|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-200 |
2.99e-36 |
|
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: 126.45 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:cd03255 25 LSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLTALENVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELTHFKTQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDAANGKLLSGML 185
Cdd:cd03255 105 LPLLLAGVPKKERRERaeeLLERVGLGDRLNHYPSELSGGQQQRVAIARAlANDP-KIILADEPTGNLDSETGKEVMELL 183
|
170
....*....|....*
gi 1681973554 186 LEEAQAQGAGIVVTS 200
Cdd:cd03255 184 RELNKEAGTTIVVVT 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
31-215 |
2.99e-33 |
|
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: 118.35 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglrRRSLSMLFQDLRLFGELTVAENIGL 110
Cdd:COG4133 24 TLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-----RRRLAYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELTHFK-TQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLEEA 189
Cdd:COG4133 99 WAALYGLRaDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAE-LIAAH 177
|
170 180
....*....|....*....|....*.
gi 1681973554 190 QAQGAGIVVTSvGSRLGLPYHKTLTL 215
Cdd:COG4133 178 LARGGAVLLTT-HQPLELAAARVLDL 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
31-198 |
3.53e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.61 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENIGL 110
Cdd:COG1136 30 SIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLRRRHIGFVFQFFNLLPELTALENVAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELTHFKTQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDAANGKLLSGMLL 186
Cdd:COG1136 110 PLLLAGVSRKERRERareLLERVGLGDRLDHRPSQLSGGQQQRVAIARAlVNRP-KLILADEPTGNLDSKTGEEVLELLR 188
|
170
....*....|..
gi 1681973554 187 EEAQAQGAGIVV 198
Cdd:COG1136 189 ELNRELGTTIVM 200
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
31-200 |
5.07e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 110.29 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGL 110
Cdd:COG4619 22 TLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW----RRQVAYVPQEPALWGG-TVRDNLPF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELTHFK-TQEQIGRMLEAAGIADK-RDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEE 188
Cdd:COG4619 97 PFQLRERKfDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREY 176
|
170
....*....|..
gi 1681973554 189 AQAQGAGIVVTS 200
Cdd:COG4619 177 LAEEGRAVLWVS 188
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-175 |
1.45e-29 |
|
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: 109.15 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI-- 108
Cdd:cd03259 22 TVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------ERRNIGMVFQDYALFPHLTVAENIaf 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 109 GLKN-ELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03259 96 GLKLrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-200 |
1.67e-26 |
|
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: 101.00 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglRRRSLSMLFQ--DLRLFGeLTVAENI 108
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVFQnpDDQFFG-PTVEEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 --GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAfIRCM--CQPfDFILLDEPVSHLDAANGKLLSG 183
Cdd:cd03225 98 afGLENLgLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVlaMDP-DILLLDEPTAGLDPAGRRELLE 175
|
170
....*....|....*..
gi 1681973554 184 mLLEEAQAQGAGIVVTS 200
Cdd:cd03225 176 -LLKKLKAEGKTIIIVT 191
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
31-199 |
2.95e-26 |
|
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: 100.38 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAEN--I 108
Cdd:TIGR03608 20 TIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETVEENldL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKN-ELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLE 187
Cdd:TIGR03608 100 GLKYkKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLE 179
|
170
....*....|..
gi 1681973554 188 EAQAQGAGIVVT 199
Cdd:TIGR03608 180 LNDEGKTIIIVT 191
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
31-199 |
5.54e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.52 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENI-- 108
Cdd:COG3638 25 EIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR-IGMIFQQFNLVPRLSVLTNVla 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -------GLKNELTHFKTQEQIG--RMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:COG3638 104 grlgrtsTWRSLLGLFPPEDRERalEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTAR 183
|
170 180
....*....|....*....|
gi 1681973554 180 LLSGMLLEEAQAQGAGIVVT 199
Cdd:COG3638 184 QVMDLLRRIAREDGITVVVN 203
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
31-199 |
1.11e-25 |
|
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: 99.68 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSlSMLFQDLRLFGELTVAENI-- 108
Cdd:TIGR02315 24 NINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRRI-GMIFQHYNLIERLTVLENVlh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -------GLKNELTHFKTQEQIGRM--LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:TIGR02315 103 grlgykpTWRSLLGRFSEEDKERALsaLERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSK 182
|
170 180
....*....|....*....|
gi 1681973554 180 LLSGMLLEEAQAQGAGIVVT 199
Cdd:TIGR02315 183 QVMDYLKRINKEDGITVIIN 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-169 |
4.06e-25 |
|
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: 95.79 E-value: 4.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGELTVAENIGL 110
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 111 KNELTHFKTQE---QIGRMLEAAGIADKRDVPVEK----LSFGQQQRVAFIRCMCQPFDFILLDEP 169
Cdd:pfam00005 83 GLLLKGLSKREkdaRAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-205 |
7.55e-25 |
|
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: 96.71 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRrSLSMLFQDLRLFGELTVAENIG 109
Cdd:cd03292 22 ISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELTHFKTQE---QIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLL 186
Cdd:cd03292 101 FALEVTGVPPREirkRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN-LL 179
|
170
....*....|....*....
gi 1681973554 187 EEAQAQGAGIVVTSVGSRL 205
Cdd:cd03292 180 KKINKAGTTVVVATHAKEL 198
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-200 |
8.78e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.66 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVA 105
Cdd:COG2884 19 SDVSLEieKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR-IGVVFQDFRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIGLKNELTHFKTQE---QIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLDAANG-KL 180
Cdd:COG2884 98 ENVALPLRVTGKSRKEirrRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVnRP-ELLLADEPTGNLDPETSwEI 176
|
170 180
....*....|....*....|
gi 1681973554 181 LSgmLLEEAQAQGAGIVVTS 200
Cdd:COG2884 177 ME--LLEEINRRGTTVLIAT 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
31-175 |
2.32e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEY-CLLeAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaaaWSGL--RRRSLSMLFQDLRLFGELTVAEN 107
Cdd:COG3842 27 SIEPGEFvALL-GPSGCGKTTLLRMIAGFETPDSGRILLDGRD--------VTGLppEKRNVGMVFQDYALFPHLTVAEN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 108 I--GLKNElthfKT-----QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDA 175
Cdd:COG3842 98 VafGLRMR----GVpkaeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDA 168
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
31-198 |
2.99e-24 |
|
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: 95.71 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENI-- 108
Cdd:cd03256 23 SINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ-IGMIFQQFNLIERLSVLENVls 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNELTHFK------TQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:cd03256 102 GRLGRRSTWRslfglfPKEEKQRalaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSR 181
|
170
....*....|....*....
gi 1681973554 180 LLSGMLLEEAQAQGAGIVV 198
Cdd:cd03256 182 QVMDLLKRINREEGITVIV 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-176 |
3.74e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.59 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ERPVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 110 L----KNELTHFKtQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:COG3840 94 LglrpGLKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
30-199 |
4.94e-23 |
|
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: 92.80 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGE-YCLLeAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:COG1120 22 LSLPPGEvTALL-GPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GL-----KNELTHFKTQ--EQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLL 181
Cdd:COG1120 97 ALgryphLGLFGRPSAEdrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEV 176
|
170
....*....|....*...
gi 1681973554 182 SGMLLEEAQAQGAGIVVT 199
Cdd:COG1120 177 LELLRRLARERGRTVVMV 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-174 |
1.75e-21 |
|
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: 89.24 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVA 105
Cdd:cd03294 41 NDVSLdvREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 106 ENIGLKNELTHFKTQEQIGRMLEA---AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEAlelVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-193 |
2.10e-21 |
|
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: 87.93 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcRGFSAAAwsglrRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPA-----DRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELTHFKTQEQIGRMLEAA---GIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLL 186
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALarvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
....*..
gi 1681973554 187 EEAQAQG 193
Cdd:cd03298 173 DLHAETK 179
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
31-199 |
4.20e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 90.66 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGL 110
Cdd:COG2274 497 TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL----RRQIGVVLQDVFLFSG-TIRENITL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELThfkTQEQIGRMLEAAGIAD--KR-----DVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:COG2274 572 GDPDA---TDEEIIEAARLAGLHDfiEAlpmgyDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
170 180
....*....|....*....|
gi 1681973554 180 LLSGMLLEEAQAQGAgIVVT 199
Cdd:COG2274 649 IILENLRRLLKGRTV-IIIA 667
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
31-198 |
4.40e-21 |
|
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: 87.49 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQDLRLFGELTVAENI-- 108
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE---IARLGIGRTFQIPRLFPELTVLENVmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -----------GLKNELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:cd03219 99 aaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180
....*....|....*....|.
gi 1681973554 178 GKLLSGmLLEEAQAQGAGIVV 198
Cdd:cd03219 179 TEELAE-LIRELRERGITVLL 198
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
33-175 |
1.51e-20 |
|
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: 85.85 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI--GL 110
Cdd:cd03299 23 ERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRDISYVPQNYALFPHMTVYKNIayGL 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 111 KNELTHFKTQE----QIGRMLeaaGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03299 97 KKRKVDKKEIErkvlEIAEML---GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
30-187 |
2.09e-20 |
|
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: 85.37 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENI- 108
Cdd:cd03300 21 LDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------KRPVNTVFQNYALFPHLTVFENIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -GLK-NELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAangKLLSGML 185
Cdd:cd03300 95 fGLRlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALvNEP-KVLLLDEPLGALDL---KLRKDMQ 170
|
..
gi 1681973554 186 LE 187
Cdd:cd03300 171 LE 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
33-175 |
3.41e-20 |
|
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: 84.83 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGfsaaawsglRRRSLSMLFQDLRLFGELTVAENIGLKN 112
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------PGPDRGYVFQQDALLPWLTVLDNVALGL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 113 ELTHFKTQEQIGR---MLEAAGIADKRD-VPVEkLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDA 175
Cdd:cd03293 99 ELQGVPKAEARERaeeLLELVGLSGFENaYPHQ-LSGGMRQRVALARALaVDP-DVLLLDEPFSALDA 164
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
29-199 |
5.40e-20 |
|
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: 83.85 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfsaaawSGLRRRSLSMLFQDLR--LFGElTVAE 106
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQDVDyqLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 107 NIGLKNELTHfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLL 186
Cdd:cd03226 92 ELLLGLKELD-AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170
....*....|...
gi 1681973554 187 EEAQAQGAGIVVT 199
Cdd:cd03226 171 ELAAQGKAVIVIT 183
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
28-200 |
6.40e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 83.87 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGadcRGFSAAAwsglrRRSLSMLFQDLRLFGELTVA 105
Cdd:cd03269 17 DDISFsvEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-----RNRIGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENI----GLKNeLTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFI-RCMCQPfDFILLDEPVSHLDAANGKL 180
Cdd:cd03269 89 DQLvylaQLKG-LKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIaAVIHDP-ELLILDEPFSGLDPVNVEL 166
|
170 180
....*....|....*....|
gi 1681973554 181 LSGMLLEEAqAQGAGIVVTS 200
Cdd:cd03269 167 LKDVIRELA-RAGKTVILST 185
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
31-199 |
6.55e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.76 E-value: 6.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEY-CLLeAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGfsaaawsglRRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:COG1116 33 TVAAGEFvALV-GPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---------PGPDRGVVFQEPALLPWLTVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELTHFKTQE---QIGRMLEAAGIADKRDV-PVEkLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDAANGKLLSGM 184
Cdd:COG1116 103 LGLELRGVPKAErreRARELLELVGLAGFEDAyPHQ-LSGGMRQRVAIARAlANDP-EVLLMDEPFGALDALTRERLQDE 180
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGAGIV-VT 199
Cdd:COG1116 181 LLRLWQETGKTVLfVT 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-176 |
6.74e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.25 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENIGL----KNELTHfKT 119
Cdd:PRK10771 34 SGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS------RRPVSMLFQENNLFSHLTVAQNIGLglnpGLKLNA-AQ 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 120 QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMC--QPfdFILLDEPVSHLDAA 176
Cdd:PRK10771 107 REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVreQP--ILLLDEPFSALDPA 163
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
34-187 |
1.23e-19 |
|
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: 83.07 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENIGLKNE 113
Cdd:cd03301 25 DGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------DRDIAMVFQNYALYPHMTVYDNIAFGLK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 114 LTHFKTQEQIGRMLEAA---GIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAangKLLSGMLLE 187
Cdd:cd03301 99 LRKVPKDEIDERVREVAellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA---KLRVQMRAE 172
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
31-175 |
1.52e-19 |
|
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: 85.09 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEY-CLLeAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglrrRSLSMLFQDLRLFGELTVAENI- 108
Cdd:TIGR03265 26 SVKKGEFvCLL-GPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK------RDYGIVFQSYALFPNLTVADNIa 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 109 -GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:TIGR03265 99 yGLKNRgMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDA 167
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-177 |
2.27e-19 |
|
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: 85.58 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFgELTVAENIGL 110
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQNPYLF-AGTIRENLRL 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 111 KNELThfkTQEQIGRMLEAAGIAD--KR-----DVPVE----KLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:COG4988 434 GRPDA---SDEELEAALEAAGLDEfvAAlpdglDTPLGeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAET 508
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-177 |
2.35e-19 |
|
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: 81.28 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIgl 110
Cdd:cd03228 24 TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQDPFLFSG-TIRENI-- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 111 knelthfktqeqigrmleaagiadkrdvpvekLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:cd03228 97 --------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-199 |
4.11e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVA 105
Cdd:PRK11629 26 HNVSFsiGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIGLKNELTHFKT---QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLS 182
Cdd:PRK11629 106 ENVAMPLLIGKKKPaeiNSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170
....*....|....*...
