|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
6.58e-123 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 347.42 E-value: 6.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 ME-ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAL 79
Cdd:COG1136 1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 AVFRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDK--RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-219 |
2.03e-109 |
|
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: 313.27 E-value: 2.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFR 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLL--DKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLagVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-222 |
5.44e-90 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 264.30 E-value: 5.44e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-221 |
1.22e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 238.03 E-value: 1.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTgkSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ---TILLITHDEKIALEAN-RIVTMEDGVIVS 221
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELL----EEINRrgtTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-220 |
5.21e-79 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 236.09 E-value: 5.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIY--GSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLDTRV--LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:TIGR02211 79 KLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEakERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-220 |
2.72e-71 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 220.72 E-value: 2.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFrRRK 86
Cdd:COG1135 5 ENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA-RRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLL---DKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLEIagvPKAEIRK-RVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG1135 163 LCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmdvvRRI---CDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-222 |
7.51e-70 |
|
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: 213.21 E-value: 7.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLDK--RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEVVEE 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-222 |
3.21e-69 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 211.98 E-value: 3.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEinSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-217 |
6.47e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 209.18 E-value: 6.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLkeealavf 82
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILLPMLLDK--RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:COG1116 79 -GPDRGVVFQEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 161 AILLADEPTGNLD---RKN-SEEIVDLLnlsnKRFNQTILLITHD--EKIALeANRIVTMEDG 217
Cdd:COG1116 158 EVLLMDEPFGALDaltRERlQDELLRLW----QETGKTVLFVTHDvdEAVFL-ADRVVVLSAR 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-220 |
6.35e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.45 E-value: 6.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLDK----------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:COG3638 79 RRR-IGMIFQQFNLVPRLSVLTNVLAGRLGRTstwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-217 |
8.05e-67 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 205.17 E-value: 8.05e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREiqRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDlSLVDRVAHRVIILDDG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-214 |
8.96e-67 |
|
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: 205.01 E-value: 8.96e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeealavfR 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 162 ILLADEPTGNLD---RKNSEEivDLLNLSNKRfNQTILLITHD--EKIALeANRIVTM 214
Cdd:cd03293 152 VLLLDEPFSALDaltREQLQE--ELLDIWRET-GKTVLLVTHDidEAVFL-ADRVVVL 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
4.05e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 207.64 E-value: 4.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEala 80
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrRRKVGLIYQFYNLIPTLDVRKNILLPmlLDKRKVD----EDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:COG3842 76 ---KRNVGMVFQDYALFPHLTVAENVAFG--LRMRGVPkaeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 157 IYRPAILLADEPTGNLDRKN----SEEIVDLLnlsnKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLreemREELRRLQ----RELGITFIYVTHDQEEALAlADRIAVMNDGRIE 215
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
3-217 |
1.53e-65 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 201.87 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPmlLDKRKVDE----DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALP--LKYRGVAKkeriERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQK-GTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
1.71e-65 |
|
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: 201.97 E-value: 1.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVf 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEI-----VSILGLSDRLNHLPSQLSGGQQQRVSIARS 155
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvllllVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
2.90e-64 |
|
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: 198.51 E-value: 2.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPmlLDKRKVDED----RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFG--LKLRGVPKAeiraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-220 |
1.72e-62 |
|
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: 195.09 E-value: 1.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFR 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRkVGLIYQFYNLIPTLDVRKNILLPMLLDK----------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIA 153
Cdd:cd03256 78 RQ-IGMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-219 |
3.63e-62 |
|
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: 193.39 E-value: 3.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRrK 86
Cdd:cd03292 4 INVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-K 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLL--DKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKI-ALEANRIVTMEDGVI 219
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELvDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
5.50e-62 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 197.22 E-value: 5.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEeala 80
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfRRRKVGLIYQFYNLIPTLDVRKNILLPMLLdkRKVDED----RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:COG3839 73 --KDRNIAMVFQSYALYPHMTVYENIAFPLKL--RKVPKAeidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 157 IYRPAILLADEPTGNLDRK--NS--EEIVDLLnlsnKRFNQTILLITHD--EKIALeANRIVTMEDGVIV 220
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKlrVEmrAEIKRLH----RRLGTTTIYVTHDqvEAMTL-ADRIAVMNDGRIQ 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-222 |
1.46e-61 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 192.30 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLL--DKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-220 |
1.82e-61 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 192.13 E-value: 1.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVf 82
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILL-PMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:COG1126 76 -RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEaeERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMrDLAKE--GMTMVVVTHEMGFAREvADRVVFMDGGRIV 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-220 |
9.58e-60 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 191.17 E-value: 9.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRrK 86
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR-Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEikARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRLV 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-222 |
1.03e-58 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 184.84 E-value: 1.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYgsnQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYN--LI-PTldVRKNI---LLPMLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:COG1122 74 RRKVGLVFQNPDdqLFaPT--VEEDVafgPENLGLPREEIRE-RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-221 |
1.74e-58 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 194.94 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAglERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDGVIVS 221
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-219 |
2.81e-58 |
|
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: 183.11 E-value: 2.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfr 83
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILL-PMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEaeERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMkDLAEE--GMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
4.77e-58 |
|
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: 191.27 E-value: 4.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSN-QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAV 81
Cdd:COG1123 260 LLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRRkVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL---GLS-DRLNHLPSQLSGGQQQRVSIARS 155
Cdd:COG1123 340 LRRR-VQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLervGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-220 |
6.79e-58 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 182.53 E-value: 6.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLDK---RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:TIGR02982 81 RRR-IGYIFQAHNLLGFLTARQNVQMALELQPnlsYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-220 |
2.29e-57 |
|
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: 182.11 E-value: 2.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPMLLDK----------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-222 |
2.99e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 181.92 E-value: 2.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIsslKEEALAVFR 83
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRkVGLIYQFY--NLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDR-LNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:COG1124 79 RR-VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDlAVVAHLCDRVAVMQNGRIVEE 220
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-214 |
3.19e-57 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 180.12 E-value: 3.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRK 86
Cdd:TIGR03608 2 KNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRfSEIVSIL---GLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKKEKR-EKKKEALekvGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTM 214
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-220 |
3.55e-56 |
|
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: 178.63 E-value: 3.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRkVGLIYQFYNLIPTLDVRKNILLPmLLDKRKVDEDRFSEIV----SILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:COG1127 81 RRR-IGMLFQGGALFDSLTVFENVAFP-LREHTDLSEAEIRELVleklELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKII 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-219 |
3.62e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.70 E-value: 3.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTkiYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQfynlIPTL---DVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDR-LNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:COG4619 73 RRQVAYVPQ----EPALwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVI 219
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDpEQIERVADRVLTLEAGRL 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-217 |
8.04e-56 |
|
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: 175.84 E-value: 8.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfR 83
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPP--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPmlldkrkvdedrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDG 217
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-220 |
7.83e-55 |
|
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: 174.37 E-value: 7.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEidERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQIQ 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-222 |
1.43e-54 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 174.61 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 6 CENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRR 85
Cdd:cd03261 3 LRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 86 kVGLIYQFYNLIPTLDVRKNILLPmLLDKRKVDEDRFSEIVS----ILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03261 79 -MGMLFQSGALFDSLTVFENVAFP-LREHTRLSEEEIREIVLekleAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-217 |
1.49e-54 |
|
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: 173.81 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGSNQTrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrR 84
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLIYQFYNL-IPTLDVRKNI---LLPMLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03225 75 RKVGLVFQNPDDqFFGPTVEEEVafgLENLGLPEEEIEE-RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDG 217
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
3.73e-54 |
|
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: 173.19 E-value: 3.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03300 71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 162 ILLADEPTGNLDRKNSEEI-VDLLNLsNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMqLELKRL-QKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQ 210
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-220 |
6.35e-53 |
|
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: 174.07 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAla 80
Cdd:TIGR03265 2 SPYLSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrrRKVGLIYQFYNLIPTLDVRKNI---LLPMLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:TIGR03265 76 ----RDYGIVFQSYALFPNLTVADNIaygLKNRGMGRAEVAE-RVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 158 YRPAILLADEPTGNLDRKNSE----EIVDLlnlsNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:TIGR03265 151 TSPGLLLLDEPLSALDARVREhlrtEIRQL----QRRLGVTTIMVTHDQEEALSmADRIVVMNHGVIE 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-220 |
4.15e-52 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 169.36 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTR--------------------VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGK 63
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 64 IYVEDTEISSLKEEALAVFRRRKVGLIYQFYNLIPTLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQ 141
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQgvPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 142 LSGGQQQRVSIARSLIYRPAILLADEPTGNLD---RKNSEEivDLLNLSNKRfNQTILLITHD--EKIALeANRIVTMED 216
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMQD--ELLRLQAEL-QKTIVFITHDldEALRL-GDRIAIMKD 236
|
....
gi 497574098 217 GVIV 220
Cdd:cd03294 237 GRLV 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-227 |
4.48e-52 |
|
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: 168.28 E-value: 4.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNIL--LPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAygLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVS----EKVVKK 227
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQvgkpEEVFKK 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-220 |
1.10e-51 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 170.33 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeeALA 80
Cdd:COG1118 1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VfRRRKVGLIYQFYNLIPTLDVRKNIL--LPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:COG1118 72 P-RERRVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIE 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-221 |
2.72e-51 |
|
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: 165.55 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 32 KGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEI-SSLKEEALAVfRRRKVGLIYQFYNLIPTLDVRKNILLPM 110
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPP-QQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 111 LLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKR 190
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|..
