEE-----ALESALEELAELQKLKQE--ILAQLSglDPIETLSGGERLR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 492156113 152 VAIARAFAadphvLFADepTGNLDSHTGERISDLLFElnkernttLVLVTHD 203
Cdd:COG0419 167 LALADLLS-----LILD--FGSLDEERLERLLDALEE--------LAIITHV 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-203 |
1.93e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 20 GDLTILHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGR-NLSELDEDQRARVRAEhVGFVF----- 93
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPA-LEYVIdgdre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 94 --QSFQLLDSLNALENVMLPMELEGRKDA------REKARDLLERVGLGK-RLTHTPRQLSGGEQQRVAIARAFAADPHV 164
Cdd:PRK10636 91 yrQLEAQLHDANERNDGHAIATIHGKLDAidawtiRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 492156113 165 LFADEPTGNLDSHTGERISDLLfelnKERNTTLVLVTHD 203
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHD 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-225 |
5.77e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 10 NLSKVVPSTEGdltiLHELSLELNKGDTLAIVGASGSGKSTLLGLLAGLDLPSAGSVILSGRnlsELDEDQRARVRAEHV 89
Cdd:PRK10982 3 NISKSFPGVKA----LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK---EIDFKSSKEALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 90 GFVFQSFQLLDSLNALENVML---PM-------------------ELEGRKDAREKARDllervglgkrlthtprqLSGG 147
Cdd:PRK10982 76 SMVHQELNLVLQRSVMDNMWLgryPTkgmfvdqdkmyrdtkaifdELDIDIDPRAKVAT-----------------LSVS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492156113 148 EQQRVAIARAFAADPHVLFADEPTGNLDSHTGERISDLLFELnKERNTTLVLVTHD-ERLAHRCRRLIRLEGGRLVAPQ 225
Cdd:PRK10982 139 QMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKmEEIFQLCDEITILRDGQWIATQ 216
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
126-223 |
6.52e-03 |
|
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: 36.82 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492156113 126 DLLERVGLGK-RLTHTPRQLSGGEQQRVAIAR--AFAADPHVLFA-DEPTGNLDSHTGERISDLLFELNKERNTTLVlVT 201
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKelSKRSTGKTLYIlDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV-IE 229
|
90 100
....*....|....*....|....*...
gi 492156113 202 HDERLAHRCRRLIRL------EGGRLVA 223
Cdd:cd03271 230 HNLDVIKCADWIIDLgpeggdGGGQVVA 257
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
143-178 |
8.34e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.02 E-value: 8.34e-03
10 20 30
....*....|....*....|....*....|....*.
gi 492156113 143 QLSGGEQQRVAIARAFAADPHVLFADEPTGNLDSHT 178
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| |