gi 1681973554 183 GMLLEEAQAQG-AGIVVT 199
Cdd:PRK11629 186 QLLGELNRLQGtAFLVVT 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-174 |
7.97e-19 |
|
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: 81.04 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCrGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENIGL 110
Cdd:cd03262 22 TVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQK-VGMVFQQFNLFPHLTVLENITL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 111 ---------KNElthfktQEQIGR-MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03262 100 apikvkgmsKAE------AEERALeLLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
31-177 |
1.03e-18 |
|
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: 81.09 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLR--RRSLSMLFQDLRLFGELTVAENI 108
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE---LRkaRRRIGMIFQHFNLLSSRTVFENV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 109 GLKNELTHFKTQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAAN 177
Cdd:cd03258 104 ALPLEIAGVPKAEIEERvleLLELVGLEDKADAYPAQLSGGQKQRVGIARALaNNP-KVLLCDEATSALDPET 175
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
29-200 |
1.18e-18 |
|
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: 79.54 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:cd03229 20 SLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT--DLEDELPPLRRRIGMVFQDFALFPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLknelthfktqeqigrmleaagiadkrdvpveKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSgMLLEE 188
Cdd:cd03229 98 AL-------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR-ALLKS 145
|
170
....*....|...
gi 1681973554 189 AQAQ-GAGIVVTS 200
Cdd:cd03229 146 LQAQlGITVVLVT 158
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-199 |
2.04e-18 |
|
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: 82.72 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFgELTVAENIGL 110
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW----RDQIAWVPQHPFLF-AGTIAENIRL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 -KNElthfKTQEQIGRMLEAAGIAD-KRDVPV----------EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANG 178
Cdd:TIGR02857 419 aRPD----ASDAEIREALERAGLDEfVAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180
....*....|....*....|.
gi 1681973554 179 KLLSGMLLEEAQAQgAGIVVT 199
Cdd:TIGR02857 495 AEVLEALRALAQGR-TVLLVT 514
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
31-199 |
2.17e-18 |
|
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: 80.24 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENIGL 110
Cdd:cd03261 22 DVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR-MGMLFQSGALFDSLTVFENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 kNELTHFK-TQEQIGRM----LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGML 185
Cdd:cd03261 101 -PLREHTRlSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLI 179
|
170
....*....|....*
gi 1681973554 186 LEEAQAQGA-GIVVT 199
Cdd:cd03261 180 RSLKKELGLtSIMVT 194
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
31-174 |
2.40e-18 |
|
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: 80.42 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfsaaAWSGLR-RRSLSMLFQDLRLFGELTVAENIG 109
Cdd:cd03295 23 EIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-----EQDPVElRRKIGYVIQQIGLFPHMTVEENIA 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 110 LKNELTHFKTQEQIGRM--------LEAAGIADKrdVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03295 98 LVPKLLKWPKEKIRERAdellalvgLDPAEFADR--YPHE-LSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
31-198 |
3.11e-18 |
|
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: 82.12 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGL 110
Cdd:COG4987 357 TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----RRRIAVVPQRPHLFDT-TLRENLRL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 -KNELTHfktqEQIGRMLEAAGIAD-------KRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANG 178
Cdd:COG4987 432 aRPDATD----EELWAALERVGLGDwlaalpdGLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
170 180
....*....|....*....|
gi 1681973554 179 KLLSGMLLEeaQAQGAGIVV 198
Cdd:COG4987 508 QALLADLLE--ALAGRTVLL 525
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
31-176 |
3.37e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIrEDYT-GKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI- 108
Cdd:COG3839 25 DIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTsGEILIGGRDVTDLPP------KDRNIAMVFQSYALYPHMTVYENIa 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 109 -GLKNElthfKT-----QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:COG3839 98 fPLKLR----KVpkaeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
31-199 |
4.33e-18 |
|
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: 79.64 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENIGL 110
Cdd:COG1127 27 DVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR-IGMLFQGGALFDSLTVFENVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 K-NELTHFKTQE--QIGRM-LEAAGIADKRD-VPVEkLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLDAANGKLLSGM 184
Cdd:COG1127 106 PlREHTDLSEAEirELVLEkLELVGLPGAADkMPSE-LSGGMRKRVALARALAlDP-EILLYDEPTAGLDPITSAVIDEL 183
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGA-GIVVT 199
Cdd:COG1127 184 IRELRDELGLtSVVVT 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
44-174 |
5.15e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 79.27 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLchflygIR-----EDYT-GKILFDGADCrGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENIGL------- 110
Cdd:COG1126 36 SGSGKSTL------LRcinllEEPDsGTITVDGEDL-TDSKKDINKLRRK-VGMVFQQFNLFPHLTVLENVTLapikvkk 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 111 --KNELthfktqEQIGR-MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLD 174
Cdd:COG1126 108 msKAEA------EERAMeLLERVGLADKADAYPAQLSGGQQQRVAIARALAmEP-KVMLFDEPTSALD 168
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-186 |
5.40e-18 |
|
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: 81.64 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfSAAAWSGLRRRSLSMLFQDLRLFGElTVAENI 108
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP----VSSLDQDEVRRRVSVCAQDAHLFDT-TVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNELThfkTQEQIGRMLEAAGIADK-RDVP----------VEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:TIGR02868 430 RLARPDA---TDEELWAALERVGLADWlRALPdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
....*....
gi 1681973554 178 GKLLSGMLL 186
Cdd:TIGR02868 507 ADELLEDLL 515
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
33-200 |
8.23e-18 |
|
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: 81.10 E-value: 8.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGI---REDYTGKILFDGADCRGFSAAawsgLRRRSLSMLFQD-LRLFGELTVAENI 108
Cdd:COG1123 30 APGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEA----LRGRRIGMVFQDpMTQLNPVTVGDQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 --GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGML 185
Cdd:COG1123 106 aeALENLgLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
|
170
....*....|....*
gi 1681973554 186 LEEAQAQGAGIVVTS 200
Cdd:COG1123 186 RELQRERGTTVLLIT 200
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
43-175 |
1.06e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.81 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsAAAWSGLRRRSLSMLFQDLRLFGELTVAENI--GLKNeLTHFKTQ 120
Cdd:COG1118 36 PSGSGKTTLLRIIAGLETPDSGRIVLNGRD-----LFTNLPPRERRVGFVFQHYALFPHMTVAENIafGLRV-RPPSKAE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 121 --EQIGRMLEA---AGIADKRdvPVEkLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLDA 175
Cdd:COG1118 110 irARVEELLELvqlEGLADRY--PSQ-LSGGQRQRVALARALAvEP-EVLLLDEPFGALDA 166
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
30-199 |
1.11e-17 |
|
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: 77.09 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglRRRSLSMLFQdlrlfgeltvaenig 109
Cdd:cd03214 20 LSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 lknelthfktqeqigrMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEA 189
Cdd:cd03214 81 ----------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLA 144
|
170
....*....|
gi 1681973554 190 QAQGAGIVVT 199
Cdd:cd03214 145 RERGKTVVMV 154
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-187 |
2.62e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.11 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 8 RVLPCVFAGEAAPRDSgvwsqEVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRR 87
Cdd:PRK11607 23 RNLTKSFDGQHAVDDV-----SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------YQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 88 SLSMLFQDLRLFGELTVAENI--GLK-NELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFI 164
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQNIafGLKqDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180
....*....|....*....|...
gi 1681973554 165 LLDEPVSHLDAangKLLSGMLLE 187
Cdd:PRK11607 172 LLDEPMGALDK---KLRDRMQLE 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-176 |
2.71e-17 |
|
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: 76.95 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI--GLKnELTHFKTQ 120
Cdd:cd03297 31 ASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLafGLK-RKRNREDR 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 121 EQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:cd03297 110 ISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
31-197 |
2.78e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGE-YCLL-EaaSGTGKTSLCHFLYGIREDYTGKILFDGADCRGFS-AAAwsglRRRSLSMLFQDLRLFGELTVAEN 107
Cdd:COG1129 26 ELRPGEvHALLgE--NGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDA----QAAGIAIIHQELNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELTHF------KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN-GKL 180
Cdd:COG1129 100 IFLGREPRRGglidwrAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREvERL 179
|
170
....*....|....*..
gi 1681973554 181 LSgmLLEEAQAQGAGIV 197
Cdd:COG1129 180 FR--IIRRLKAQGVAII 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
31-199 |
3.40e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.24 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsAAAWSGLRRRSLSMLFQDLRLFGELTVAENIGL 110
Cdd:TIGR01189 22 TLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-----LAEQRDEPHENILYLGHLPGLKPELSALENLHF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELtHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAQ 190
Cdd:TIGR01189 97 WAAI-HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLA 175
|
....*....
gi 1681973554 191 AQGAGIVVT 199
Cdd:TIGR01189 176 RGGIVLLTT 184
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
34-179 |
4.23e-17 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 76.30 E-value: 4.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLyGIREDY-TGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENIGLKN 112
Cdd:NF038007 30 KGDFVSIMGPSGSGKSTLLNII-GMFDSLdSGSLTLAGKEVTNLSYSQKIILRRELIGYIFQSFNLIPHLSIFDNVALPL 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 113 ELTHFKTQEQIGRM---LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:NF038007 109 KYRGVAKKERIERVnqvLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-187 |
1.63e-16 |
|
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: 76.38 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 40 LEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI--GLK-NELTH 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP------HLRHINMVFQSYALFPHMTVEENVafGLKmRKVPR 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 117 FKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAangKLLSGMLLE 187
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDK---KLRDQMQLE 142
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-176 |
6.54e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVA 105
Cdd:PRK10908 19 QGVTFhmRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ-IGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 106 ENIGLKnELTHFKTQEQIGRMLEAA----GIADK-RDVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK10908 98 DNVAIP-LIIAGASGDDIRRRVSAAldkvGLLDKaKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-208 |
1.23e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfsaaawSGLRRRSLSMLFQDLRLFGELTVAENIGLKNEL 114
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-------RGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 115 THFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAQAQGA 194
Cdd:PRK13543 110 HGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGA 189
|
170
....*....|....
gi 1681973554 195 GIVVTSvGSRLGLP 208
Cdd:PRK13543 190 ALVTTH-GAYAAPP 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-175 |
1.54e-15 |
|
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: 72.76 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 32 FRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaAAWSGLRRRSLSMLFQDLRLFGELTVAENI--G 109
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGED------ATDVPVQERNVGFVFQHYALFRHMTVFDNVafG 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 110 LK--------NELTHFKTQEQIGRMLEAAGIADKrdVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03296 99 LRvkprserpPEAEIRAKVHELLKLVQLDWLADR--YPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-175 |
2.15e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaAAWSGLRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED------VTHRSIQQRDICMVFQSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 109 GLKNELTHFKTQEQIGRMLEA------AGIADKRdvpVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRVKEAlelvdlAGFEDRY---VDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
45-200 |
2.62e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.83 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGadcrgfsaaawsglrrRSLSmlFQDLRLFGEL----------TVAENIG----L 110
Cdd:COG4152 37 GAGKTTTIRIILGILAPDSGEVLWDG----------------EPLD--PEDRRRIGYLpeerglypkmKVGEQLVylarL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNeLTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDAANGKLLSGMLLEEA 189
Cdd:COG4152 99 KG-LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAlLHDP-ELLILDEPFSGLDPVNVELLKDVIRELA 176
|
170
....*....|.
gi 1681973554 190 qAQGAGIVVTS 200
Cdd:COG4152 177 -AKGTTVIFSS 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-198 |
3.49e-15 |
|
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: 71.49 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENI--GL 110
Cdd:cd03251 26 PAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQDVFLFND-TVAENIayGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNElthfkTQEQIGRMLEAA-------GIADKRDVPVE----KLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:cd03251 101 PGA-----TREEVEEAARAAnahefimELPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170
....*....|....*....