gi 497574098 191 FNQTILLITHD-EKIALEANRIVTMEDGVIVS 221
Cdd:cd03297 181 LNIPVIFVTHDlSEAEYLADRIVVMEDGRLQY 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-220 |
6.16e-50 |
|
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: 165.23 E-value: 6.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRP---TSGKIYVEDTEISSLKEEAL 79
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 AVFRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL---GLSD---RLNHLPSQLSGGQQQRVS 151
Cdd:COG0444 81 RKIRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLervGLPDperRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVAVMYAGRIV 230
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-219 |
2.15e-49 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 161.51 E-value: 2.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealavFRRRK 86
Cdd:TIGR00968 4 ANISKRFGSFQ----ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILL-------PMLLDKRKVDEdrFSEIVSILGLSDRLnhlPSQLSGGQQQRVSIARSLIYR 159
Cdd:TIGR00968 74 IGFVFQHYALFKHLTVRDNIAFgleirkhPKAKIKARVEE--LLELVQLEGLGDRY---PNQLSGGQRQRVALARALAVE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:TIGR00968 149 PQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEvADRIVVMSNGKI 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-220 |
2.42e-49 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 162.24 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQT-RVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRrKVGLIYQF--YNLIPTlDVRKNI---LLPMLLDKRKVDEdRFSEIVSILGLSDR-LNHLPSQLSGGQQQRVSIARSL 156
Cdd:TIGR04521 81 RK-KVGLVFQFpeHQLFEE-TVYKDIafgPKNLGLSEEEAEE-RVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 157 IYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
2.92e-49 |
|
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: 160.97 E-value: 2.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeeala 80
Cdd:cd03296 1 MSI-EVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vFRRRKVGLIYQFYNLIPTLDVRKNILL-----------PMLLDKRKVDEdrFSEIVSILGLSDRLnhlPSQLSGGQQQR 149
Cdd:cd03296 71 -VQERNVGFVFQHYALFRHMTVFDNVAFglrvkprserpPEAEIRAKVHE--LLKLVQLDWLADRY---PAQLSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
1.38e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNI-----LLPMlldKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:COG1131 72 RRRIGYVPQEPALYPDLTVRENLrffarLYGL---PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELL-RELAAEGKTVLLSTHYleeaERL---CDRVAIIDKGRIV 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-220 |
2.28e-48 |
|
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: 159.00 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNI-LLPMLLD-KRKVDEDRFSEIVSILGLSDR--LNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:cd03295 74 RRKIGYVIQQIGLFPHMTVEENIaLVPKLLKwPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 160 PAILLADEPTGNLD---RKN-SEEIVDLlnlsNKRFNQTILLITHD--EKIALeANRIVTMEDGVIV 220
Cdd:cd03295 154 PPLLLMDEPFGALDpitRDQlQEEFKRL----QQELGKTIVFVTHDidEAFRL-ADRIAIMKNGEIV 215
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-220 |
2.11e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 158.33 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:COG1125 5 ENVTKRYPDGTV---AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL----RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNI-LLPMLL--DKRKVDEdRFSEIVSILGL--SDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIaTVPRLLgwDKERIRA-RVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 162 ILLADEPTGNLDRKNSEEIVD-LLNLsNKRFNQTILLITHD--EKIALeANRIVTMEDGVIV 220
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDeLLRL-QRELGKTIVFVTHDidEALKL-GDRIAVMREGRIV 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-220 |
5.65e-47 |
|
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: 163.01 E-value: 5.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:COG4988 337 IELEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFynliPTL---DVRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQR 149
Cdd:COG4988 410 RRQIAWVPQN----PYLfagTIRENLRLG----RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVD-LLNLSNKRfnqTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQaLRRLAKGR---TVILITHRLALLAQADRILVLDDGRIV 550
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
1.88e-46 |
|
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: 153.75 E-value: 1.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKR------------KVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVS 151
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTGsglllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-222 |
3.63e-46 |
|
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: 153.66 E-value: 3.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvf 82
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrRKVGLIYQFYNLIPTLDVRKNILL------PMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 157 IYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQ 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
7.82e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.91 E-value: 7.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 ME-ILKCENLTKIYGSNqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPT---SGKIYVEDTEISSLKE 76
Cdd:COG1123 1 MTpLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EalavFRRRKVGLIYQ--FYNLIPtLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:COG1123 79 A----LRGRRIGMVFQdpMTQLNP-VTVGDQIAEALENLGLSRAEarARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
9.61e-46 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 151.83 E-value: 9.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGsnQTRVTAlnnvNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:COG3840 2 LRLDDLTYRYG--DFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPmLLDKRKVDEDRFSEIVSIL---GLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIGLG-LRPGLKLTAEQRAQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpEDAARIADRVLLVADGRIA 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-222 |
1.71e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.20 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDteISSLKEEAL-AVf 82
Cdd:TIGR04520 1 IEVENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLwEI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQfyN----LIPTL---DVR---KNILLPMLLDKRKVDEdrfseIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:TIGR04520 76 -RKKVGMVFQ--NpdnqFVGATvedDVAfglENLGVPREEMRKRVDE-----ALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-222 |
3.30e-45 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 150.96 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:COG0411 2 DPLLEVRGLTKRFGG----LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrRRKVGLIYQFYNLIPTLDVRKNILLPML-------------LDKRKVDEDRFS----EIVSILGLSDRLNHLPSQLS 143
Cdd:COG0411 78 ---RLGIARTFQNPRLFPELTVLENVLVAAHarlgrgllaallrLPRARREEREAReraeELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 144 GGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-217 |
3.97e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 150.02 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIY-GSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAv 81
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQ----ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:PRK10908 76 FLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNkRFNQTILLITHDEK-IALEANRIVTMEDG 217
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGlISRRSYRMLTLSDG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
1.56e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 149.63 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFrrrkvgliyQFYNLIPTLDVRKNILLPMLLdkRKVD----EDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:COG4525 81 VF---------QKDALLPWLNVLDNVAFGLRL--RGVPkaerRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 157 IYRPAILLADEPTGNLD---RKNSEEIvdLLNLSnKRFNQTILLITHD-EKIALEANRIVTM 214
Cdd:COG4525 150 AADPRFLLMDEPFGALDaltREQMQEL--LLDVW-QRTGKGVFLITHSvEEALFLATRLVVM 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-217 |
1.65e-44 |
|
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: 146.76 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTlDVRKNIllpmlldkrkvdedrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03228 75 RKNIAYVPQDPFLFSG-TIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 164 LADEPTGNLDRKNSEEIVD-LLNLSNKRfnqTILLITHDEKIALEANRIVTMEDG 217
Cdd:cd03228 119 ILDEATSALDPETEALILEaLRALAKGK---TVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-220 |
1.69e-44 |
|
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: 157.69 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQ----FYNliptlDVRKNIllpmLLDKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQ 148
Cdd:COG2274 548 RRQIGVVLQdvflFSG-----TIRENI----TLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDllNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILE--NLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-220 |
2.11e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 148.62 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIS---SLKEE 77
Cdd:COG4161 1 MSI-QLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 ALAVFRRrKVGLIYQFYNLIPTLDVRKNIL-LPMLLDK--RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIAR 154
Cdd:COG4161 76 AIRLLRQ-KVGMVFQQYNLWPHLTVMENLIeAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLN-LSNKRFNQTIllITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIReLSQTGITQVI--VTHEVEFARKvASQVVYMEKGRII 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
1.17e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEI---SSLKEE 77
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 ALAVFRRrKVGLIYQFYNLIPTLDVRKN-ILLPML---LDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIA 153
Cdd:PRK11124 76 AIRELRR-NVGMVFQQYNLWPHLTVQQNlIEAPCRvlgLSKDQALA-RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLLN-LSNKRFNQTIllITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIReLAETGITQVI--VTHEVEVARKtASRVVYMENGHIV 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
1.89e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 146.75 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 rrkVGLIYQFYNLIPTLDVRKNILLPMLLDKRkvdeDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:PRK11247 83 ---TRLMFQDARLLPWKKVIDNVGLGLKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD--EKIALeANRIVTMEDGVI 219
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDvsEAVAM-ADRVLLIEEGKI 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-220 |
2.08e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 149.99 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEealavf 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 161 AILLADEPTGNLDRKNSE----EIVDLLnlsnKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDrmqlEVVDIL----ERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFV 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-217 |
3.03e-43 |
|
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: 145.27 E-value: 3.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTK---IYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVED----TEISSL 74
Cdd:COG4778 3 TLLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 75 KE-EALAVfRRRKVGLIYQFYNLIP---TLDVRKNILLPMLLDkRKVDEDRFSEIVSILGLSDRLNHL-PSQLSGGQQQR 149
Cdd:COG4778 83 SPrEILAL-RRRTIGYVSQFLRVIPrvsALDVVAEPLLERGVD-REEARARARELLARLNLPERLWDLpPATFSGGEQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNlSNKRFNQTILLITHDEKI--ALeANRIVTMEDG 217
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE-EAKARGTAIIGIFHDEEVreAV-ADRVVDVTPF 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-220 |
7.86e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 144.25 E-value: 7.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGG-----VDRPTSGKIYVEDTEISSLKEEALAV 81
Cdd:cd03260 4 RDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frRRKVGLIYQFYNLIPtLDVRKNILLP---MLLDKRKVDEDRFSEIVSILGL----SDRLNhlPSQLSGGQQQRVSIAR 154
Cdd:cd03260 80 --RRRVGMVFQKPNPFP-GSIYDNVAYGlrlHGIKLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ--TILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELI----AELKKeyTIVIVTHNmQQAARVADRTAFLLNGRLV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
8.00e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.46 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeeala 80
Cdd:COG1121 4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfRRRKVGLIYQFYNLIPT-----LDV-------RKNILLPMlldkRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQ 148
Cdd:COG1121 73 --ARRRIGYVPQRAEVDWDfpitvRDVvlmgrygRRGLFRRP----SRADREAVDEALERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDGVI 219
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLV 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-219 |
1.02e-42 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 142.15 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNIllpmlldkrkvdedrfseivsilglsdrlnhlpsQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-222 |
1.29e-42 |
|
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: 142.19 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfrr 84
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLiyqfynliptldvrknilLPMLLDKrkvdedrfseiVSILGLSDRLNhlpSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:cd03214 73 RKIAY------------------VPQALEL-----------LGLAHLADRPF---NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQ 179
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-220 |
4.19e-42 |
|
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: 149.92 E-value: 4.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQ----FYNliptlDVRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQ 148
Cdd:COG4987 408 RRRIAVVPQrphlFDT-----TLRENLRLA----RPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERR 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIV-DLLNLSNkrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLaDLLEALA---GRTVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
6.79e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.92 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQ-TRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlav 81
Cdd:COG1101 1 MLELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 fRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKR--------KVDEDRFSEIVSIL--GLSDRLNHLPSQLSGGQQQR 149
Cdd:COG1101 78 -RAKYIGRVFQdpMMGTAPSMTIEENLALAYRRGKRrglrrgltKKRRELFRELLATLglGLENRLDTKVGLLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIvdlLNLSNK---RFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALV---LELTEKiveENNLTTLMVTHNMEQALDyGNRLIMMHEGRII 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-219 |
9.31e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 145.48 E-value: 9.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavf 82
Cdd:PRK09452 14 LVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEitPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTmSDRIVVMRDGRI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-216 |
1.21e-41 |
|
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: 140.31 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:COG4133 3 LEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLN--LSNKRfnqTILLITHDEkIALEANRIVTMED 216
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAahLARGG---AVLLTTHQP-LELAAARVLDLGD 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-169 |
2.06e-41 |
|
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: 138.16 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNLIPTLDV 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 103 RKNILLPMLLD--KRKVDEDRFSEIVSILGLSD----RLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPT 169
Cdd:pfam00005 77 RENLRLGLLLKglSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
3.06e-41 |
|
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: 139.88 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:cd03224 1 LEVENLNAGYGKSQ----ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL-GLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVLERGRVVLE 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-219 |
8.17e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 142.53 E-value: 8.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEealavfRRRK 86
Cdd:PRK10851 6 ANIKKSFG----RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNI-----LLP------MLLDKRKVDedRFSEIVSILGLSDRLnhlPSQLSGGQQQRVSIARS 155
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIafgltVLPrrerpnAAAIKAKVT--QLLEMVQLAHLADRY---PAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-220 |
9.01e-41 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 139.22 E-value: 9.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILL--PMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-217 |
2.10e-40 |
|
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: 141.39 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 25 NVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisSLKEEALAVFR---RRKVGLIYQFYNLIPTLD 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSARGIFLpphRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIV 181
Cdd:COG4148 94 VRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 497574098 182 DLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSlDEVARLADHVVLLEQG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-220 |
2.32e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.41 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIY--GSNQTRVtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlKEEA 78
Cdd:PRK13637 1 MSI-KIENLTHIYmeGTPFEKK-ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 79 LAvFRRRKVGLIYQF--YNLIPTlDVRKNILL-PMLLDKRKVD-EDRFSEIVSILGLS--DRLNHLPSQLSGGQQQRVSI 152
Cdd:PRK13637 78 LS-DIRKKVGLVFQYpeYQLFEE-TIEKDIAFgPINLGLSEEEiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCE 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-225 |
3.98e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 138.28 E-value: 3.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGS-----NQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK 75
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVFRRrKVGLIYQ--FYNLIPTLDVRKNILLPM--LLDKRKVD-EDRFSEIVSILGLSDR-LNHLPSQLSGGQQQR 149
Cdd:PRK10419 81 RAQRKAFRR-DIQMVFQdsISAVNPRKTVREIIREPLrhLLSLDKAErLARASEMLRAVDLDDSvLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSEKVV 225
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVETQPV 236
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-220 |
4.93e-40 |
|
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: 139.94 E-value: 4.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 38 IVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfrRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKV 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 118 DE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTI 195
Cdd:TIGR01187 75 AEikPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|....*.