gi 1681973554 180 LLSGMlLEEAQAQGAGIVV 198
Cdd:cd03251 176 LVQAA-LERLMKNRTTFVI 193
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
44-174 |
4.57e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLchflygIR-----EDYT-GKILFDGADCRGFSAAAwsgLR--RRSLSMLFQDLRLFGELTVAENIGLKNELT 115
Cdd:COG1135 40 SGAGKSTL------IRcinllERPTsGSVLVDGVDLTALSERE---LRaaRRKIGMIFQHFNLLSSRTVAENVALPLEIA 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 116 HF---KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLD 174
Cdd:COG1135 111 GVpkaEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALaNNP-KVLLCDEATSALD 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-200 |
4.81e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCrGFSAAAWSGLRRrSLSMLFQ--DLRLFGElTVAEN 107
Cdd:PRK13636 27 INIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRE-SVGMVFQdpDNQLFSA-SVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 I--GLKN-ELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGM 184
Cdd:PRK13636 104 VsfGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL 183
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGAGIVVTS 200
Cdd:PRK13636 184 LVEMQKELGLTIIIAT 199
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-175 |
6.05e-15 |
|
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: 72.63 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQD--LRLFGELTVAENI 108
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRR-VQMVFQDpySSLNPRMTVGDII 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 109 --GLKN--ELTHFKTQEQIGRMLEAAG----IADKRdvPVEkLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDA 175
Cdd:COG1123 366 aePLRLhgLLSRAERRERVAELLERVGlppdLADRY--PHE-LSGGQRQRVAIARAlALEP-KLLILDEPTSALDV 437
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
31-192 |
6.06e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI-- 108
Cdd:PRK09452 36 TINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA------ENRHVNTVFQSYALFPHMTVFENVaf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNElthfKT-QEQIG-------RMLEAAGIADKRdvpVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAangKL 180
Cdd:PRK09452 110 GLRMQ----KTpAAEITprvmealRMVQLEEFAQRK---PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY---KL 179
|
170
....*....|..
gi 1681973554 181 LSGMLLEEAQAQ 192
Cdd:PRK09452 180 RKQMQNELKALQ 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
33-175 |
7.40e-15 |
|
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: 70.61 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAaWSGLRRRSLSMLFQDLrlFGEL----TVAENI 108
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR-LRKIRRKEIQMVFQDP--MSSLnprmTIGEQI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 109 G---LKNELTHFKTQEQIGRMLEAAGIADKRDV----PVEkLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDA 175
Cdd:cd03257 106 AeplRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnryPHE-LSGGQRQRVAIARALaLNP-KLLIADEPTSALDV 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
28-198 |
8.94e-15 |
|
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: 69.17 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgFSAAAWSGLRRRsLSMLFQDLRLFGElTVA 105
Cdd:cd03246 19 RNVSFSiePGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAD---ISQWDPNELGDH-VGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIglknelthfktqeqigrmleaagiadkrdvpvekLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmL 185
Cdd:cd03246 94 ENI----------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQ-A 138
|
170
....*....|...
gi 1681973554 186 LEEAQAQGAGIVV 198
Cdd:cd03246 139 IAALKAAGATRIV 151
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
31-200 |
9.26e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 70.50 E-value: 9.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADC-----------------RGFSAAAW----SGLRRRsl 89
Cdd:COG1121 28 TIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarrrigyvpqraevdWDFPITVRdvvlMGRYGR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 90 smlfqdLRLFGELTVAEniglknelthfktQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEP 169
Cdd:COG1121 106 ------RGLFRRPSRAD-------------REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEP 166
|
170 180 190
....*....|....*....|....*....|.
gi 1681973554 170 VSHLDAANGKLLSGmLLEEAQAQGAGIVVTS 200
Cdd:COG1121 167 FAGVDAATEEALYE-LLRELRREGKTILVVT 196
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
44-175 |
1.38e-14 |
|
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: 70.85 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDY---TGKILFDGADCRGFSAAAWSGLRRRSLSMLFQD------------------LRLFGEL 102
Cdd:COG0444 40 SGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKIRGREIQMIFQDpmtslnpvmtvgdqiaepLRIHGGL 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 103 TVAEniglknelthfkTQEQIGRMLEAAGIADKRDV----PVEkLSFGQQQRVAFIR-CMCQPfDFILLDEPVSHLDA 175
Cdd:COG0444 120 SKAE------------ARERAIELLERVGLPDPERRldryPHE-LSGGMRQRVMIARaLALEP-KLLIADEPTTALDV 183
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
43-196 |
1.43e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 70.28 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglrRRSLsmLFQDLRLFGELTVAENI--GLK-NELTHFKT 119
Cdd:COG4525 41 ASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-------DRGV--VFQKDALLPWLNVLDNVafGLRlRGVPKAER 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 120 QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAANGKLLSGMLLEEAQAQGAGI 196
Cdd:COG4525 112 RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALaADP-RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGV 188
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-174 |
1.44e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.60 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 24 GVWSQEVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELT 103
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 104 VAENIGLKNELTHFKTQEQIGRMLEA---AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDAlrqVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
43-177 |
1.69e-14 |
|
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: 69.52 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSL---CHFLYGIRED--YTGKILFDGADCRGFSAAAWSgLRRRsLSMLFQDLRLFgELTVAENI--GLK--NE 113
Cdd:cd03260 34 PSGCGKSTLlrlLNRLNDLIPGapDEGEVLLDGKDIYDLDVDVLE-LRRR-VGMVFQKPNPF-PGSIYDNVayGLRlhGI 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 114 LTHFKTQEQIGRMLEAAGIAD--KRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:cd03260 111 KLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIS 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
35-198 |
1.73e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaaawsglRRRSLSMLFQDLRLFG-------ELTVAEN 107
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP------------IRRQRDEYHQDLLYLGhqpgiktELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLle 187
Cdd:PRK13538 95 LRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL-- 172
|
170
....*....|.
gi 1681973554 188 EAQAQGAGIVV 198
Cdd:PRK13538 173 AQHAEQGGMVI 183
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-192 |
1.76e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREdYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFgELTVAENIGLKNeltHFKTQEQ 122
Cdd:PRK11174 384 PSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESW----RKHLSWVGQNPQLP-HGTLRDNVLLGN---PDASDEQ 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 123 IGRMLEAAGIAD--KR-----DVPVEK----LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAQA 191
Cdd:PRK11174 455 LQQALENAWVSEflPLlpqglDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR 534
|
.
gi 1681973554 192 Q 192
Cdd:PRK11174 535 Q 535
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-200 |
2.19e-14 |
|
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: 71.01 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIRE--DYTGKILFDGADCRgfsAAAWSGLRRRSLSMLFQDLRLFGELTVAEN 107
Cdd:TIGR02633 22 LEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLK---ASNIRDTERAGIVIIHQELTLVPELSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELTH----------FKTQEQIGRMLEAAGIADKRdvPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:TIGR02633 99 IFLGNEITLpggrmaynamYLRAKNLLRELQLDADNVTR--PVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKE 176
|
170 180
....*....|....*....|...
gi 1681973554 178 GKLLSGmLLEEAQAQGAGIVVTS 200
Cdd:TIGR02633 177 TEILLD-IIRDLKAHGVACVYIS 198
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-200 |
2.88e-14 |
|
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: 68.93 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglrRRSLSMLFQDLRLFGELTVAEN 107
Cdd:cd03266 24 VSFTvkPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-----RRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELTHFKTQEQIGRMLEAA---GIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGm 184
Cdd:cd03266 99 LEYFAGLYGLKGDELTARLEELAdrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE- 177
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGAGIVVTS 200
Cdd:cd03266 178 FIRQLRALGKCILFST 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
43-177 |
3.40e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.58 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFgELTVAENIGLKNELThfkTQEQ 122
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQDTFLF-SGTIRENIRYGRPDA---TDEE 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 123 IGRMLEAAGIAD-------KRDVPVE----KLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:COG1132 446 VEEAAKAAQAHEfiealpdGYDTVVGergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-174 |
4.56e-14 |
|
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: 68.34 E-value: 4.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYG-IREDyTGKILFDGADcrgFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPD-SGKILLDGQD---ITKLPMHKRARLGIGYLPQEASIFRKLTVEENI 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 109 GLKNELTHFKTQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03218 97 LAVLEIRGLSKKEREEKleeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-176 |
4.83e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENI--GLK- 111
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGVGMVFQSYALYPHLSVAENMsfGLKl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 112 -----NELThfKTQEQIGRMLEAAGIADKRdvPvEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK11000 103 agakkEEIN--QRVNQVAEVLQLAHLLDRK--P-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-174 |
5.45e-14 |
|
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: 70.10 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIrEDYTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDlrLFGEL----TVAENIG-----LKNEL 114
Cdd:COG4172 321 SGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQD--PFGSLsprmTVGQIIAeglrvHGPGL 396
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 115 THFKTQEQIGRMLEAAGI-ADKRD-VPVEkLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLD 174
Cdd:COG4172 397 SAAERRARVAEALEEVGLdPAARHrYPHE-FSGGQRQRIAIARALIlEP-KLLVLDEPTSALD 457
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-174 |
7.51e-14 |
|
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: 68.99 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 38 CLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI--GLKnELT 115
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLryGMK-RAR 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 116 HFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:TIGR02142 105 PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
31-173 |
1.10e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGE-YCLL-EaaSGTGKTSLCHFLYGIredYT---GKILFDGADCRGFS-AAAwsglRRRSLSMLFQDLRLFGELTV 104
Cdd:COG3845 27 TVRPGEiHALLgE--NGAGKSTLMKILYGL---YQpdsGEILIDGKPVRIRSpRDA----IALGIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 105 AENIGLKNELTHF------KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL 173
Cdd:COG3845 98 AENIVLGLEPTKGgrldrkAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
30-199 |
1.26e-13 |
|
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: 65.73 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQdlrlfgeltvaenig 109
Cdd:cd00267 20 LTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----RRRIGYVPQ--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 lknelthfktqeqigrmleaagiadkrdvpvekLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEA 189
Cdd:cd00267 81 ---------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELA 127
|
170
....*....|
gi 1681973554 190 QAQGAGIVVT 199
Cdd:cd00267 128 EEGRTVIIVT 137
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-205 |
1.30e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGfsAAAWSGLRRRSLSMLFQDLRLFGELTVAENI- 108
Cdd:PRK09493 22 LNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND--PKVDERLIRQEAGMVFQQFYLFPHLTALENVm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -------GLKNElthfKTQEQIGRMLEAAGIADKRD-VPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA-NGK 179
Cdd:PRK09493 100 fgplrvrGASKE----EAEKQARELLAKVGLAERAHhYPSE-LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElRHE 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1681973554 180 LLSGM--LLEEAQAQgagIVVT-------SVGSRL 205
Cdd:PRK09493 175 VLKVMqdLAEEGMTM---VIVTheigfaeKVASRL 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-181 |
1.34e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIRE--DYTGKILFDGADCRGfsaaawSGLR---RRSLSMLFQDLRLFGELTVAEN 107
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQA------SNIRdteRAGIAIIHQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELTHF------KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLL 181
Cdd:PRK13549 103 IFLGNEITPGgimdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL 182
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
31-199 |
2.88e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGL 110
Cdd:PRK10247 29 SLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELTHFKTQEQ-IGRMLEAAGIADKR-DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEE 188
Cdd:PRK10247 104 PWQIRNQQPDPAiFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRY 183
|
170
....*....|..
gi 1681973554 189 AQAQGAGIV-VT 199
Cdd:PRK10247 184 VREQNIAVLwVT 195
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
33-174 |
3.03e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 66.36 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSL---CHFLygirEDYT-GKILFDGADCR-------GFSAAAWSGLRR-RS-LSMLFQDLRLF 99
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFlrcINLL----ETPDsGEIRVGGEEIRlkpdrdgELVPADRRQLQRiRTrLGMVFQSFNLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 100 GELTVAENI--------GL-KNElthfkTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPV 170
Cdd:COG4598 108 SHMTVLENVieapvhvlGRpKAE-----AIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
....
gi 1681973554 171 SHLD 174
Cdd:COG4598 183 SALD 186
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-187 |
3.57e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 40 LEAASGTGKTSLCHFLYGIREDY-----TGKILFDGADCRGFSAaawSGLRRRsLSMLFQDLRLFGELTVAENI--GLK- 111
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDV---IELRRR-VQMVFQIPNPIPNLSIFENValGLKl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 112 NELTHFKT--QEQIGRMLEAAG----IADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGML 185
Cdd:PRK14247 110 NRLVKSKKelQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF 189
|
..
gi 1681973554 186 LE 187
Cdd:PRK14247 190 LE 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
35-175 |
3.83e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglRRRSLSMLFQDLRLFGELTVAENI--GLK- 111
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQHYALFRHMTVFDNIafGLTv 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 112 -------NELTHFKTQEQIGRMLEAAGIADKrdVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK10851 102 lprrerpNAAAIKAKVTQLLEMVQLAHLADR--YPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-199 |
4.31e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYG-IREDYTG----KILFDGADCRGFSAAAWSGLRRRSlSMLFQDLRLFGELT 103
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLSGlITGDKSAgshiELLGRTVQREGRLARDIRKSRANT-GYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 104 VAEN--IGLKNELTHFKT------QEQIGRMLEA---AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSH 172
Cdd:PRK09984 103 VLENvlIGALGSTPFWRTcfswftREQKQRALQAltrVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180
....*....|....*....|....*..
gi 1681973554 173 LDAANGKLLSGMLLEEAQAQGAGIVVT 199
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITVVVT 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
34-176 |
8.04e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.98 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsGLR--RRSLSMLFQDLRLFGELTVAENIGLK 111
Cdd:PRK11153 30 AGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEK---ELRkaRRQIGMIFQHFNLLSSRTVFDNVALP 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 112 NELTHfKTQEQIGR----MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAA 176
Cdd:PRK11153 107 LELAG-TPKAEIKArvteLLELVGLSDKADRYPAQLSGGQKQRVAIARALaSNP-KVLLCDEATSALDPA 174
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-174 |
1.47e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.63 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ---IARMGVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 ------GLKNELTH--FKT-------QEQIGRM---LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPV 170
Cdd:PRK11300 102 lvaqhqQLKTGLFSglLKTpafrraeSEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
....
gi 1681973554 171 SHLD 174
Cdd:PRK11300 182 AGLN 185
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
33-169 |
1.50e-12 |
|
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: 63.99 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQDLRLFGELTVAENI--GL 110
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE---RARAGIGYVPEGRRIFPELTVEENLllGA 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 111 KNeLTHFKTQEQIGRMLEAAGI-ADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEP 169
Cdd:cd03224 101 YA-RRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARAlMSRP-KLLLLDEP 159
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-174 |
2.09e-12 |
|
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: 63.37 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLeAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfsaAAWSGLRRRsLSMLFQDLRLFGELTVAE---N 107
Cdd:cd03264 22 TLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRRR-IGYLPQEFGVYPNFTVREfldY 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 108 IGLKNELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03264 96 IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
45-215 |
3.04e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDG---ADCRGFSAAAWSGLRRRslsmlfqdlrLFGELTVAENI----GLKNElthf 117
Cdd:PRK13539 38 GSGKTTLLRLIAGLLPPAAGTIKLDGgdiDDPDVAEACHYLGHRNA----------MKPALTVAENLefwaAFLGG---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 118 kTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLEEAQAQGaGIV 197
Cdd:PRK13539 104 -EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE-LIRAHLAQG-GIV 180
|
170
....*....|....*...
gi 1681973554 198 VTSVGSRLGLPYHKTLTL 215
Cdd:PRK13539 181 IAATHIPLGLPGARELDL 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
45-174 |
3.92e-12 |
|
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: 63.01 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGLKNELThfkTQEQIG 124
Cdd:cd03254 39 GAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFSG-TIMENIRLGRPNA---TDEEVI 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1681973554 125 RMLEAAGIAD--KR------DVPVEK---LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03254 111 EAAKEAGAHDfiMKlpngydTVLGENggnLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
29-198 |
5.66e-12 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 62.91 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:TIGR03873 21 DVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRA----RARRVALVEQDSDTAVPLTVRDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -----------GLKNELTHFKTQEQIGRMlEAAGIADkRDVPVekLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD-AA 176
Cdd:TIGR03873 97 algriphrslwAGDSPHDAAVVDRALART-ELSHLAD-RDMST--LSGGERQRVHVARALAQEPKLLLLDEPTNHLDvRA 172
|
170 180
....*....|....*....|..
gi 1681973554 177 NGKLLSgmLLEEAQAQGAGIVV 198
Cdd:TIGR03873 173 QLETLA--LVRELAATGVTVVA 192
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-200 |
9.02e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.48 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYG-IREDyTGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENI 108
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPD-HGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 G--LKNeltHFKTQEQIGRM-----LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLL 181
Cdd:PRK11831 106 AypLRE---HTQLPAPLLHStvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170
....*....|....*....
gi 1681973554 182 SGMLLEEAQAQGAGIVVTS 200
Cdd:PRK11831 183 VKLISELNSALGVTCVVVS 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
44-200 |
1.02e-11 |
|
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: 60.91 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglRRRSLSMLFQDLR---LFGELTVAENIGLKNELthfktq 120
Cdd:cd03215 35 VGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYVPEDRKregLVLDLSVAENIALSSLL------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 121 eqigrmleaagiadkrdvpveklSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAqAQGAGIVVTS 200
Cdd:cd03215 106 -----------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLIS 161
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-200 |
1.75e-11 |
|
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: 62.46 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsAAAWS-GLRRRSLSMLFQDLRLFgELTVAENIGLKNELT------- 115
Cdd:COG4618 367 SGSGKSTLARLLVGVWPPTAGSVRLDGAD-----LSQWDrEELGRHIGYLPQDVELF-DGTIAENIARFGDADpekvvaa 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 116 ------HfktqEQIGRM-------LEAAGIAdkrdvpvekLSFGQQQRVAFIRCMC-QPFdFILLDEPVSHLDAANGKLL 181
Cdd:COG4618 441 aklagvH----EMILRLpdgydtrIGEGGAR---------LSGGQRQRIGLARALYgDPR-LVVLDEPNSNLDDEGEAAL 506
|
170
....*....|....*....
gi 1681973554 182 SGMlLEEAQAQGAGIVVTS 200
Cdd:COG4618 507 AAA-IRALKARGATVVVIT 524
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
32-174 |
2.05e-11 |
|
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: 61.16 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 32 FRKGEYCLLEAASGTGKTSLCHFL-------YGIRedYTGKILFDGADC--RGFSAAAwsgLRRRsLSMLFQDLRLFgEL 102
Cdd:TIGR00972 24 IPKNQVTALIGPSGCGKSTLLRSLnrmndlvPGVR--IEGKVLFDGQDIydKKIDVVE---LRRR-VGMVFQKPNPF-PM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 103 TVAENI--GLKNELTHFKTQ--EQIGRMLEAAGI----ADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:TIGR00972 97 SIYDNIayGPRLHGIKDKKEldEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPTSALD 176
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-174 |
2.11e-11 |
|
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: 61.09 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGLKNELThfkTQEQ 122
Cdd:cd03253 35 PSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVLFND-TIGYNIRYGRPDA---TDEE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 123 IGRMLEAAGIADK--------------RDVpveKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03253 107 VIEAAKAAQIHDKimrfpdgydtivgeRGL---KLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-200 |
2.22e-11 |
|
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: 62.13 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIrEDY---TGKIL----------------FDGADCR--------------G 75
Cdd:TIGR03269 20 SFTIEEGEVLGILGRSGAGKSVLMHVLRGM-DQYeptSGRIIyhvalcekcgyverpsKVGEPCPvcggtlepeevdfwN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 76 FSAAAWSGLRRRSLSMLFQDLRLFGELTVAENIGLKNELTHFKTQEQIGR---MLEAAGIADKRDVPVEKLSFGQQQRVA 152
Cdd:TIGR03269 99 LSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRavdLIEMVQLSHRITHIARDLSGGEKQRVV 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1681973554 153 FIRCMC-QPFDFiLLDEPVSHLDAANGKLLSGMLLEEAQAQGAGIVVTS 200
Cdd:TIGR03269 179 LARQLAkEPFLF-LADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
28-201 |
2.25e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIRE--DYTGKILFDGADCRgfsaaaWSGLR---RRSLSMLFQDLRLFG 100
Cdd:NF040905 18 DDVNLsvREGEIHALCGENGAGKSTLMKVLSGVYPhgSYEGEILFDGEVCR------FKDIRdseALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 101 ELTVAENIGLKNELTHF------KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL- 173
Cdd:NF040905 92 YLSIAENIFLGNERAKRgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALn 171
|
170 180
....*....|....*....|....*...
gi 1681973554 174 DAANGKLLSgmLLEEAQAQGagivVTSV 201
Cdd:NF040905 172 EEDSAALLD--LLLELKAQG----ITSI 193
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-187 |
2.70e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYT------GKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGELTVAENIGLKNELTHF 117
Cdd:PRK14246 45 SGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 118 KTQEQIGRMLEAA--------GIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLE 187
Cdd:PRK14246 121 KEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-200 |
2.81e-11 |
|
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: 60.31 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsgLRRrsLSMLFQDLRLFGELTVAENIGL 110
Cdd:cd03268 22 HVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA----LRR--IGALIEAPGFYPNLTARENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELTHFKTQEqIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAq 190
Cdd:cd03268 96 LARLLGIRKKR-IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR- 173
|
170
....*....|
gi 1681973554 191 AQGAGIVVTS 200
Cdd:cd03268 174 DQGITVLISS 183
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
44-176 |
3.50e-11 |
|
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: 61.27 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYG--------IREDytGKILFDGAdcRGFSAAAWsglrRRSLSMLFQDLRLFGELTVAENI--GLKNE 113
Cdd:COG4148 34 SGSGKTTLLRAIAGlerpdsgrIRLG--GEVLQDSA--RGIFLPPH----RRRIGYVFQEARLFPHLSVRGNLlyGRKRA 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 114 LTHFKTQ--EQIGRMLeaaGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLDAA 176
Cdd:COG4148 106 PRAERRIsfDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRAlLSSP-RLLLMDEPLAALDLA 167
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
35-199 |
3.94e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI------ 108
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNVevpavy 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -GLKNELTHFKTQEQIGRMleaaGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLE 187
Cdd:PRK10535 114 aGLERKQRLLRAQELLQRL----GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMA-ILH 188
|
170
....*....|...
gi 1681973554 188 EAQAQG-AGIVVT 199
Cdd:PRK10535 189 QLRDRGhTVIIVT 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
30-200 |
5.40e-11 |
|
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: 59.47 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaAAWSGLR------RRSLSMLFqdlrlfgELT 103
Cdd:cd03235 20 FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------LEKERKRigyvpqRRSIDRDF-------PIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 104 VAENI--GLKNELTHFKTQEQIGR-----MLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:cd03235 87 VRDVVlmGLYGHKGLFRRLSKADKakvdeALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180
....*....|....*....|....
gi 1681973554 177 NGKLLSGmLLEEAQAQGAGIVVTS 200
Cdd:cd03235 167 TQEDIYE-LLRELRREGMTILVVT 189
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-174 |
6.42e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.63 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 23 SGVwsqEVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSglrrRSLSMLFQDLRLFGEL 102
Cdd:PRK09536 20 DGV---DLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 103 TVAENI--GLKNELTHFKTQEQIG-----RMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK09536 93 DVRQVVemGRTPHRSRFDTWTETDraaveRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
30-198 |
8.30e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsAAAWSGLRR-RSLSMLFQDLRLFGELTVAENI 108
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-----LADWSPAELaRRRAVLPQHSSLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GL---KNELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQ------PFDFILLDEPVSHLDAANGK 179
Cdd:PRK13548 98 AMgraPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQH 177
|
170
....*....|....*....
gi 1681973554 180 LLSGMLLEEAQAQGAGIVV 198
Cdd:PRK13548 178 HVLRLARQLAHERGLAVIV 196
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-198 |
9.32e-11 |
|
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: 59.40 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGfsaaawSGLRRRslsMLFQDLRLFGELTVAENI 108
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE------PGPDRM---VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GL--KNELTHFKTQEQ---IGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSG 183
Cdd:TIGR01184 76 ALavDRVLPDLSKSERraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170
....*....|....*
gi 1681973554 184 MLLEEAQAQGAGIVV 198
Cdd:TIGR01184 156 ELMQIWEEHRVTVLM 170
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-199 |
1.01e-10 |
|
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: 58.66 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 21 RDSGVWSQEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCrGFSAAAWSglrrRSLSMLFQDLRL 98
Cdd:cd03231 10 RDGRALFSGLSFTlaAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIA----RGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 99 FGELTVAENIGLkneLTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANG 178
Cdd:cd03231 85 KTTLSVLENLRF---WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|.
gi 1681973554 179 KLLSGMLLEEAQAQGAGIVVT 199
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTT 182
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
30-199 |
1.08e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI- 108
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDED---ISLLPLHARARRGIGYLPQEASIFRRLSVYDNLm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 ---GLKNELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANgKLLSGML 185
Cdd:PRK10895 101 avlQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS-VIDIKRI 179
|
170
....*....|....