gi 497574098 196 LLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:TIGR01187 155 VFVTHDQEEAMTmSDRIAIMRKGKIA 180
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-217 |
7.69e-40 |
|
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: 136.44 E-value: 7.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFrrrkvgliyQFYNLIPTLDV 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF---------QNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMLLDKRKVDEDRFSEIV----SILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSE 178
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIVeehiALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497574098 179 EIVD-LLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR01184 152 NLQEeLMQIWEEH-RVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-227 |
1.01e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.91 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSN--QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDteISSLKEEAL 79
Cdd:PRK13633 3 EMIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 AVFRRrKVGLIYQFYN--LIPTL---DVR---KNILLPMLLDKRKVDEDrfseiVSILGLSDRLNHLPSQLSGGQQQRVS 151
Cdd:PRK13633 81 WDIRN-KAGMVFQNPDnqIVATIveeDVAfgpENLGIPPEEIRERVDES-----LKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSEKVVKK 227
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
1.40e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 136.42 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK----E 76
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVFRRRKVGLIYQFYNLIPTLDVRKNILL-PMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIA 153
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLL-NLSNKRfnQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIrQLAQEK--RTMVIVTHEMSFARDvADRAIFMDQGRIVEQ 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-220 |
2.02e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 138.70 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYV--EDTEISSLKEealavfrrR 85
Cdd:PRK11432 11 NITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgEDVTHRSIQQ--------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 86 KVGLIYQFYNLIPTLDVRKNIL--LPML---LDKRKVDEDRFSEIVSILGLSDRLnhlPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGygLKMLgvpKEERKQRVKEALELVDLAGFEDRY---VDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 161 AILLADEPTGNLD----RKNSEEIVDLlnlsNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK11432 156 KVLLFDEPLSNLDanlrRSMREKIREL----QQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIM 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-219 |
3.61e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 135.22 E-value: 3.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfrRRKV 87
Cdd:PRK09493 6 NVSKHFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI--RQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTLDVRKNILL-PMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVRgaSKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 165 ADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMqDLAEE--GMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
5.25e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 135.91 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSNQTRvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEissLKEEAlaV 81
Cdd:PRK13635 4 EIIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEET--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FR-RRKVGLIYQ-----FYNLIPTLDVR---KNILLPMLLDKRKVDEdrfseIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:PRK13635 77 WDvRRQVGMVFQnpdnqFVGATVQDDVAfglENIGVPREEMVERVDQ-----ALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-217 |
5.40e-39 |
|
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: 131.98 E-value: 5.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrR 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLIyqfynliptldvrknillpmlldkrkvdedrfseivsilglsdrlnhlpSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:cd00267 73 RRIGYV-------------------------------------------------PQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEA-NRIVTMEDG 217
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-221 |
2.45e-38 |
|
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: 132.27 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeealavfRR 84
Cdd:cd03235 1 EVEDLTVSYG----GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLIYQFYNLIPT--LDVRKNILLPMLLDK------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:cd03235 68 KRIGYVPQRRSIDRDfpISVRDVVLMGLYGHKglfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 157 IYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVS 221
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEyFDRVLLLNRTVVAS 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
5.39e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 133.61 E-value: 5.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQF--YNLIPT 99
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQFpeHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 lDVRKNILL-PMLLDKRKVD-EDRFSEIVSILGLS-DRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKN 176
Cdd:PRK13634 102 -TVEKDICFgPMNFGVSEEDaKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497574098 177 SEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVF 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-225 |
1.03e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 132.24 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSN-----QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEE 77
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 ALAVFRRrKVGLIYQ--FYNLIPTLDVRKNILLPM--LLDKRKVD-EDRFSEIVSILGL-SDRLNHLPSQLSGGQQQRVS 151
Cdd:TIGR02769 82 QRRAFRR-DVQLVFQdsPSAVNPRMTVRQIIGEPLrhLTSLDESEqKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSEKVV 225
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-217 |
3.14e-37 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 129.55 E-value: 3.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:cd03263 1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLdKRKVDEDRFSEIV---SILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRFYARL-KGLPKSEIKEEVElllRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSnkRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSmDEAEALCDRIAIMSDG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-222 |
3.24e-37 |
|
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: 129.41 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeEALAVfrRRK 86
Cdd:cd03265 4 ENLVKKYGDF----EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EPREV--RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYgvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITH--DEKIALeANRIVTMEDGVIVSE 222
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHymEEAEQL-CDRVAIIDHGRIIAE 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-220 |
5.68e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 135.20 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTL-LHLLGGVdrPTSGKIYVEDTEISSLKEEALAVFRRRkVGLIYQ--FYN 95
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQdpFGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 96 LIPTLDVRKNILLPMLLDKRKVD-EDRFSEIVSIL---GLS-DRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:COG4172 375 LSPRMTVGQIIAEGLRVHGPGLSaAERRARVAEALeevGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKI--ALeANRIVTMEDGVIV 220
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvrAL-AHRVMVMKDGKVV 505
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-217 |
8.13e-37 |
|
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: 132.16 E-value: 8.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 26 VNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQFYNLIPTLDVRKN 105
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 106 ILLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN 185
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190
....*....|....*....|....*....|...
gi 497574098 186 LSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSlQEVLRLADRVVVLEDG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
9.74e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 134.81 E-value: 9.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKS----TLLHLLGGVDRPTSGKIYVEDTEISSLKE 76
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVFRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL---GLSD---RLNHLPSQLSGGQQQ 148
Cdd:COG4172 84 RELRRIRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLervGIPDperRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRF---ADRVAVMRQGEIV 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-220 |
1.14e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 128.09 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealAVFRRRKVGLIYQ----FYNLI 97
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD----PADLRRNIGYVPQdvtlFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 ptldvRKNILLPMLLdkrkVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:cd03245 95 -----RDNITLGAPL----ADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497574098 167 EPTGNLDRKNSEEIVDllNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03245 166 EPTSAMDMNSEERLKE--RLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-220 |
2.23e-36 |
|
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: 127.22 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 28 LSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfrRRKVGLIYQFYNLIPTLDVRKNIL 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA------DRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 108 LPML--LDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN 185
Cdd:cd03298 93 LGLSpgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 497574098 186 LSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:cd03298 173 DLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-219 |
7.57e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 129.76 E-value: 7.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfrRRKV 87
Cdd:PRK11000 8 NVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTLDVRKNILLPMLL---DKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLagaKKEEINQ-RVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 165 ADEPTGNLD---RKNSE-EIVDLlnlsNKRFNQTILLITHDEKIALE-ANRIVTMEDGVI 219
Cdd:PRK11000 157 LDEPLSNLDaalRVQMRiEISRL----HKRLGRTMIYVTHDQVEAMTlADKIVVLDAGRV 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-219 |
1.05e-35 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 125.36 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 27 NLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfrRRKVGLIYQFYNLIPTLDVRKNI 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY------QRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 107 LLPML--LDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLL 184
Cdd:TIGR01277 92 GLGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 497574098 185 NLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVI 219
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKI 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
1.13e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.45 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISsLKEEALAVFR 83
Cdd:COG4598 9 LEVRDLHKSFGDLEV----LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIR-LKPDRDGELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 ----------RRKVGLIYQFYNLIPTLDVRKNILL-PMLLDKRKVDE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQRV 150
Cdd:COG4598 84 padrrqlqriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEaiERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 151 SIARSLIYRPAILLADEPTGNLD-----------RKNSEEivdllnlsnkrfNQTILLITHDEKIALE-ANRIVTMEDGV 218
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDpelvgevlkvmRDLAEE------------GRTMLVVTHEMGFARDvSSHVVFLHQGR 231
|
.
gi 497574098 219 I 219
Cdd:COG4598 232 I 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-220 |
1.46e-35 |
|
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: 125.48 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:COG0410 1 MPMLEVENLHAGYG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrRRKVGLIYQFYNLIPTLDVRKNILLPMLL--DKRKVDED------RFSEivsilgLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:COG0410 77 ---RLGIGYVPEGRRIFPSLTVEENLLLGAYArrDRAEVRADlervyeLFPR------LKERRRQRAGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ---TILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGLAPLIVEEIFEII----RRLNRegvTILLVEQNARFALEiADRAYVLERGRIV 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-220 |
3.13e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIY-------GSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK 75
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVFRRRkVGLIYQ--FYNLIPTLDVRKNILLPM----LLDKRKVDEdRFSEIVSILGLS-DRLNHLPSQLSGGQQQ 148
Cdd:COG4608 87 GRELRPLRRR-MQMVFQdpYASLNPRMTVGDIIAEPLrihgLASKAERRE-RVAELLELVGLRpEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDlsvvRHI---SDRVAVMYLGKIV 237
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
1.11e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.60 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK-EEAlav 81
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 fRRRKVGLIYQFYNLIPTLDVRKNILL------PMLLDKRKVdEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARS 155
Cdd:COG1129 77 -QAAGIAIIHQELNLVPNLSVAENIFLgreprrGGLIDWRAM-RRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSE---EIVDLLnlsnKRFNQTILLITH--DEKIALeANRIVTMEDGVIVSEKVVK 226
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVErlfRIIRRL----KAQGVAIIYISHrlDEVFEI-ADRVTVLRDGRLVGTGPVA 225
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-227 |
1.47e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 129.99 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 6 CENLTKIYGSNQTrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRR 85
Cdd:TIGR03375 466 FRNVSFAYPGQET--PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL----RR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 86 KVGLIYQ----FYNliptlDVRKNILLpmllDKRKVDEDRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRV 150
Cdd:TIGR03375 540 NIGYVPQdprlFYG-----TLRDNIAL----GAPYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAV 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnlsnKRF--NQTILLITHdeKIAL--EANRIVTMEDGVIVS----E 222
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRL----KRWlaGKTLVLVTH--RTSLldLVDRIIVMDNGRIVAdgpkD 684
|
....*
gi 497574098 223 KVVKK 227
Cdd:TIGR03375 685 QVLEA 689
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-214 |
2.97e-34 |
|
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: 127.79 E-value: 2.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslkeEALAVFRRRK 86
Cdd:TIGR02857 325 SGVSVAYPG---RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA----DADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQfynlIPTL---DVRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSI 152
Cdd:TIGR02857 398 IAWVPQ----HPFLfagTIAENIRLA----RPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVD-LLNLSNkrfNQTILLITHDEKIALEANRIVTM 214
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEaLRALAQ---GRTVLLVTHRLALAALADRIVVL 529
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-216 |
3.38e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.43 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRP---TSGKIYVEDTEISSLKEEala 80
Cdd:COG4136 2 LSLENLTITLGG----RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrRRKVGLIYQFYNLIPTLDVRKNIL--LPMLLdKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY 158
Cdd:COG4136 75 ---QRRIGILFQDDLLFPHLSVGENLAfaLPPTI-GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 159 RPAILLADEPTGNLD---RKNSEEIVdllnlsnkrFNQTI------LLITHDEKIALEANRIVTMED 216
Cdd:COG4136 151 EPRALLLDEPFSKLDaalRAQFREFV---------FEQIRqrgipaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-219 |
3.42e-34 |
|
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: 120.40 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTlDVRKNIllpmlldkrkvdedrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
3-222 |
5.03e-34 |
|
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: 122.02 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLH-------LLGGVDrpTSGKIYVEDTEISSLK 75
Cdd:TIGR00972 1 AIEIENLNLFYGEKE----ALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVR--IEGKVLFDGQDIYDKK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVfrRRKVGLIYQFYNLIPtLDVRKNILLPMLLDKRKvDEDRFSEIV--SILG------LSDRLNHLPSQLSGGQQ 147
Cdd:TIGR00972 75 IDVVEL--RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIK-DKKELDEIVeeSLKKaalwdeVKDRLHDSALGLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 148 QRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFnqTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARiSDRTAFFYDGELVEY 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-220 |
6.84e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.20 E-value: 6.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQ----Fynli 97
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQdtflF---- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 pTLDVRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:COG1132 427 -SGTIRENIRYG----RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497574098 167 EPTGNLDRKNSEEIVDllNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG1132 502 EATSALDTETEALIQE--ALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-200 |
8.17e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.68 E-value: 8.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLL------H-LLGGVDrpTSGKIYVEDTEISSLK 75
Cdd:COG1117 11 KIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmNdLIPGAR--VEGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVfrRRKVGLIYQFYNLIPTlDVRKNILLPM----LLDKRKVDEdrfseIV--SILG------LSDRLNHLPSQLS 143
Cdd:COG1117 85 VDVVEL--RRRVGMVFQKPNPFPK-SIYDNVAYGLrlhgIKSKSELDE-----IVeeSLRKaalwdeVKDRLKKSALGLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 144 GGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN-LSNKRfnqTILLITH 200
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILeLKKDY---TIVIVTH 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-220 |
1.11e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.84 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVTalnnvnLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDteisslKEEALAVFR 83
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFD------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILL---PMLldkrKVDED---RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:PRK10771 70 RRPVSMLFQENNLFSHLTVAQNIGLglnPGL----KLNAAqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-220 |
2.25e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.87 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGSNQTrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrR 84
Cdd:PRK13632 9 KVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLIYQFY-NLIPTLDVRKNILLPmlLDKRKVDEDRFSEIVSIL----GLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:PRK13632 83 KKIGIIFQNPdNQFIGATVEDDIAFG--LENKKVPPKKMKDIIDDLakkvGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 160 PAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-222 |
4.35e-33 |
|
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: 119.25 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNLIPTlD 101
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNIllpmLLDKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:cd03254 93 IMENI----RLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497574098 171 NLDRKnSEEIV--DLLNLSNKRfnqTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:cd03254 169 NIDTE-TEKLIqeALEKLMKGR---TSIIIAHRLSTIKNADKILVLDDGKIIEE 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-220 |
1.42e-32 |
|
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: 117.29 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVsIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfr 83
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVR---------KNIllpmllDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIAR 154
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVRefldyiawlKGI------PSKEVKA-RVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 155 SLIYRPAILLADEPTGNLDrknSEEIVDLLN-LSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLD---PEERIRFRNlLSELGEDRIVILSTHIvEDVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-222 |
1.49e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 1.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQ-----FYNL 96
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQnpdnqFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTLDVR---KNILLPMLLDKRKVdedrfSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK13648 100 IVKYDVAfglENHAVPYDEMHRRV-----SEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 174 RKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
5.54e-32 |
|
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: 115.43 E-value: 5.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealavfRRRK 86
Cdd:cd03226 3 ENISFSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLI-----YQFYnlipTLDVRKNILLPM-LLDKrkvDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03226 73 IGYVmqdvdYQLF----TDSVREELLLGLkELDA---GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLN-LSNKrfNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIReLAAQ--GKAVIVITHDyEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-220 |
5.89e-32 |
|
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: 116.48 E-value: 5.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNLIPT 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 lDVRKNILLPmlLDKRKVDED----RFSEIVS-ILGLSDRLNHL----PSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:cd03249 92 -TIAENIRYG--KPDATDEEVeeaaKKANIHDfIMSLPDGYDTLvgerGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 171 NLDRKnSEEIVDlLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03249 169 ALDAE-SEKLVQ-EALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVV 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-201 |
8.42e-32 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 118.29 E-value: 8.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKS----TLLHLLGGVDRpTSGKIYVEDTEISSLKE 76
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVFRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGL------SDRLNHLPSQLSGGQQQ 148
Cdd:PRK09473 89 KELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAvkmpeaRKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-220 |
1.42e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.11 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGSN-QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKI--------------- 64
Cdd:PRK13651 1 MQI-KVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 65 ---YVEDTEISSLKEEALAVFR--RRKVGLIYQF--YNLIPTlDVRKNIL---LPMLLDKRKVDEdRFSEIVSILGLS-D 133
Cdd:PRK13651 80 kekVLEKLVIQKTRFKKIKKIKeiRRRVGVVFQFaeYQLFEQ-TIEKDIIfgpVSMGVSKEEAKK-RAAKYIELVGLDeS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 134 RLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIV 212
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEwTKRTI 236
|
....*...