gi 1681973554 186 LEEAQAQGAGIVVT 199
Cdd:PRK10895 180 IEHLRDSGLGVLIT 193
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-174 |
1.48e-10 |
|
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: 58.54 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKilfdgADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAE 106
Cdd:cd03265 18 GVSFrvRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR-----ATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 107 NI-------GLKNElthfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03265 93 NLyiharlyGVPGA----ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-187 |
1.97e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.09 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDG--------ADcrgfsaaawsglrrRSLSMLFQDLRLFGE 101
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelepAD--------------RDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 102 LTVAENI--GLKNELThfkTQEQIG-RMLEAAGIA------DKRdvPVEkLSFGQQQRVAFIRCMC-QPFDFiLLDEPVS 171
Cdd:PRK11650 91 MSVRENMayGLKIRGM---PKAEIEeRVAEAARILelepllDRK--PRE-LSGGQRQRVAMGRAIVrEPAVF-LFDEPLS 163
|
170
....*....|....*.
gi 1681973554 172 HLDAangKLLSGMLLE 187
Cdd:PRK11650 164 NLDA---KLRVQMRLE 176
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-174 |
2.55e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGAD---CRGFSAAAWSGLRRRsLSMLFQDLRLFGEL 102
Cdd:COG4161 19 FDINLEcpSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLLRQK-VGMVFQQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 103 TVAENI--------GLKNElthfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHL 173
Cdd:COG4161 98 TVMENLieapckvlGLSKE----QAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAlMMEP-QVLLFDEPTAAL 172
|
.
gi 1681973554 174 D 174
Cdd:COG4161 173 D 173
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-205 |
2.56e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.87 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAENI 108
Cdd:PRK10584 30 ELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNEL---THFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGML 185
Cdd:PRK10584 110 ELPALLrgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180
....*....|....*....|
gi 1681973554 186 LEEAQAQGAGIVVTSVGSRL 205
Cdd:PRK10584 190 FSLNREHGTTLILVTHDLQL 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
45-169 |
3.28e-10 |
|
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: 57.68 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQDLRLFGELTVAEN--IGLKNELTHFKTQEQ 122
Cdd:COG0410 39 GAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR---IARLGIGYVPEGRRIFPSLTVEENllLGAYARRDRAEVRAD 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 123 IGRMLEaagI----ADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEP 169
Cdd:COG0410 116 LERVYE---LfprlKERRRQRAGTLSGGEQQMLAIGRAlMSRP-KLLLLDEP 163
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
45-198 |
3.50e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.10 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSglrrRSLSMLFQDLRLFGELTVAENI--GLKNELTHF----- 117
Cdd:PRK11231 38 GCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHLTPEGITVRELVayGRSPWLSLWgrlsa 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 118 KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLEEAQAQGAGIV 197
Cdd:PRK11231 114 EDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR-LMRELNTQGKTVV 192
|
.
gi 1681973554 198 V 198
Cdd:PRK11231 193 T 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-174 |
3.87e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.84 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSL--CHFLYGIREDYT---GKILFDGADCRGFSAAAWSGLRRRsLSMLFQDLRLFGELTVAEN 107
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTARSLSQQKGLIRQLRQH-VGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 108 I-----GLKNELThfKTQEQIGRMLEA-AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK11264 106 IiegpvIVKGEPK--EEATARARELLAkVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
44-175 |
4.14e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILfdgADCRGFSAAawsglrRRSLSMLFQDLRLFGELTVAENIGLKneLT-HFKTQEQ 122
Cdd:PRK11247 47 SGCGKSTLLRLLAGLETPSAGELL---AGTAPLAEA------REDTRLMFQDARLLPWKKVIDNVGLG--LKgQWRDAAL 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 123 igRMLEAAGIADK-RDVPVeKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK11247 116 --QALAAVGLADRaNEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
30-193 |
4.95e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLrRRSLSMLFQDlrLFGEL----TVA 105
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF-RRDIQMVFQD--SISAVnprkTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIG--LKNeLTHFKTQEQIGR---MLEAAG----IADKRDvpvEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK10419 110 EIIRepLRH-LLSLDKAERLARaseMLRAVDlddsVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170
....*....|....*....
gi 1681973554 177 ngkLLSGM--LLEEAQAQG 193
Cdd:PRK10419 186 ---LQAGVirLLKKLQQQF 201
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
44-174 |
7.01e-10 |
|
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: 56.73 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFsaaawsGLR--RRSLSMLFQDLRLFgELTVAENIGLKNElthfKTQE 121
Cdd:cd03244 39 TGSGKSSLLLALFRLVELSSGSILIDGVDISKI------GLHdlRSRISIIPQDPVLF-SGTIRSNLDPFGE----YSDE 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 122 QIGRMLEAAGI-------ADKRDVPVEK----LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03244 108 ELWQALERVGLkefveslPGGLDTVVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
30-187 |
1.39e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglrRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:TIGR01257 951 ITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV-----RQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNEL---THFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLL 186
Cdd:TIGR01257 1026 FYAQLkgrSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
.
gi 1681973554 187 E 187
Cdd:TIGR01257 1106 K 1106
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-200 |
1.83e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGADCRgFSAAAWSglRRRSLSMLFQDLRLFGELTVAENIGLKNELTHF------- 117
Cdd:PRK10762 40 GAGKSTMMKVLTGIYTRDAGSILYLGKEVT-FNGPKSS--QEAGIGIIHQELNLIPQLTIAENIFLGREFVNRfgridwk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 118 KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL-DAANGKLLSgmLLEEAQAQGAGI 196
Cdd:PRK10762 117 KMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR--VIRELKSQGRGI 194
|
....
gi 1681973554 197 VVTS 200
Cdd:PRK10762 195 VYIS 198
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-179 |
3.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.38 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawSGLrRRSLSMLFQDLRL-FGELTVAENI 108
Cdd:PRK13644 23 LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKL--QGI-RKLVGIVFQNPETqFVGRTVEEDL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 109 GLKNE---LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:PRK13644 100 AFGPEnlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
34-174 |
3.92e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKI-----LFDgadcrgFSAAAWSG---LRRRSLSMLFQDLRLFGELTVA 105
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFD------FSKTPSDKairELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 106 ENI--------GLKNElthfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLD 174
Cdd:PRK11124 101 QNLieapcrvlGLSKD----QALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAlMMEP-QVLLFDEPTAALD 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
31-174 |
3.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 55.10 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGAdcRGFSAAAWSglRRRSLSMLFQ--DLRLFGElTVAENI 108
Cdd:PRK13642 29 SITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE--LLTAENVWN--LRRKIGMVFQnpDNQFVGA-TVEDDV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 109 GLKNELTHFKTQEQIGRMLEA---AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEAllaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-180 |
4.75e-09 |
|
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: 54.47 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKT---SLCHFLYGIREdytGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFgELTVAEN 107
Cdd:cd03249 25 TIPPGKTVALVGSSGCGKStvvSLLERFYDPTS---GEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLF-DGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGL-KNELThfktQEQIGRMLEAAGI-------ADKRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03249 97 IRYgKPDAT----DEEVEEAAKKANIhdfimslPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
....*
gi 1681973554 176 ANGKL 180
Cdd:cd03249 173 ESEKL 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-174 |
5.36e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 54.74 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfSAAAWSglRRRSLSMLFQ--DLRLFGElTV 104
Cdd:PRK13650 25 DVSFhvKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVWD--IRHKIGMVFQnpDNQFVGA-TV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 105 AENI--GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13650 100 EDDVafGLENKgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-174 |
5.90e-09 |
|
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: 54.41 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 22 DSGVWSQEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCrGFSAAAWsglRRRSLSMLFQDLRLF 99
Cdd:cd03252 13 DGPVILDNISLRikPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADPAW---LRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 100 GElTVAENIGLKNELTHFKtqeqigRMLEAAGIADKRDVPVE--------------KLSFGQQQRVAFIRCMCQPFDFIL 165
Cdd:cd03252 89 NR-SIRDNIALADPGMSME------RVIEAAKLAGAHDFISElpegydtivgeqgaGLSGGQRQRIAIARALIHNPRILI 161
|
....*....
gi 1681973554 166 LDEPVSHLD 174
Cdd:cd03252 162 FDEATSALD 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-200 |
6.56e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLrrrSLSMLFQDLRLFGELTVAENIGL 110
Cdd:PRK09700 27 TVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL---GIGIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KNELT----------HFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL-DAANGK 179
Cdd:PRK09700 104 GRHLTkkvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDY 183
|
170 180
....*....|....*....|.
gi 1681973554 180 LLsgMLLEEAQAQGAGIVVTS 200
Cdd:PRK09700 184 LF--LIMNQLRKEGTAIVYIS 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
33-169 |
1.05e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQDLRLFGELTVAENI---G 109
Cdd:PRK11614 29 NQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK---IMREAVAIVPEGRRVFSRMTVEENLamgG 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 110 LKNELTHFktQEQIGRMLEA-AGIADKRDVPVEKLSFGQQQRVAFIRC-MCQPfDFILLDEP 169
Cdd:PRK11614 106 FFAERDQF--QERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRAlMSQP-RLLLLDEP 164
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-176 |
1.11e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAEN 107
Cdd:PRK13657 354 VSFeaKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IglknelthfktqeQIGR-------MLEAAGIA----------DKRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILL 166
Cdd:PRK13657 429 I-------------RVGRpdatdeeMRAAAERAqahdfierkpDGYDTVVgergRQLSGGERQRLAIARALLKDPPILIL 495
|
170
....*....|
gi 1681973554 167 DEPVSHLDAA 176
Cdd:PRK13657 496 DEATSALDVE 505
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
34-200 |
1.36e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 53.54 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGA----DCRGFSAAawsglrRRSLSMLFQ--DLRLFGElTVAE- 106
Cdd:PRK13639 27 KGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKSLLEV------RKTVGIVFQnpDDQLFAP-TVEEd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 107 ------NIGLKNElthfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDaANGKL 180
Cdd:PRK13639 100 vafgplNLGLSKE----EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLD-PMGAS 174
|
170 180
....*....|....*....|
gi 1681973554 181 LSGMLLEEAQAQGAGIVVTS 200
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIIST 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
32-200 |
1.45e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 32 FRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGadcRGFSAAAWSGLRRRsLSMLFQDL--RLFGElTVAENI- 108
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG---REVNAENEKWVRSK-VGLVFQDPddQVFSS-TVWDDVa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 -GLKN-ELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAnGKLLSGMLL 186
Cdd:PRK13647 103 fGPVNmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR-GQETLMEIL 181
|
170
....*....|....
gi 1681973554 187 EEAQAQGAGIVVTS 200
Cdd:PRK13647 182 DRLHNQGKTVIVAT 195
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
43-199 |
1.47e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.43 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCR----------GFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENI---- 108
Cdd:PRK10619 39 SSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTR-LTMVFQHFNLWSHMTVLENVmeap 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 ----GLKNElthfKTQEQIGRMLEAAGIADKRDV--PVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA-NGKLL 181
Cdd:PRK10619 118 iqvlGLSKQ----EARERAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARALAMEPEVLLFDEPTSALDPElVGEVL 192
|
170 180
....*....|....*....|
gi 1681973554 182 SGM--LLEEAQAQgagIVVT 199
Cdd:PRK10619 193 RIMqqLAEEGKTM---VVVT 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-215 |
1.78e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.66 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILF-DGADcrgfsaaawsglrrrslsMLF--QDLRLfGELTVAE 106
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR------------------VLFlpQRPYL-PLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 107 NIGLKNELTHFkTQEQIGRMLEAAG---IADKRDVPV---EKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAANGK 179
Cdd:COG4178 445 ALLYPATAEAF-SDAELREALEAVGlghLAERLDEEAdwdQVLSLGEQQRLAFARLLlHKP-DWLFLDEATSALDEENEA 522
|
170 180 190
....*....|....*....|....*....|....*...