gi 497574098 213 TMEDGVIV 220
Cdd:PRK13651 237 FFKDGKII 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
1.47e-31 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 118.02 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEeala 80
Cdd:PRK11650 1 MAGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfRRRKVGLIYQFYNLIPTLDVRKNilLPMLLDKRKVDED----RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:PRK11650 74 --ADRDIAMVFQNYALYPHMSVREN--MAYGLKIRGMPKAeieeRVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 157 IYRPAILLADEPTGNLDRK----NSEEIVDLlnlsNKRFNQTILLITHD--EKIALeANRIVTMEDGVI 219
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKlrvqMRLEIQRL----HRRLKTTSLYVTHDqvEAMTL-ADRVVVMNGGVA 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-214 |
2.07e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 114.81 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQfynlIPTL-- 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQ----TPTLfg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 -DVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDR-LNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSE 178
Cdd:PRK10247 95 dTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 497574098 179 EIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTM 214
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-226 |
2.07e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.95 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfrRRKVGLIYQFYN---LIP 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV--RKTVGIVFQNPDdqlFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TldVRKNIL---LPMLLDKRKVdEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRK 175
Cdd:PRK13639 95 T--VEEDVAfgpLNLGLSKEEV-EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497574098 176 NSEEIVDLLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDGVIVSEKVVK 226
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-222 |
2.30e-31 |
|
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: 112.52 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSL-KEEAlavf 82
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYqfynliptldvrknillpmlldkrkvdedrfseivsilglsdrlnhlpsQLSGGQQQRVSIARSLIYRPAI 162
Cdd:cd03216 73 RRAGIAMVY-------------------------------------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ---TILLITH--DEKIALeANRIVTMEDGVIVSE 222
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVI----RRLRAqgvAVIFISHrlDEVFEI-ADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
2.80e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.60 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEissLKEEALA 80
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFRRrKVGLIYQ-----FYNLIPTLDVR---KNILLPMLLDKRKVDEdrfseIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:PRK13650 78 DIRH-KIGMVFQnpdnqFVGATVEDDVAfglENKGIPHEEMKERVNE-----ALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALeANRIVTMEDGVIVS 221
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDlDEVAL-SDRVLVMKNGQVES 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-220 |
4.18e-31 |
|
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: 114.12 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQfYNLIPTLD 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVLQ-ENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:cd03252 92 IRDNIALA----DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 171 NLDRKnSEEIVdLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03252 168 ALDYE-SEHAI-MRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
4.36e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.10 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSNQT-RVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:PRK13631 20 IILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFR------------RRKVGLIYQF--YNLIPTlDVRKNILL-PMLLDKRKVDEDRFSEI-VSILGL-SDRLNHLPSQLS 143
Cdd:PRK13631 100 ITNpyskkiknfkelRRRVSMVFQFpeYQLFKD-TIEKDIMFgPVALGVKKSEAKKLAKFyLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 144 GGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
6.48e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslKEEALA 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VfrRRKVGLIYQFYN-LIPTLDVRKNIL---LPMLLDKRKVdEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL 156
Cdd:PRK13652 76 V--RKFVGLVFQNPDdQIFSPTVEQDIAfgpINLGLDEETV-AHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 157 IYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSEKVVKK 227
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-222 |
7.55e-31 |
|
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: 112.85 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavf 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNlSNKRFNQTILLITH--DEKIALeANRIVTMEDGVIVSE 222
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTHimQEVERL-CDRVVVLHRGRVVYE 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-222 |
1.17e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 112.62 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLL---DKRKVDEDRFsEIVSILglSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAAlprRSRKIPDEIY-ELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVAS 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-222 |
1.19e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 115.22 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKS-TLLHLLGGVDRPtsGKIYVEDTEISSLKEEAL 79
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 AVFRRRK-----VGLIYQ--FYNLIPTLDVRKNILLPMLLDK---RKVDEDRFSEIVSILGLSD---RLNHLPSQLSGGQ 146
Cdd:PRK11022 79 SEKERRNlvgaeVAMIFQdpMTSLNPCYTVGFQIMEAIKVHQggnKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 147 QQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVET 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
1.99e-30 |
|
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: 117.21 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGS-NQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVE--DTEISSLKEEA 78
Cdd:TIGR03269 278 PIIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 79 LAVFR-RRKVGLIYQFYNLIPTLDVRKNIL------LPMLLDKRKV---------DEDRFSEIvsilglsdrLNHLPSQL 142
Cdd:TIGR03269 358 DGRGRaKRYIGILHQEYDLYPHRTVLDNLTeaigleLPDELARMKAvitlkmvgfDEEKAEEI---------LDKYPDEL 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 143 SGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-227 |
5.26e-30 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 111.31 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 25 NVNLSVQKGDFVSIVGASGSGKST----LLHLLGGVDRPTSGKIYVEDTEISSLKeealavFRRRKVGLIYQ----FYNL 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQnprtAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTLdvrKNILLPMLLDKRKVDEDRFSEIVSIL---GLSDR---LNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:TIGR02770 78 LFTM---GNHAIETLRSLGKLSKQARALILEALeavGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRFNQTILLITHDEK-IALEANRIVTMEDGVIVSEKVVKK 227
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGvVARIADEVAVMDDGRIVERGTVKE 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
5.87e-30 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 111.33 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGK-IYV--EDTEISSLKEe 77
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgERRGGEDVWE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 aLavfrRRKVGLI-----YQFYNLIPTLDVrknIL--------LPMLLDKRkvDEDRFSEIVSILGLSDRLNHLPSQLSG 144
Cdd:COG1119 76 -L----RKRIGLVspalqLRFPRDETVLDV---VLsgffdsigLYREPTDE--QRERARELLELLGLAHLADRPFGTLSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 145 GQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRVV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-217 |
5.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.62 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEIlKCENLTKIYGSNQTRVT-ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIS------S 73
Cdd:PRK13641 1 MSI-KFENVDYIYSPGTPMEKkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 74 LKEealavfRRRKVGLIYQFynliPTLDVRKNILLPMLLDKRK---VDEDRFSEI----VSILGLSDRL-NHLPSQLSGG 145
Cdd:PRK13641 80 LKK------LRKKVSLVFQF----PEAQLFENTVLKDVEFGPKnfgFSEDEAKEKalkwLKKVGLSEDLiSKSPFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 146 QQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-222 |
8.34e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.18 E-value: 8.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQFYNLIPTLD 101
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 -VRKNILL-----PMLLDKRKvdeDRFSEIVSILGLS-DRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDR 174
Cdd:PRK13646 102 tVEREIIFgpknfKMNLDEVK---NYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 175 KNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-226 |
1.04e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.12 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTE--ISSLKeEAla 80
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPR-DA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfRRRKVGLIYQFYNLIPTLDVRKNILL------PMLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIAR 154
Cdd:COG3845 78 --IALGIGMVHQHFMLVPNLTVAENIVLgleptkGGRLDRKAARA-RIRELSERYGLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ---TILLITH--DEKIALeANRIVTMEDGVIVSEKVVK 226
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEIL----RRLAAegkSIIFITHklREVMAI-ADRVTVLRRGKVVGTVDTA 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-217 |
1.63e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.46 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAv 81
Cdd:PRK11300 4 PLLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frrRKvGLIYQFYN--LIPTLDVRKNIL-----------LPMLLD----KRKVDE--DRFSEIVSILGLSDRLNHLPSQL 142
Cdd:PRK11300 79 ---RM-GVVRTFQHvrLFREMTVIENLLvaqhqqlktglFSGLLKtpafRRAESEalDRAATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 143 SGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDG 217
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-220 |
1.97e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.99 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQF-YNLIPTL 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNILL-PMLLDKRKVDEDRFS-EIVSILGLSDRL-NHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNS 177
Cdd:PRK13649 102 TVLKDVAFgPQNFGVSQEEAEALArEKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 178 EEIVDLLnlsnKRFNQ---TILLITH-DEKIALEANRIVTMEDGVIV 220
Cdd:PRK13649 182 KELMTLF----KKLHQsgmTIVLVTHlMDDVANYADFVYVLEKGKLV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-222 |
2.96e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfRRRK 86
Cdd:PRK13548 6 RNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA--RRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VglIYQFYNLIPTLDVRKNI---LLPMLLDKRKVDE--DRFSEIVSILGLSDRLNHlpsQLSGGQQQRVSIARSLI---- 157
Cdd:PRK13548 80 V--LPQHSSLSFPFTVEEVVamgRAPHGLSRAEDDAlvAAALAQVDLAHLAGRDYP---QLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 158 --YRPAILLADEPTGNLDRKNSEEIVDLL-NLSNKRfNQTILLITHDEKIA-LEANRIVTMEDGVIVSE 222
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLArQLAHER-GLAVIVVLHDLNLAaRYADRIVLLHQGRLVAD 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-221 |
3.41e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.89 E-value: 3.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 38 IVGASGSGKSTLLHLLGGVDRPTSGKIYVED-TEISSLKEEALAVFRRRkVGLIYQFYNLIPTLDVRKNILLPMlldkRK 116
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEKRR-IGYVFQDARLFPHYKVRGNLRYGM----AK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 117 VDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD--RKNseEIVDLLNLSNKRFNQT 194
Cdd:PRK11144 104 SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKR--ELLPYLERLAREINIP 181
|
170 180
....*....|....*....|....*....
gi 497574098 195 ILLITH--DEKIALeANRIVTMEDGVIVS 221
Cdd:PRK11144 182 ILYVSHslDEILRL-ADRVVVLEQGKVKA 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-200 |
3.94e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.23 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGV-----DRPTSGKIYVEDTEISSLK 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALavfrRRKVGLIYQFYNLIPTLDVRKNILLPMLLDK----RKVDEDRFSEIVSILGL----SDRLNHLPSQLSGGQQ 147
Cdd:PRK14247 77 VIEL----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvksKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 148 QRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRfNQTILLITH 200
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF-LELKK-DMTIVLVTH 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-222 |
3.97e-29 |
|
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: 108.07 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfr 83
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLdkRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARL--LGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELI-LSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLIEE 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-217 |
6.48e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.33 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLL-HLLGGVDRPTSGKIYVEDTEISSLKEEALAV 81
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLITGDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRR---KVGLIYQFYNLIPTLDVRKNILLPMLLDK----------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQ 148
Cdd:PRK09984 80 DIRKsraNTGYIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDG 217
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-220 |
7.38e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 113.38 E-value: 7.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQ-FYNLIPTL 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVSQrVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 dvRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLPS----------QLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK11160 431 --RDNLLLA----APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 171 NLDRKNSEEIVDLLNLSNKrfNQTILLITHdEKIALEA-NRIVTMEDGVIV 220
Cdd:PRK11160 505 GLDAETERQILELLAEHAQ--NKTVLMITH-RLTGLEQfDRICVMDNGQII 552
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-220 |
9.23e-29 |
|
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: 108.09 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQ----FYNli 97
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQIGLVSQdvflFND-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 ptlDVRKNILLpmllDKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:cd03251 91 ---TVAENIAY----GRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497574098 167 EPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03251 164 EATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-222 |
9.93e-29 |
|
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: 112.59 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVD--RPTSGKI-----------YVEDTE 70
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 71 I---------SSLKEEAL-------AVFR--RRKVGLIYQ-FYNLIPTLDVRKNIL--LPMLLDKRKVDEDRFSEIVSIL 129
Cdd:TIGR03269 77 KvgepcpvcgGTLEPEEVdfwnlsdKLRRriRKRIAIMLQrTFALYGDDTVLDNVLeaLEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 130 GLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITH-DEKIALEA 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwPEVIEDLS 236
|
250
....*....|....
gi 497574098 209 NRIVTMEDGVIVSE 222
Cdd:TIGR03269 237 DKAIWLENGEIKEE 250
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-222 |
1.08e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.52 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEE--ALAV 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FR-------RRKVGLIYQFYNLIPTLDVRKNIL---LPMLLDKRKVDEDRFSEIVSILGLSDRLN-HLPSQLSGGQQQRV 150
Cdd:PRK10619 82 ADknqlrllRTRLTMVFQHFNLWSHMTVLENVMeapIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-221 |
1.98e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 108.67 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVT-ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAV 81
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRRKVGLIYQF--YNLIPTLDVRKNILLPMLLDKRKVDEDRF-SEIVSILGLSDRL-NHLPSQLSGGQQQRVSIARSLI 157
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEETVLKDVAFGPQNFGIPKEKAEKIaAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNlSNKRFNQTILLITH-DEKIALEANRIVTMEDGVIVS 221
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIIS 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-222 |
5.21e-28 |
|
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: 106.16 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 17 QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNL 96
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTlDVRKNILLpmllDKRKVDEDRFSEIVSILGLSDRLNHLPSQ-----------LSGGQQQRVSIARSLIYRPAILLA 165
Cdd:cd03253 87 FND-TIGYNIRY----GRPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 166 DEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-202 |
1.30e-27 |
|
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: 109.37 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNLIPTlD 101
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:TIGR02868 425 VRENLRLA----RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|...
gi 497574098 171 NLDRKNSEEIV-DLLNLSNKRfnqTILLITHDE 202
Cdd:TIGR02868 501 HLDAETADELLeDLLAALSGR---TVVLITHHL 530
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-220 |
1.47e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 105.17 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGsnQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfrrRK 86
Cdd:COG4604 5 KNVSKRYG--GKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKniLL-----------PMLLDKRKVDE--DRFseivSILGLSDRlnHLpSQLSGGQQQRVSIA 153
Cdd:COG4604 77 LAILRQENHINSRLTVRE--LVafgrfpyskgrLTAEDREIIDEaiAYL----DLEDLADR--YL-DELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDekI---ALEANRIVTMEDGVIV 220
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD--InfaSCYADHIVAMKDGRVV 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-180 |
1.60e-27 |
|
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: 104.55 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealaVFR 83
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-----MHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIY--QFYNLIPTLDVRKNIL--LPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYR 159
Cdd:cd03218 72 RARLGIGYlpQEASIFRKLTVEENILavLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180
....*....|....*....|.
gi 497574098 160 PAILLADEPTGNLDRKNSEEI 180
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDI 172
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-201 |
1.81e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 105.17 E-value: 1.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfrrrkvGLIYQFYNLIPTLD 101
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEE 179
Cdd:PRK11248 87 VQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|..
gi 497574098 180 IVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHD 188
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-220 |
2.01e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.81 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfR 83
Cdd:COG4559 2 LEAENLSVRLGGR----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKV-----GLIYQFynliPTLDVrknILL---PMLLDKRKVDE--DRFSEIVSILGLSDRLNHlpsQLSGGQQQRVSIA 153
Cdd:COG4559 76 RRAVlpqhsSLAFPF----TVEEV---VALgraPHGSSAAQDRQivREALALVGLAHLAGRSYQ---TLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 154 RSL--IYRPA-----ILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQ---TILLITHDEKI-ALEANRIVTMEDGVIV 220
Cdd:COG4559 146 RVLaqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLA----RQLARrggGVVAVLHDLNLaAQYADRILLLHQGRLV 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-214 |
2.18e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.08 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGkiyvedteisslkeeALAVFRRRKVGLIYQFYNLIP 98
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG---------------TVRRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TLDVRKNILLPM--------LLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:NF040873 69 SLPLTVRDLVAMgrwarrglWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTM 214
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-220 |
3.22e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRV--------------------TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGK 63
Cdd:PRK10070 5 LEIKNLYKIFGEHPQRAfkyieqglskeqilektglsLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 64 IYVEDTEISSLKEEALAVFRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSI--LGLSDRLNHLPSQ 141
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALrqVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 142 LSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVV 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-227 |
4.40e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.30 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:PRK10253 8 LRGEQLTLGYGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 rRKVGLIYQfyNLIPTLDVRKNILL--------PMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARS 155
Cdd:PRK10253 81 -RRIGLLAQ--NATTPGDITVQELVargryphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSEKVVKK 227
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKE 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-220 |
4.43e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 102.74 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA--- 80
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 ----VFRRRKVG--LIY--QFYNLIPTlDVRKNILlpMLLDKrkvdedrfseivsiLGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:cd03269 77 eergLYPKMKVIdqLVYlaQLKGLKKE-EARRRID--EWLER--------------LELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNlSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIR-ELARAGKTVILSTHQmELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-222 |
4.82e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYgSNQTRvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavf 82
Cdd:PRK13647 4 IIEVEDLHFRY-KDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQ-----FYNLIPTLDVRKNILlPMLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:PRK13647 78 -RSKVGLVFQdpddqVFSSTVWDDVAFGPV-NMGLDKDEVER-RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVLAE 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-217 |
4.89e-27 |
|
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: 102.13 E-value: 4.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavFRRRKVGLIyqfynliptld 101
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYV----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 vrknillPmlldkrkvdEDRFSE-IVSILGLSDRLNhLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEI 180
Cdd:cd03215 81 -------P---------EDRKREgLVLDLSVAENIA-LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 497574098 181 VDLLNLSNKRfNQTILLIT--HDEKIALeANRIVTMEDG 217
Cdd:cd03215 144 YRLIRELADA-GKAVLLISseLDELLGL-CDRILVMYEG 180
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-220 |
5.30e-27 |
|
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: 103.57 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrrRKVGLIY-QFYNLIP 98
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFL-----RRIGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TLDVRKNILLpmLLDKRKVDEDRF----SEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDR 174
Cdd:cd03267 109 DLPVIDSFYL--LAAIYDLPPARFkkrlDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 175 KNSEEIVDLLNLSNKRFNQTILLITHDEK-IALEANRIVTMEDGVIV 220
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLL 233
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-200 |
5.49e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.77 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGV-----DRPTSGKIYVEDTEISSLKEEA 78
Cdd:PRK14267 5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 79 LAVfrRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL--------GLSDRLNHLPSQLSGGQQQRV 150
Cdd:PRK14267 81 IEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFnqTILLITH 200
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-205 |
1.29e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 104.28 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIY------GSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKE 76
Cdd:PRK11308 5 LLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVfRRRKVGLIYQfyNLIPTLDVRKNI--LL--PMLLDKRKVDEDRFSEIVSIL---GL----SDRLNHLpsqLSGG 145
Cdd:PRK11308 85 EAQKL-LRQKIQIVFQ--NPYGSLNPRKKVgqILeePLLINTSLSAAERREKALAMMakvGLrpehYDRYPHM---FSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 146 QQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIA 205
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlsvvEHIA 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-220 |
1.60e-26 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 102.60 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:TIGR02323 3 LLQVSGLSKSYGGGK----GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKV-----GLIYQFY--NLIPTLDVRKNI-LLPMLLDKRKVDEDRFS-----EIVSILglSDRLNHLPSQLSGGQQQR 149
Cdd:TIGR02323 79 ERRRLmrtewGFVHQNPrdGLRMRVSAGANIgERLMAIGARHYGNIRATaqdwlEEVEID--PTRIDDLPRAFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIA-LEANRIVTMEDGVIV 220
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVArLLAQRLLVMQQGRVV 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-221 |
2.82e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.78 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFR-RRKVGLIYQF--YNLIP 98
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRlRKEIGLVFQFpeYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TlDVRKNILL-PMLLDKRKvdEDRFSEIVSILGL----SDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK13645 106 E-TIEKDIAFgPVNLGENK--QEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 174 RKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVS 221
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVIS 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-220 |
1.00e-25 |
|
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: 104.44 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTkiYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:COG4618 331 LSVENLT--VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 rRKVGLIYQFYNLIP-TldVRKNIllpmlldkrkvdeDRFSE-----IVS----------ILGLSD----RLNHLPSQLS 143
Cdd:COG4618 406 -RHIGYLPQDVELFDgT--IAENI-------------ARFGDadpekVVAaaklagvhemILRLPDgydtRIGEGGARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 144 GGQQQRVSIARSLIYRPAILLADEPTGNLDrknsEEIVDLLN--LSN-KRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLD----DEGEAALAaaIRAlKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-217 |
1.20e-25 |
|
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: 99.08 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSN-QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslkeealavfrrr 85
Cdd:cd03250 4 EDASFTWDSGeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 86 kVGLIYQFYNLIPTlDVRKNIL--LPMlldkrkvDEDRFSEIVSILGLSDRLNHLPSQ-----------LSGGQQQRVSI 152
Cdd:cd03250 68 -IAYVSQEPWIQNG-TIRENILfgKPF-------DEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-222 |
1.30e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.94 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYgSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALav 81
Cdd:PRK13642 3 KILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frRRKVGLIYQ-----FYNLIPTLDV---RKNILLPMLLDKRKVDEDRFSeiVSILGLSDRLnhlPSQLSGGQQQRVSIA 153
Cdd:PRK13642 80 --RRKIGMVFQnpdnqFVGATVEDDVafgMENQGIPREEMIKRVDEALLA--VNMLDFKTRE---PARLSGGQKQRVAVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
1.34e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 6 CENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVE-DTEISSLK--------- 75
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLPqeppldddl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 ---EEALAVFRRRKVglIYQFYNLI------PTLDVRKNILLPMLLDKRkvD----EDRFSEIVSILGLSDR-LNHLPSQ 141
Cdd:COG0488 77 tvlDTVLDGDAELRA--LEAELEELeaklaePDEDLERLAELQEEFEAL--GgweaEARAEEILSGLGFPEEdLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 142 LSGGQQQRVSIARSLIYRPAILLADEPTGNLDRknsEEIV---DLLnlsnKRFNQTILLITHD----EKIaleANRIVTM 214
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEwleEFL----KNYPGTVLVVSHDryflDRV---ATRILEL 222
|
....*..