gi 1681973554 180 LLSGMLLEEAqaqgAGIVVTSVGSRLGL-PYH-KTLTL 215
Cdd:COG4178 523 ALYQLLREEL----PGTTVISVGHRSTLaAFHdRVLEL 556
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-200 |
1.81e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDgadcrgfsaaawsglrrrslsmlFQDLRLFGELTVAENI 108
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----------------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNELThfktqeQIGRMLEAAGIAD----KRdvPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGM 184
Cdd:COG2401 107 GRKGDFK------DAVELLNAVGLSDavlwLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGAGIVVTS 200
Cdd:COG2401 179 LQKLARRAGITLVVAT 194
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-168 |
2.07e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgFSAAAWSGLRRRsLSMLFQDLRLFGELTVAENIGL 110
Cdd:PRK10522 345 TIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKP---VTAEQPEDYRKL-FSAVFTDFHLFDQLLGPEGKPA 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 111 KNELthfktqeqIGRMLEAAGIADKrdVPVE-------KLSFGQQQRVAFIRCMCQPFDFILLDE 168
Cdd:PRK10522 421 NPAL--------VEKWLERLKMAHK--LELEdgrisnlKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
44-174 |
3.41e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSgLRRRSLSMLFQDLrlFGEL--------TVAENIGLKNELT 115
Cdd:PRK11308 50 SGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK-LLRQKIQIVFQNP--YGSLnprkkvgqILEEPLLINTSLS 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 116 HFKTQEQIGRMLEAAGI----ADKrdVPvEKLSFGQQQRVAFIRC-MCQPfDFILLDEPVSHLD 174
Cdd:PRK11308 127 AAERREKALAMMAKVGLrpehYDR--YP-HMFSGGQRQRIAIARAlMLDP-DVVVADEPVSALD 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-193 |
3.72e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSglrrRSLSMLFQDLRLFGELTVAENIG 109
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 L-----KNELTHFKTQEQ--IGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLS 182
Cdd:PRK10253 104 RgryphQPLFTRWRKEDEeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170
....*....|.
gi 1681973554 183 GMLLEEAQAQG 193
Cdd:PRK10253 184 ELLSELNREKG 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
45-169 |
4.71e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYGIREDYTGKILFDGADCRGFS-AAAwsglRRRSLSMLFQDLR---LFGELTVAENIGLKN--ELTHF- 117
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDA----IRAGIAYVPEDRKgegLVLDLSIRENITLASldRLSRGg 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 118 -----KTQEQIGRMLEAAGI-ADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEP 169
Cdd:COG1129 364 lldrrRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
31-175 |
5.07e-08 |
|
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: 50.77 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsAAAWSGLRRRSLSMLFQDLRLFGElTVAENIGl 110
Cdd:cd03247 24 ELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----VSDLEKALSSLISVLNQRPYLFDT-TLRNNLG- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 111 knelthfktqeqigrmleaagiadkrdvpvEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03247 97 ------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-175 |
5.25e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAW--SGLrrrslSMLFQDLRLFGELT 103
Cdd:PRK11288 21 DDISFdcRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlaAGV-----AIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 104 VAENIGL-----KNELTHFKT-QEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK11288 96 VAENLYLgqlphKGGIVNRRLlNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
28-197 |
7.44e-08 |
|
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: 50.90 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGireDY---TGKILFDGADCRGFSAAA----WSGLRRRSLSMLFQDLRL 98
Cdd:COG4778 28 DGVSFsvAAGECVALTGPSGAGKSTLLKCIYG---NYlpdSGSILVRHDGGWVDLAQAspreILALRRRTIGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 99 FGELT----VAENIgLKNELTHFKTQEQIGRMLEAAGIADKR-DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL 173
Cdd:COG4778 105 IPRVSaldvVAEPL-LERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASL 183
|
170 180
....*....|....*....|....*
gi 1681973554 174 DAAN-GKLLSgmLLEEAQAQGAGIV 197
Cdd:COG4778 184 DAANrAVVVE--LIEEAKARGTAII 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-174 |
1.03e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 51.25 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSgLRRRSLSMLFQD--LRLFGELTVA 105
Cdd:PRK15079 40 VTLRlyEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR-AVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 106 ENIG--LKN---ELTHFKTQEQIGRMLEAAGIADK--RDVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK15079 119 EIIAepLRTyhpKLSRQEVKDRVKAMMLKVGLLPNliNRYPHE-FSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
43-199 |
1.37e-07 |
|
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: 49.86 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFL--YGIREDYTGKILFDGADcrgFSAAAWsglrRRSLSMLFQDLRLFGELTVAENiglknelthfktq 120
Cdd:cd03213 43 PSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSF----RKIIGYVPQDDILHPTLTVRET------------- 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1681973554 121 eqigrMLEAAGIadkrdvpvEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEAQaQGAGIVVT 199
Cdd:cd03213 103 -----LMFAAKL--------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICS 167
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
31-175 |
1.44e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAaawsglrrrSLSMLFQDLRLFGELTVAENIGL 110
Cdd:PRK11248 23 TLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---------ERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 111 KNELTHFKTQEQI---GRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK11248 94 GLQLAGVEKMQRLeiaHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-200 |
1.46e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 40 LEAASGTGKTSLCHFLYGIREDYTGKILFDGADC----RGFSAAawsglrRRSLSMLFQDLR---LFGELTVAENIGLKN 112
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLAL------RQQVATVFQDPEqqiFYTDIDSDIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 113 ELThfkTQEQIGRML-EAAGIADK---RDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAnGKLLSGMLLEE 188
Cdd:PRK13638 106 LGV---PEAEITRRVdEALTLVDAqhfRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA-GRTQMIAIIRR 181
|
170
....*....|..
gi 1681973554 189 AQAQGAGIVVTS 200
Cdd:PRK13638 182 IVAQGNHVIISS 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-182 |
1.57e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.52 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGadcrgfSAAAWSGLR--RRSLSMLFQ--DLRLFGEl 102
Cdd:PRK13648 27 DVSFNipKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN------QAITDDNFEklRKHIGIVFQnpDNQFVGS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 103 TVAENI--GLKNELT-HFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD-AANG 178
Cdd:PRK13648 100 IVKYDVafGLENHAVpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDpDARQ 179
|
....
gi 1681973554 179 KLLS 182
Cdd:PRK13648 180 NLLD 183
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
30-175 |
1.75e-07 |
|
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: 49.96 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGE-YCLLeAASGTGKTSLCHFLYG-IREDYT--GKILFDGadcRGFSAAAWsglrRRSLSMLFQDLRLFGELTVA 105
Cdd:cd03234 28 LHVESGQvMAIL-GSSGSGKTTLLDAISGrVEGGGTtsGQILFNG---QPRKPDQF----QKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 106 ENI--GLKNELTHFKTQEQIGRM-----LEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:cd03234 100 ETLtyTAILRLPRKSSDAIRKKRvedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
31-197 |
2.09e-07 |
|
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: 48.96 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGE-YCLLeAASGTGKTSLCHFLYGIREDYTGKILFDGadcrgfsaaawsglrrrslsmlfqdlrlfgeltvaenig 109
Cdd:cd03216 22 SVRRGEvHALL-GENGAGKSTLMKILSGLYKPDSGEILVDG--------------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 lknELTHFKTQeqigRMLEAAGIAdkrdvPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLEEA 189
Cdd:cd03216 62 ---KEVSFASP----RDARRAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIRRL 128
|
....*...
gi 1681973554 190 QAQGAGIV 197
Cdd:cd03216 129 RAQGVAVI 136
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
141-215 |
2.10e-07 |
|
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: 49.07 E-value: 2.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 141 EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLleeaqaQGAGIVVTSVGSRLGLP--YHKTLTL 215
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL------KELGITVISVGHRPSLWkfHDRVLDL 160
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
140-199 |
2.50e-07 |
|
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: 48.21 E-value: 2.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 140 VEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEEaqaQGAGIVVT 199
Cdd:cd03221 68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY---PGTVILVS 124
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
45-169 |
2.76e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.26 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 45 GTGKTSLCHFLYG-IREDYtGKILFDGADCrgfsaaawSGL----R-RRSLSMLFQDLRLFGELTVAENIGLKNELTHFK 118
Cdd:COG1137 39 GAGKTTTFYMIVGlVKPDS-GRIFLDGEDI--------THLpmhkRaRLGIGYLPQEASIFRKLTVEDNILAVLELRKLS 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 119 TQEQIGRM---LEAAGIADKRDVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEP 169
Cdd:COG1137 110 KKEREERLeelLEEFGITHLRKSKAYSLSGGERRRVEIARALaTNP-KFILLDEP 163
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-215 |
2.93e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCrgfsaaawSGLRRRSLSMLFQDLRLFGELTVAENIG 109
Cdd:PRK13541 21 ITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI--------NNIAKPYCTYIGHNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELthFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLeeA 189
Cdd:PRK13541 93 FWSEI--YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV--M 168
|
170 180
....*....|....*....|....*.
gi 1681973554 190 QAQGAGIVVTSVGSRLGLPYHKTLTL 215
Cdd:PRK13541 169 KANSGGIVLLSSHLESSIKSAQILQL 194
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
30-215 |
3.04e-07 |
|
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: 48.95 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFsaaawsGLR--RRSLSMLFQDLRLFGElTVA 105
Cdd:cd03369 27 VSFKvkAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI------PLEdlRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIGLKNELThfktQEQIGRMLEAAGIADKrdvpvekLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGML 185
Cdd:cd03369 100 SNLDPFDEYS----DEEIYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|..
gi 1681973554 186 LEEaqAQGAGIVVtsVGSRLG--LPYHKTLTL 215
Cdd:cd03369 169 REE--FTNSTILT--IAHRLRtiIDYDKILVM 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-174 |
3.21e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGK-TSLCHFLYGIREDytGKILFDGADCRGFSAAAWSGLRRRsLSMLFQDL------RLFGELT 103
Cdd:PRK15134 308 TLRPGETLGLVGESGSGKsTTGLALLRLINSQ--GEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPnsslnpRLNVLQI 384
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 104 VAEniGLK---NELTHFKTQEQIGRMLEAAGI--ADKRDVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK15134 385 IEE--GLRvhqPTLSAAQREQQVIAVMEEVGLdpETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-174 |
3.26e-07 |
|
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: 49.33 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaaawsglrrrsLSMLFQDLRLFGELTVAENIG- 109
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------------VSYKPQYIKADYEGTVRDLLSs 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 110 -LKNELTHFKTQEQIGRMLEAAGIADKRdvpVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03237 85 iTKDFYTHPYFKTEIAKPLQIEQILDRE---VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-175 |
4.06e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGE-YCLLeAASGTGKTSLCHFLYGIREDYTGKILFDGadcrgfsaaawsGLRrrsLSMLFQDLRLFGELTVAENI 108
Cdd:COG0488 19 LSINPGDrIGLV-GRNGAGKSTLLKILAGELEPDSGEVSIPK------------GLR---IGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 --------GLKNELTHFKTQE---------------------------QIGRMLEAAGI-ADKRDVPVEKLSFGQQQRVA 152
Cdd:COG0488 83 ldgdaelrALEAELEELEAKLaepdedlerlaelqeefealggweaeaRAEEILSGLGFpEEDLDRPVSELSGGWRRRVA 162
|
170 180
....*....|....*....|...
gi 1681973554 153 FIRCMCQPFDFILLDEPVSHLDA 175
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
137-199 |
4.41e-07 |
|
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: 49.55 E-value: 4.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLleeAQAQGAGIVVT 199
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL---QEYPGTVVAVT 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
86-187 |
4.99e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 86 RRSLSMLFQDLRLFGELTVAEN--IGLK-NELTHFKTQ--EQIGRMLEAAGIADK-----RDVPvEKLSFGQQQRVAFIR 155
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNvaIGVKlNGLVKSKKEldERVEWALKKAALWDEvkdrlNDYP-SNLSGGQRQRLVIAR 162
|
90 100 110
....*....|....*....|....*....|..
gi 1681973554 156 CMCQPFDFILLDEPVSHLDAANGKLLSGMLLE 187
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFE 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
30-174 |
5.05e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.00 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIRE-----DYTGKILFDGADCrgFSAAAWSGLRRRSLSMLFQDLRLFgELTV 104
Cdd:PRK14239 26 LDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI--YSPRTDTVDLRKEIGMVFQQPNPF-PMSI 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 105 AENI--GLKNELTHFKT--QEQIGRMLEAAGIADK-RDVPVEK---LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK14239 103 YENVvyGLRLKGIKDKQvlDEAVEKSLKGASIWDEvKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-200 |
5.44e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLrrrSLSMLFQDLRLFGELTVAENI-- 108
Cdd:PRK15439 33 TLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPLLFPNLSVKENIlf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNeltHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMlLEE 188
Cdd:PRK15439 110 GLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSR-IRE 185
|
170
....*....|..
gi 1681973554 189 AQAQGAGIVVTS 200
Cdd:PRK15439 186 LLAQGVGIVFIS 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
44-174 |
7.72e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.86 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENIGLKNEltHFKTQEQI 123
Cdd:PRK11176 378 SGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL----RNQVALVSQNVHLFND-TIANNIAYART--EQYSREQI 450
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 124 ---GRMLEAAGIADKRD-----VPVEK---LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK11176 451 eeaARMAYAMDFINKMDngldtVIGENgvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-187 |
1.08e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 60 EDYT-----GKILFDGADCRGFSaaawsgLR--RRSLSMLFQDLRLFgELTVAENIGLKNELThfkTQEQIGRMLEAAGI 132
Cdd:PTZ00265 1268 EDSTvfknsGKILLDGVDICDYN------LKdlRNLFSIVSQEPMLF-NMSIYENIKFGKEDA---TREDVKRACKFAAI 1337
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1681973554 133 -------ADKRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLE 187
Cdd:PTZ00265 1338 defieslPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
31-174 |
1.42e-06 |
|
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: 48.26 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGAD------CRGFSAaawSGLRRRSLSMLFQDLRLFGELTV 104
Cdd:TIGR03269 306 EVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDewvdmtKPGPDG---RGRAKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 105 AEN----IGLknELThfktqEQIGRM-----LEAAGIADKRDVPV-----EKLSFGQQQRVAFIRCMCQPFDFILLDEPV 170
Cdd:TIGR03269 383 LDNlteaIGL--ELP-----DELARMkavitLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
....
gi 1681973554 171 SHLD 174
Cdd:TIGR03269 456 GTMD 459
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
31-174 |
1.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.39 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAaWSglRRRSLSMLFQ--DLRLFG---ELTVA 105
Cdd:PRK13633 32 EVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL-WD--IRNKAGMVFQnpDNQIVAtivEEDVA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 106 ---ENIGLKNElthfKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAF--IRCMcQPfDFILLDEPVSHLD 174
Cdd:PRK13633 109 fgpENLGIPPE----EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIagILAM-RP-ECIIFDEPTAMLD 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
44-174 |
1.64e-06 |
|
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: 47.76 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKT----SLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQD-------LRLFGElTVAENIGLKN 112
Cdd:COG4172 45 SGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRIAMIFQEpmtslnpLHTIGK-QIAEVLRLHR 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 113 ELTHFKTQEQIGRMLEAAGIADKR----DVPVEkLSFGQQQRVafircM------CQPfDFILLDEPVSHLD 174
Cdd:COG4172 124 GLSGAAARARALELLERVGIPDPErrldAYPHQ-LSGGQRQRV-----MiamalaNEP-DLLIADEPTTALD 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
28-200 |
2.03e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTFR--KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAawsglRRRSLSMLFQDLRLFGELTVA 105
Cdd:PRK13540 18 QQISFHlpAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-----YQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENIGLKnelTHFK-TQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANgkLLSGM 184
Cdd:PRK13540 93 ENCLYD---IHFSpGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS--LLTII 167
|
170
....*....|....*..
gi 1681973554 185 L-LEEAQAQGAGIVVTS 200
Cdd:PRK13540 168 TkIQEHRAKGGAVLLTS 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
44-200 |
3.33e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRRSLSMLFQD-LR--LFGELTVAENIGLKnelTHFKTQ 120
Cdd:COG3845 293 AGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---RRRLGVAYIPEDrLGrgLVPDMSVAENLILG---RYRRPP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 121 EQIGRML-------EAAGIADKRDV-------PVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLL 186
Cdd:COG3845 367 FSRGGFLdrkairaFAEELIEEFDVrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLL 446
|
170
....*....|....
gi 1681973554 187 EEAqAQGAGIVVTS 200
Cdd:COG3845 447 ELR-DAGAAVLLIS 459
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-174 |
3.50e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKI------LFDGAdcRGFSAAAwsglRRRSLSMLFQDLRLFGELTVAENI--GLKNELT 115
Cdd:PRK11144 33 SGAGKTSLINAISGLTRPQKGRIvlngrvLFDAE--KGICLPP----EKRRIGYVFQDARLFPHYKVRGNLryGMAKSMV 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 116 -HFktqEQIGRMLeaaGIAD--KRdVPVeKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK11144 107 aQF---DKIVALL---GIEPllDR-YPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-200 |
5.46e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREdYTGKILFDGADCRGFSAA------AWSGLRRRSLSML--FQDLRLFGEL 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAelarhrAYLSQQQTPPFAMpvFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 103 TVAENIGlknelthfktQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQ------PF-DFILLDEPVSHLDA 175
Cdd:PRK03695 97 KTRTEAV----------ASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinPAgQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*
gi 1681973554 176 ANGKLLSgMLLEEAQAQGAGIVVTS 200
Cdd:PRK03695 167 AQQAALD-RLLSELCQQGIAVVMSS 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
137-175 |
5.71e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 5.71e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
35-174 |
6.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 45.81 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGfSAAAWSGLRRRsLSMLFQ--DLRLFGElTVAENI--GL 110
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKK-VGLVFQypEYQLFEE-TIEKDIafGP 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 111 KN-ELTHFKTQEQIGRMLEAAGI-----ADKRdvPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13637 110 INlGLSEEEIENRVKRAMNIVGLdyedyKDKS--PFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-199 |
1.06e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.21 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKIlfdgaDCRGFSAAAWSG------LRRR-SLSMLFQDLRLFgELTVA 105
Cdd:PRK13641 31 EEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI-----TIAGYHITPETGnknlkkLRKKvSLVFQFPEAQLF-ENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENI--GLKN-ELTHFKTQEQIGRMLEAAGIADK--RDVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKL 180
Cdd:PRK13641 105 KDVefGPKNfGFSEDEAKEKALKWLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170
....*....|....*....
gi 1681973554 181 LSGMLLEEAQAQGAGIVVT 199
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVT 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-210 |
1.53e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgFSAAAWSGLRRRslsMLFQDLRlfGELTVAENIG- 109
Cdd:PRK15112 35 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRIR---MIFQDPS--TSLNPRQRISq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 -------LKNELTHFKTQEQIGRMLEAAGI-ADKRDVPVEKLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLDAANGKL 180
Cdd:PRK15112 109 ildfplrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALIlRP-KVIIADEALASLDMSMRSQ 187
|
170 180 190
....*....|....*....|....*....|
gi 1681973554 181 LSGMLLEEAQAQgaGIVVTSVGSRLGLPYH 210
Cdd:PRK15112 188 LINLMLELQEKQ--GISYIYVTQHLGMMKH 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
44-174 |
1.57e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.39 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSL--CH-----FLYGIREDytGKILFDGADCRGfSAAAWSGLRRRsLSMLFQDLRLFGElTVAENIGLKNELTH 116
Cdd:PRK14243 45 SGCGKSTIlrCFnrlndLIPGFRVE--GKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARING 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 117 FK--TQEQIGRMLEAAG----IADKRDVPVEKLSFGQQQRVAFIRCMC-QPfDFILLDEPVSHLD 174
Cdd:PRK14243 120 YKgdMDELVERSLRQAAlwdeVKDKLKQSGLSLSGGQQQRLCIARAIAvQP-EVILMDEPCSALD 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-188 |
1.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.97 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGADCRGFsaaawsGLR--RRSLSMLFQDLRLFGElTVAENIGLKNElthfKTQE 121
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF------GLTdlRRVLSIIPQSPVLFSG-TVRFNIDPFSE----HNDA 1339
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1681973554 122 QIGRMLEAAGIAD-------KRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGMLLEE 188
Cdd:PLN03232 1340 DLWEALERAHIKDvidrnpfGLDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREE 1417
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
30-174 |
1.75e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.21 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgFSAAAWSGLRRRsLSMLFQ--DLRLFGeLTVAEN 107
Cdd:PRK13632 30 FEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT---ISKENLKEIRKK-IGIIFQnpDNQFIG-ATVEDD 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 I--GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13632 105 IafGLENKkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-176 |
1.82e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsglR-RRSLSMLFQDLR---LFGELTVAENI 108
Cdd:PRK15439 287 RAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RlARGLVYLPEDRQssgLYLDAPLAWNV 362
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 109 G--LKNELTHFKTQEQIGRMLE----AAGIA-DKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK15439 363 CalTHNRRGFWIKPARENAVLEryrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-200 |
2.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.34 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQ--DLRLFGELTVA- 105
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEETVLKd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 -----ENIGLKNElthfKTQEQIGRMLEAAGIADK--RDVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDaANG 178
Cdd:PRK13643 106 vafgpQNFGIPKE----KAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD-PKA 179
|
170 180
....*....|....*....|..
gi 1681973554 179 KLLSGMLLEEAQAQGAGIVVTS 200
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVT 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-175 |
2.92e-05 |
|
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: 43.61 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGadcRGFSAAAWSGLRRRsLSMLFQDLRLFGElTVA 105
Cdd:cd03248 31 QDVSFtlHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG---KPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 106 ENI--GLknelthfkTQEQIGRMLEAA----------GIADKRDVPV-EK---LSFGQQQRVAFIRCMCQPFDFILLDEP 169
Cdd:cd03248 106 DNIayGL--------QSCSFECVKEAAqkahahsfisELASGYDTEVgEKgsqLSGGQKQRVAIARALIRNPQVLILDEA 177
|
....*.
gi 1681973554 170 VSHLDA 175
Cdd:cd03248 178 TSALDA 183
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
31-199 |
3.17e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.53 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIR----EDYTGKILFDGadcrgfSAAAWSGLRRRSLSMLFQDLRlfgeltVAE 106
Cdd:PRK10418 25 TLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDG------KPVAPCALRGRKIATIMQNPR------SAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 107 NiGLKNELTHFK-TQEQIGRM---------LEAAGIADKRDV----PVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSH 172
Cdd:PRK10418 93 N-PLHTMHTHAReTCLALGKPaddatltaaLEAVGLENAARVlklyPFE-MSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190
....*....|....*....|....*....|
gi 1681973554 173 LDA-ANGKLLSgmLLEE-AQAQGAGI-VVT 199
Cdd:PRK10418 171 LDVvAQARILD--LLESiVQKRALGMlLVT 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
101-174 |
4.00e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.52 E-value: 4.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 101 ELTVAENIGlknELTHFKTQEQIGRMLEAAGIA-DKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:COG0488 393 DKTVLDELR---DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-176 |
5.44e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.86 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 33 RKGEYCLLEAASGTGKTSLCHFLYGI---REDYTGKILFDGADCRgfSAAAWSglRRRSLSMLFQ--DLRLFGElTVAEN 107
Cdd:PRK13640 31 PRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT--AKTVWD--IREKVGIVFQnpDNQFVGA-TVGDD 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 108 I--GLKN-ELTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK13640 106 VafGLENrAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
86-176 |
7.80e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.33 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 86 RRSLSMLFQDLRLFgELTVAENIGLKNELTHFKTQEQIGRMLEAA--------GIADKRDVPVEKLSFGQQQRVAFIRCM 157
Cdd:PRK14258 87 RRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKLEIDDIVESAlkdadlwdEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
90
....*....|....*....
gi 1681973554 158 CQPFDFILLDEPVSHLDAA 176
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPI 184
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
44-175 |
9.14e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.78 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGadcRGFSAAAWSGLRRrSLSMLFQDLRLFGElTVAENIGLKNELThfktQEQI 123
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDG---RPLSSLSHSVLRQ-GVAMVQQDPVVLAD-TFLANVTLGRDIS----EEQV 446
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1681973554 124 GRMLEAAGIAD-KRDVPV----------EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:PRK10790 447 WQALETVQLAElARSLPDglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-188 |
9.78e-05 |
|
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: 41.93 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 34 KGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGElTVAENIGLKN- 112
Cdd:cd03290 26 TGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TVEENITFGSp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 113 -------------------ELTHFKTQEQIGRMleaaGIadkrdvpveKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL 173
Cdd:cd03290 105 fnkqrykavtdacslqpdiDLLPFGDQTEIGER----GI---------NLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170
....*....|....*
gi 1681973554 174 DAAngklLSGMLLEE 188
Cdd:cd03290 172 DIH----LSDHLMQE 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
31-200 |
1.05e-04 |
|
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: 41.93 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaaAWS---GLRRRSLSMLFQDLRLFGELTVAEN 107
Cdd:cd03267 43 TIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-------PWKrrkKFLRRIGVVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNE---LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGM 184
Cdd:cd03267 116 FYLLAAiydLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170
....*....|....*.