gi 497574098 215 EDGVIVS 221
Cdd:COG0488 223 DRGKLTL 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-220 |
1.58e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.00 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVF 82
Cdd:PRK11701 6 LLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKV-----GLIYQfyN----LIPTLDVRKNILLP-MLLDKRKVDEDRFS-----EIVSILglSDRLNHLPSQLSGGQQ 147
Cdd:PRK11701 82 ERRRLlrtewGFVHQ--HprdgLRMQVSAGGNIGERlMAVGARHYGDIRATagdwlERVEID--AARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 148 QRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIA-LEANRIVTMEDGVIV 220
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVArLLAHRLLVMKQGRVV 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-220 |
2.69e-25 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 103.26 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSnqTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:TIGR02203 334 RNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL----RRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTlDVRKNILLPmllDKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARS 155
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYG---RTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-220 |
2.96e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 103.28 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 13 YGSNqtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfrrrkvgliyQ 92
Cdd:TIGR01193 485 YGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-----------Q 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 FYNLIP------TLDVRKNILLPmllDKRKVDEDRFSEIVSI-----------LGLSDRLNHLPSQLSGGQQQRVSIARS 155
Cdd:TIGR01193 549 FINYLPqepyifSGSILENLLLG---AKENVSQDEIWAACEIaeikddienmpLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 156 LIYRPAILLADEPTGNLDRKNSEEIVD-LLNLSNKrfnqTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNnLLNLQDK----TIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-217 |
3.02e-25 |
|
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: 96.36 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteisslkeealavfr 83
Cdd:cd03221 1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 rrkvgliyqfynliptldvrknillpmlldkrkvdedrfseivsILGLSDRLNHLPsQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03221 58 --------------------------------------------TWGSTVKIGYFE-QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLnlsnKRFNQTILLITHDEK-IALEANRIVTMEDG 217
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYfLDQVATKIIELEDG 143
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-222 |
7.69e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfrRRKVGLIYQFY-NLIPTL 100
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKL--RESVGMVFQDPdNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNI---LLPMLLDKRKVDEdRFSEIVSILGLSdRLNHLPSQ-LSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKN 176
Cdd:PRK13636 99 SVYQDVsfgAVNLKLPEDEVRK-RVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 177 SEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-220 |
9.38e-25 |
|
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: 97.18 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:cd03244 6 KNVSLRYRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQfynlIPTL---DVRKNillpmlLD--KRKVDEDRFS--------EIVSIL--GLSDRLNHLPSQLSGGQQQRVS 151
Cdd:cd03244 80 ISIIPQ----DPVLfsgTIRSN------LDpfGEYSDEELWQalervglkEFVESLpgGLDTVVEEGGENLSVGQRQLLC 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNlsNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-222 |
1.52e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVE--DT-EISSLKEealavfRRRKVGLIY-----QF 93
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTgDFSKLQG------IRKLVGIVFqnpetQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 YNLIPTLDVR---KNILLPMLLDKRKVDEdRFSEIvsilGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK13644 91 VGRTVEEDLAfgpENLCLPPIEIRKRVDR-ALAEI----GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-168 |
1.62e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.02 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslkeeALA 80
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-----HLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFRRRKVGLIY--Q----FYNLiptlDVRKNIL--LPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:COG1137 72 MHKRARLGIGYlpQeasiFRKL----TVEDNILavLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170
....*....|....*.
gi 497574098 153 ARSLIYRPAILLADEP 168
Cdd:COG1137 148 ARALATNPKFILLDEP 163
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-220 |
1.97e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 96.45 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeISSLKEEALAvfrrrkvgliyqfynLIP 98
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGLGGG---------------FNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TLDVRKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLnHLP-SQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRK 175
Cdd:cd03220 98 ELTGRENIYLNGRLLglSRKEIDEKIDEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497574098 176 NSEEIVDLLN--LSNKRfnqTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:cd03220 177 FQEKCQRRLRelLKQGK---TVILVSHDPSSIKRlCDRALVLEKGKIR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-222 |
2.15e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.07 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfRRRKV 87
Cdd:cd03247 5 NVSFSYPEQEQ--QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTldvrknillpmlldkrkvdedrfseivSILglsdrlNHLPSQLSGGQQQRVSIARSLIYRPAILLADE 167
Cdd:cd03247 78 SVLNQRPYLFDT---------------------------TLR------NNLGRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 168 PTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-220 |
2.52e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKE--EALAVFRRRKVGLIYQFYNLIPTL 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNILLPM----LLDKR---KVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK14246 106 SIYDNIAYPLkshgIKEKReikKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497574098 174 RKNSEEIVDLLNLSNKRFnqTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK14246 186 IVNSQAIEKLITELKNEI--AIVIVSHNpQQVARVADYVAFLYNGELV 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
2.75e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.85 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTR-----------------VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIY 65
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 66 VEDtEISSLKEEALAvfrrRKVGLIY-Q----FYNL--IPTLDVRKNILlpmlldkrKVDEDRF----SEIVSILGLSDR 134
Cdd:COG4586 81 VLG-YVPFKRRKEFA----RRIGVVFgQrsqlWWDLpaIDSFRLLKAIY--------RIPDAEYkkrlDELVELLDLGEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 135 LNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIaleANR 210
Cdd:COG4586 148 LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmddiEAL---CDR 224
|
250
....*....|
gi 497574098 211 IVTMEDGVIV 220
Cdd:COG4586 225 VIVIDHGRII 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-220 |
3.40e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKS-TLLHLLGGVDRP----TSGKIYVEDTEISSLK 75
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVFRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSIL---GL---SDRLNHLPSQLSGGQQ 147
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQepMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLdrvGIrqaAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 148 QRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIV 220
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-227 |
6.90e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.16 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKS-TLLHLLGGVDRpTSGKIYVE-------DTEISS 73
Cdd:PRK10261 11 DVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDkmllrrrSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 74 LKEEALAVFRRRK---VGLIYQ--FYNLIPTLDVRKNILLPMLLD------------KRKVDEDRFSEIVSILGlsdrln 136
Cdd:PRK10261 90 LSEQSAAQMRHVRgadMAMIFQepMTSLNPVFTVGEQIAESIRLHqgasreeamveaKRMLDQVRIPEAQTILS------ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 137 HLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTME 215
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMY 243
|
250
....*....|..
gi 497574098 216 DGVIVSEKVVKK 227
Cdd:PRK10261 244 QGEAVETGSVEQ 255
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-220 |
2.19e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.61 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQfyNliPTL 100
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESW----RKHLSWVGQ--N--PQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 ---DVRKNILLP----------MLLDKRKVDEdrFseivsILGLSDRLNHLPSQ----LSGGQQQRVSIARSLIYRPAIL 163
Cdd:PRK11174 435 phgTLRDNVLLGnpdasdeqlqQALENAWVSE--F-----LPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 164 LADEPTGNLDRkNSEEIVdLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK11174 508 LLDEPTASLDA-HSEQLV-MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-219 |
2.21e-23 |
|
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: 93.69 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYgSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavf 82
Cdd:cd03248 11 IVKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFynliPTL---DVRKNILLPMlldkRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQ 148
Cdd:cd03248 87 -HSKVSLVGQE----PVLfarSLQDNIAYGL----QSCSFECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfnQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-222 |
3.35e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 18 TRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGV---DRPTSGKIYVEDTEISSlkEEALAVfrRRKVGLIYQ-- 92
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDI--REKVGIVFQnp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 ---FYNLIPTLDVrknillPMLLDKRKVDEDRFSEIV----SILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLA 165
Cdd:PRK13640 94 dnqFVGATVGDDV------AFGLENRAVPRPEMIKIVrdvlADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 166 DEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-219 |
3.51e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 97.03 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTkiYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:TIGR01842 317 LSVENVT--IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG--- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 rRKVGLIYQFYNLIPTlDVRKNILLPmlldKRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSI 152
Cdd:TIGR01842 392 -KHIGYLPQDVELFPG-TVAENIARF----GENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIAL 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-211 |
3.57e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSNQtrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGV-----DRPTSGKIYVEDTEISSLKE 76
Cdd:PRK14239 4 PILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVfrRRKVGLIYQFYNLIPtLDVRKNILLPMLLDKRKvDEDRFSEIV--SILGLS------DRLNHLPSQLSGGQQQ 148
Cdd:PRK14239 80 DTVDL--RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIK-DKQVLDEAVekSLKGASiwdevkDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVD-LLNLSNKrfnQTILLITHDEKialEANRI 211
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEEtLLGLKDD---YTMLLVTRSMQ---QASRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-222 |
3.93e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTkiygsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK-EEALA 80
Cdd:COG1129 255 VVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 ---VF---RRRKVGliyqfynLIPTLDVRKNILLPML--------LDKRKVDEdRFSEIVSILGL-SDRLNHLPSQLSGG 145
Cdd:COG1129 327 agiAYvpeDRKGEG-------LVLDLSIRENITLASLdrlsrgglLDRRRERA-LAEEYIKRLRIkTPSPEQPVGNLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 146 QQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN-LSNKrfNQTILLIT--HDEKIALeANRIVTMEDGVIVSE 222
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIReLAAE--GKAVIVISseLPELLGL-SDRILVMREGRIVGE 475
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-220 |
7.09e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 96.33 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 16 NQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFyn 95
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQE-- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 96 liPTL---DVRKNILLPMlldkRKVDEDRFSEIVSILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPA 161
Cdd:TIGR00958 564 --PVLfsgSVRENIAYGL----TDTPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 162 ILLADEPTGNLDrknsEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:TIGR00958 638 VLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2-220 |
8.13e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 8.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIY------------------GSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGK 63
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 64 IYVeDTEISSLKEealavfrrrkVGLIYQfynliPTLDVRKNILLPMLL---DKRKVDEdRFSEIVSILGLSDRLnHLP- 139
Cdd:COG1134 83 VEV-NGRVSALLE----------LGAGFH-----PELTGRENIYLNGRLlglSRKEIDE-KFDEIVEFAELGDFI-DQPv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 140 SQLSGGQQQRVSIARSLIYRPAILLADE--PTGNLD--RKnseeivdllnlSNKRFNQ------TILLITHDEKIALE-A 208
Cdd:COG1134 145 KTYSSGMRARLAFAVATAVDPDILLVDEvlAVGDAAfqKK-----------CLARIRElresgrTVIFVSHSMGAVRRlC 213
|
250
....*....|..