gi 1681973554 185 LLEEAQAQGAGIVVTS 200
Cdd:cd03267 196 LKEYNRERGTTVLLTS 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-168 |
1.28e-04 |
|
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: 41.36 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsGLRrrslsmlfqdlrlfGELTVAENI-- 108
Cdd:cd03220 44 EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG--GFN--------------PELTGRENIyl 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 109 -----GLKNELTHFKTQEqigrMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDE 168
Cdd:cd03220 108 ngrllGLSRKEIDEKIDE----IIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-200 |
1.40e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSA--AAWSGlrrrsLSMLFQDLRLFGELTVAEN 107
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkeALENG-----ISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 IGLKNELT------HFKTQEQIGRMLEAAGI-ADKRDvPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGKL 180
Cdd:PRK10982 94 MWLGRYPTkgmfvdQDKMYRDTKAIFDELDIdIDPRA-KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180
....*....|....*....|
gi 1681973554 181 LSgMLLEEAQAQGAGIVVTS 200
Cdd:PRK10982 173 LF-TIIRKLKERGCGIVYIS 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-215 |
1.58e-04 |
|
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: 42.24 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADcrgfsaAAWSGLR--RRSLSMLFQDLRLF-GELTV-- 104
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN------IAKIGLHdlRFKITIIPQDPVLFsGSLRMnl 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 105 -------AENIGLKNELTHFKTQeqigrmleAAGIADKRDVPV----EKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHL 173
Cdd:TIGR00957 1381 dpfsqysDEEVWWALELAHLKTF--------VSALPDKLDHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1681973554 174 DAANGKLLSGMLleeaQAQGAGIVVTSVGSRLG--LPYHKTLTL 215
Cdd:TIGR00957 1453 DLETDNLIQSTI----RTQFEDCTVLTIAHRLNtiMDYTRVIVL 1492
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-174 |
1.80e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 41.54 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRgfSAAAWSglRRRSLSMLFQ--DLRLFGElT 103
Cdd:PRK13635 24 KDVSFsvYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWD--VRRQVGMVFQnpDNQFVGA-T 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1681973554 104 VAENI--GLKNE-LTHFKTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13635 99 VQDDVafGLENIgVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-200 |
2.11e-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: 41.35 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTF--RKGEYCLLEAASGTGKTSLCHFLYGIRE-DYTGKILFDG--ADCRGFSAAAwsglrRRSLSMLFQDLRLFG--- 100
Cdd:TIGR02633 278 DVSFslRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNPAQAI-----RAGIAMVPEDRKRHGivp 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 101 ELTVAENIGLkNELTHFKTQEQIGRMLEAAGI--ADKR--------DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPV 170
Cdd:TIGR02633 353 ILGVGKNITL-SVLKSFCFKMRIDAAAELQIIgsAIQRlkvktaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190
....*....|....*....|....*....|
gi 1681973554 171 SHLDAAnGKLLSGMLLEEAQAQGAGIVVTS 200
Cdd:TIGR02633 432 RGVDVG-AKYEIYKLINQLAQEGVAIIVVS 460
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-174 |
2.56e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 2.56e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13409 448 DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-201 |
4.94e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.42 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 32 FRKGEYCLLEAASGTGKTSLCHFLYGIRE---DYTGKILFDGadcrgfSAAAWSGLRRRSlSMLFQDLRLFGELTVAENI 108
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNG------MPIDAKEMRAIS-AYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 ------GLKNELTHFKTQEQIGRMLEAAGIADKRD----VP--VEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:TIGR00955 121 mfqahlRMPRRVTKKEKRERVDEVLQALGLRKCANtrigVPgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....*....
gi 1681973554 177 NG----KLLSGMlleeaqAQGAGIVVTSV 201
Cdd:TIGR00955 201 MAysvvQVLKGL------AQKGKTIICTI 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
137-174 |
5.17e-04 |
|
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: 40.54 E-value: 5.17e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:COG1245 450 DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
30-176 |
5.62e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.77 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSglrrRSLSMLFQDLRLFGELTVAENIG 109
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTVRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 110 LKNELTHfktqEQIGRMleaaGIADKRDVP---------------VEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK10575 108 IGRYPWH----GALGRF----GAADREKVEeaislvglkplahrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
..
gi 1681973554 175 AA 176
Cdd:PRK10575 180 IA 181
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
31-174 |
6.00e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIRED---YTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQD--------LRLF 99
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmtslnpyMRVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 100 GELTvaENIGLKNELTHFKTQEQIGRMLEAAGIADKRD----VPVEkLSFGQQQRVAF-IRCMCQPfDFILLDEPVSHLD 174
Cdd:PRK09473 118 EQLM--EVLMLHKGMSKAEAFEESVRMLDAVKMPEARKrmkmYPHE-FSGGMRQRVMIaMALLCRP-KLLIADEPTTALD 193
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
31-181 |
6.07e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 40.09 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 31 TFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWsglrRRSLSMLFQDLRLFGElTVAENI-- 108
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SVRENIay 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKnelthFKTQEQIGRMLEAAGIAD-------KRDVPV-EK---LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAAN 177
Cdd:TIGR00958 578 GLT-----DTPDEEIMAAAKAANAHDfimefpnGYDTEVgEKgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
....
gi 1681973554 178 GKLL 181
Cdd:TIGR00958 653 EQLL 656
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
118-200 |
9.58e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.10 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 118 KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA-ANGKLLSgmLLEEAQAQGAGI 196
Cdd:PRK15056 118 RDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVkTEARIIS--LLRELRDEGKTM 195
|
....
gi 1681973554 197 VVTS 200
Cdd:PRK15056 196 LVST 199
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
67-200 |
9.69e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 67 LFDGADCRGFSAAAWSGLRRRSLSMLFQDLRLFGELTVAEniglKNELTHFKTQEQIGRMLEAAgiaDKRDVPVEKLSFG 146
Cdd:pfam13304 168 VLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIE----KSLLVDDRLRERGLILLENG---GGGELPAFELSDG 240
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1681973554 147 QQQ---RVAFIRCMCQPFDFILLDEPVSHLDAANGKLLSGmLLEEAQAQGAGIVVTS 200
Cdd:pfam13304 241 TKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLE-LLKELSRNGAQLILTT 296
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-176 |
1.20e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 39.45 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLrRRSLSMLFQ------DLRLFGELTVAENI 108
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAL-RRDIQFIFQdpyaslDPRQTVGDSIMEPL 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 109 GLKNELTHFKTQEQIGRMLEAAGIADKR--DVPVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:PRK10261 429 RVHGLLPGKAAAARVAWLLERVGLLPEHawRYPHE-FSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-200 |
1.38e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 38.61 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 29 EVTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQ--DLRLFgELTVAE 106
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLF-EDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 107 NI--GLKN-ELTHFKTQEQIGRMLEAAGIAdkRDV----PVEkLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:PRK13646 106 EIifGPKNfKMNLDEVKNYAHRLLMDLGFS--RDVmsqsPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180
....*....|....*....|.
gi 1681973554 180 LLSGMLLEEAQAQGAGIVVTS 200
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVS 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-176 |
1.49e-03 |
|
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: 38.40 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 35 GEYCLLEAASGTGKTSLCHFLYGIREDY---TGKILFDGADCRGFSAAAwsglrRRSLSMLFQDLRLFGELTVAENIglk 111
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-----PGEIIYVSEEDVHFPTLTVRETL--- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1681973554 112 neltHFKTQEQIGRMleaagiadkrdvpVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAA 176
Cdd:cd03233 105 ----DFALRCKGNEF-------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
103-174 |
1.68e-03 |
|
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: 38.50 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 103 TVAENIGLKNELthfKTQEQIGRMLEAAGIADKRdvpVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:cd03236 106 KVGELLKKKDER---GKLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-198 |
1.72e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 38.57 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAWSGLRRRSLSMLFQ--DLRLFGElTVAEN 107
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 108 I--GLKNELTHFKTQEQIGR-MLEAAGIADK--RDVPVEkLSFGQQQRVAF--IRCMcQPfDFILLDEPVSHLDAANGKL 180
Cdd:PRK13649 107 VafGPQNFGVSQEEAEALAReKLALVGISESlfEKNPFE-LSGGQMRRVAIagILAM-EP-KILVLDEPTAGLDPKGRKE 183
|
170
....*....|....*...
gi 1681973554 181 LSgMLLEEAQAQGAGIVV 198
Cdd:PRK13649 184 LM-TLFKKLHQSGMTIVL 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
43-174 |
1.87e-03 |
|
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: 38.65 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 43 ASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSAAAwsgLRRrSLSMLFQDLRLFGElTVAENIGLKNELThfkTQEQ 122
Cdd:COG5265 392 PSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRA-AIGIVPQDTVLFND-TIAYNIAYGRPDA---SEEE 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 123 IGRMLEAAGIAD-------KRDVPV-E---KLSFGQQQRVAFIRCmcqpfdfIL-------LDEPVSHLD 174
Cdd:COG5265 464 VEAAARAAQIHDfieslpdGYDTRVgErglKLSGGEKQRVAIART-------LLknppiliFDEATSALD 526
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
139-186 |
2.09e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 2.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1681973554 139 PVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA-ANGKLLSGMLL 186
Cdd:PLN03073 624 PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEALIQGLVL 672
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-177 |
2.24e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 30 VTFRKGEYCLLEAASGTGKTSLCHFLYGireDYTGKILFDGADCRGFSA------AAWSGLR------------RRSLSM 91
Cdd:PRK13547 22 LRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGAPRGARVTGDVTlngeplAAIDAPRlarlravlpqaaQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 92 LFQDLRLFGELTVAENIGlknELTHfKTQEQIGRMLEAAGIA--DKRDVPVekLSFGQQQRVAFIRCMCQ---------P 160
Cdd:PRK13547 99 SAREIVLLGRYPHARRAG---ALTH-RDGEIAWQALALAGATalVGRDVTT--LSGGELARVQFARVLAQlwpphdaaqP 172
|
170
....*....|....*..
gi 1681973554 161 FDFILLDEPVSHLDAAN 177
Cdd:PRK13547 173 PRYLLLDEPTAALDLAH 189
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
100-200 |
2.59e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 37.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 100 GELTVAENIGLkNELTHFKTQEQIGRMLEA----AGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDA 175
Cdd:COG1134 101 PELTGRENIYL-NGRLLGLSRKEIDEKFDEivefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
90 100
....*....|....*....|....*.
gi 1681973554 176 A-NGKllSGMLLEEAQAQGAGIVVTS 200
Cdd:COG1134 180 AfQKK--CLARIRELRESGRTVIFVS 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-174 |
2.72e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.25 E-value: 2.72e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13409 207 DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
98-174 |
4.00e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.80 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 98 LFGELTVAENIGLKNELTHF---KTQEQIGRMLEAAGIADKRDVPVEKLSFGQQQR----VAFIRcmcQPfDFILLDEPV 170
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLpaaEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslaVAVIH---KP-ELLILDEPT 425
|
....
gi 1681973554 171 SHLD 174
Cdd:NF033858 426 SGVD 429
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
137-187 |
7.52e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 36.85 E-value: 7.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 137 DVPVEKLSFGQQQRVAFIRCM-CQPfDFILLDEPVSHLDAANGKLLSGMLLE 187
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALvSNP-DVLLLDEPTNHLDIETIEWLEGFLKT 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-174 |
8.68e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 36.69 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 28 QEVTF--RKGEYCLLEAASGTGKTSLCHFLYGIREDYTGKILFDGADCRGFSA--AAWSGL-----RRRslsmlfqDLRL 98
Cdd:PRK09700 280 RDISFsvCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldAVKKGMayiteSRR-------DNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 99 FGELTVAENI---------------GLKNELTHFKTQEQIGRML--EAAGIadkrDVPVEKLSFGQQQRVAFIRCMCQPF 161
Cdd:PRK09700 353 FPNFSIAQNMaisrslkdggykgamGLFHEVDEQRTAENQRELLalKCHSV----NQNITELSGGNQQKVLISKWLCCCP 428
|
170
....*....|...
gi 1681973554 162 DFILLDEPVSHLD 174
Cdd:PRK09700 429 EVIIFDEPTRGID 441
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
143-179 |
8.83e-03 |
|
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: 36.85 E-value: 8.83e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1681973554 143 LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANGK 179
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
44-174 |
9.14e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 36.32 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 44 SGTGKTSLCHFLYGIREDYTGKILFDGadcrgfSAAAWSGLR--RRSLSMLFQ--DLRLFGElTVAE-------NIGLKN 112
Cdd:PRK13652 39 NGAGKSTLFRHFNGILKPTSGSVLIRG------EPITKENIRevRKFVGLVFQnpDDQIFSP-TVEQdiafgpiNLGLDE 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1681973554 113 ELTHFKTQEQIgRMLeaaGIADKRDVPVEKLSFGQQQRVAFIRCMCQPFDFILLDEPVSHLD 174
Cdd:PRK13652 112 ETVAHRVSSAL-HML---GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
143-187 |
9.22e-03 |
|
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: 35.91 E-value: 9.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1681973554 143 LSFGQQQRVAFIRCMCQPFDFILLDEPVSHLDAANG-----KLLSGMLLE 187
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGrhifeNCILGLLLN 177
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
90-199 |
9.82e-03 |
|
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: 35.41 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681973554 90 SMLFQDLRLFGELTVAENIGLKNELTHFKTQEQIGRMLEaagiadkrdvpVEKLSFGQQQRVA----FIRCMCQPFDFIL 165
Cdd:cd03227 36 TILDAIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFT-----------RLQLSGGEKELSAlaliLALASLKPRPLYI 104
|
90 100 110
....*....|....*....|....*....|....
gi 1681973554 166 LDEPVSHLDAANGKLLSGMLLEEAQAQGAGIVVT 199
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT 138
|
|
| |