gi 497574098 209 NRIVTMEDGVIV 220
Cdd:COG1134 214 DRAIWLEKGRLV 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-226 |
2.10e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfr 83
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKR---------KVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIAR 154
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSEKVVK 226
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVS 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-220 |
2.24e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.68 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 17 QTRVTALNNVNLSVQKGDFVSIVGASGSGKS-TLLHLLG----GVDRpTSGKIYVEDTEIsslkeeALAVFRRRKVGLIY 91
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGilpaGVRQ-TAGRVLLDGKPV------APCALRGRKIATIM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 92 Q----FYNliPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGLSDR---LNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:PRK10418 86 QnprsAFN--PLHTMHTHARETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEK-IALEANRIVTMEDGVIV 220
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRIV 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-222 |
2.43e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEI---SSLKEEALAVFRRRkVGLIYQFYNLI 97
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFRRR-VGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 PtLDVRKNILLPMLLDK-------RKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK14271 114 P-MSIMDNVLAGVRAHKlvprkefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRFnqTILLITHD-EKIALEANRIVTMEDGVIVSE 222
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-220 |
2.60e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.09 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealavf 82
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGliyqfY-----NLIPTLDVRKNIL-LPML--LDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIAR 154
Cdd:COG4152 70 -RRRIG-----YlpeerGLYPKMKVGEQLVyLARLkgLSKAEAKR-RADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVI-RELAAKGTTVIFSSHQmelvEEL---CDRIVIINKGRKV 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-200 |
2.83e-22 |
|
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: 90.79 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRP---TSGKIYVEDTEISSlkeealAVFRRRkVGLIYQFYNLIPT 99
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP------DQFQKC-VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 LDVRKNIL-LPMLLDKRKVDEDRFSEIVSILGLSDrLNHLP------SQLSGGQQQRVSIARSLIYRPAILLADEPTGNL 172
Cdd:cd03234 96 LTVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRD-LALTRiggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*...
gi 497574098 173 DRKNSEEIVDLLNLSNKRfNQTILLITH 200
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-223 |
5.44e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.02 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 14 GSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGG--VDRPTSGKIYVEDTEISslkeealavfrrRKVGLIY 91
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG------------REASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 92 QFYNLIPTLDVrknillpmlldkrkvdedrfSEIVSILGLSDRLNHL--PSQLSGGQQQRVSIARSLIYRPAILLADEPT 169
Cdd:COG2401 105 AIGRKGDFKDA--------------------VELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 170 GNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKI--ALEANRIVTMEDGVIVSEK 223
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVidDLQPDLLIFVGYGGVPEEK 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-201 |
6.12e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKST----LLHLLggvdrPTSGKIYVEDTEISSLKEEALAVFRRRkVGLIYQFYN- 95
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPNs 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 96 -LIPTLDVRKNIL------LPMLLDKRKvdEDRFSEIVSILGLSDRLNH-LPSQLSGGQQQRVSIARSLIYRPAILLADE 167
Cdd:PRK15134 374 sLNPRLNVLQIIEeglrvhQPTLSAAQR--EQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190
....*....|....*....|....*....|....
gi 497574098 168 PTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-221 |
8.12e-22 |
|
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: 89.01 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfr 83
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIYQfynlIPTL---DVRKNillpmlLDKrkvdEDRFS--EIVSILGLSDRlnhlPSQLSGGQQQRVSIARSLIY 158
Cdd:cd03369 81 RSSLTIIPQ----DPTLfsgTIRSN------LDP----FDEYSdeEIYGALRVSEG----GLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIVS 221
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-200 |
1.21e-21 |
|
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: 88.38 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVTA--LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGG--VDRPTSGKIYVEDTeisSLKEEALavf 82
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR---PLDKRSF--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILLPMLLdkrkvdedrfseivsilglsdrlnhlpSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:cd03213 81 -RKIIGYVPQDDILHPTLTVRETLMFAAKL---------------------------RGLSGGERKRVSIALELVSNPSL 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITH 200
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLrRLADT--GRTIICSIH 169
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-220 |
1.34e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.47 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:PRK10790 344 DNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQfynlIPTL---DVRKNILLpmlldKRKVDEDR---------FSEIVSIL--GLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:PRK10790 417 VAMVQQ----DPVVladTFLANVTL-----GRDISEEQvwqaletvqLAELARSLpdGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSnkRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-201 |
1.52e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLH-------LLGGVDrpTSGKIYVEDTEISSLK 75
Cdd:PRK14243 10 VLRTENLNVYYGSF----LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 76 EEALAVfrRRKVGLIYQFYNLIPTlDVRKNILLPMLLDKRKVDEDRFSE-----IVSILGLSDRLNHLPSQLSGGQQQRV 150
Cdd:PRK14243 84 VDPVEV--RRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVErslrqAALWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFnqTILLITHD 201
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHN 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-201 |
2.08e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.44 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVTAL--NNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFrR 84
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCifDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 85 RKVGLIYQFYNLIPTLDVRKNILLPmLLDKRKVDEDRFSEIVSI----LGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYP-LREHTQLPAPLLHSTVMMkleaVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-220 |
2.31e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYV-EDTEISSLKEEALav 81
Cdd:COG0488 315 VLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQE-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frrrkvgliyqfynlipTLDVRKNILLPMlldKRKVDEDRFSEIVSILGL----SDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:COG0488 389 -----------------ELDPDKTVLDEL---RDGAPGGTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLNlsnkRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALD----DFPGTVLLVSHDryflDRV---ATRILEFEDGGVR 508
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-222 |
3.08e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.40 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEealA 80
Cdd:PRK11614 3 KVMLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRfseIVSILGLSDRLNHLPSQ----LSGGQQQRVSIARSL 156
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQER---IKWVYELFPRLHERRIQragtMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 157 IYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENGHVVLE 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-220 |
3.18e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.69 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGS-----NQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEE 77
Cdd:PRK15112 4 LLEVRNLSKTFRYrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 alavFRRRKVGLIYQ--FYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILG----LSDRLNHLPSQLSGGQQQRVS 151
Cdd:PRK15112 84 ----YRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 152 IARSLIYRPAILLADEPTGNLDRKNSEEIVDL-LNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLmLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-222 |
3.26e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavf 82
Cdd:PRK13537 7 PIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNILL----------------PMLLDKRKvdedrfseivsilgLSDRLNHLPSQLSGGQ 146
Cdd:PRK13537 79 -RQRVGVVPQFDNLDPDFTVRENLLVfgryfglsaaaaralvPPLLEFAK--------------LENKADAKVGELSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 147 QQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITH-DEKIALEANRIVTMEDGVIVSE 222
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHfMEEAERLCDRLCVIEEGRKIAE 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-222 |
3.99e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvf 82
Cdd:PRK11231 2 TLRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrRKVGLIYQFYnLIPT-LDVRKNILL---PML-LDKRKVDEDRFS-----EIVSILGLSDRlnhLPSQLSGGQQQRVSI 152
Cdd:PRK11231 76 --RRLALLPQHH-LTPEgITVRELVAYgrsPWLsLWGRLSAEDNARvnqamEQTRINHLADR---RLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRyCDHLVVLANGHVMAQ 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-222 |
7.77e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTkiyGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslkeeALAV 81
Cdd:COG3845 256 VVLEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT-----GLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRRKVGLIY-----QFYNLIPTLDVRKNILL------PM----LLDKRKVDE------DRFSeiVSILGLSDRLnhlpS 140
Cdd:COG3845 328 RERRRLGVAYipedrLGRGLVPDMSVAENLILgryrrpPFsrggFLDRKAIRAfaeeliEEFD--VRTPGPDTPA----R 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 141 QLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVD-LLNLSNKrfNQTILLITH--DEKIALeANRIVTMEDG 217
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDA--GAAVLLISEdlDEILAL-SDRIAVMYEG 478
|
....*
gi 497574098 218 VIVSE 222
Cdd:COG3845 479 RIVGE 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-217 |
8.17e-21 |
|
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: 90.27 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPT---SGKIYVEDTEissLKEEAL 79
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSP---LKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 AVFRRRKVGLIYQFYNLIPTLDVRKNILL--PMLLDKRKVDED----RFSEIVSILGLSDRLNHLP-SQLSGGQQQRVSI 152
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNlSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIR-DLKAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-222 |
8.99e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfrRRKV 87
Cdd:PRK13536 46 GVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-----RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTLDVRKNILL---PMLLDKRKVdEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILL 164
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVfgrYFGMSTREI-EAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 165 ADEPTGNLDRKNSEEIVDLLNLSNKRfNQTILLITHdekIALEA----NRIVTMEDGVIVSE 222
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTH---FMEEAerlcDRLCVLEAGRKIAE 253
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-220 |
9.79e-21 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.88 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQ---------F 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQdtvlfndtiA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 YNLI---PTL---DVRKNILLPMLldkrkvdeDRFseivsILGLSDRLNHLPSQ----LSGGQQQRVSIARSLIYRPAIL 163
Cdd:COG5265 450 YNIAygrPDAseeEVEAAARAAQI--------HDF-----IESLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-217 |
2.33e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDteisslKEEALAVFRRrkvglIYqfynlIPTLDV 102
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------GARVLFLPQR-----PY-----LPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPmlLDKRKVDEDRFSEIVSILGLSDRLNHL------PSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKN 176
Cdd:COG4178 443 REALLYP--ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497574098 177 SEEIVDLLNlsNKRFNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:COG4178 521 EAALYQLLR--EELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-220 |
3.82e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.09 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQFYNLIpTLD 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNIAVVFQDAGLF-NRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILL--------PMLLDKRKVDEDRFseivsILGLSDRLNHLP----SQLSGGQQQRVSIARSLIYRPAILLADEPT 169
Cdd:PRK13657 425 IEDNIRVgrpdatdeEMRAAAERAQAHDF-----IERKPDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 170 GNLDRKNSEEIVDLLNlsNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK13657 500 SALDVETEAKVKAALD--ELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-173 |
1.30e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALA 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 vfrRRKVGLIYQ----------FYNLIPTLDVRKNIllpmlldKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRV 150
Cdd:PRK10895 77 ---RRGIGYLPQeasifrrlsvYDNLMAVLQIRDDL-------SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRV 146
|
170 180
....*....|....*....|...
gi 497574098 151 SIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVD 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-173 |
1.35e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfrrRKVGLIYQFYNLIPT 99
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 LDVRKNILL---PML--------LDKRKVdeDRFSEIVSILGLSDRlnhlP-SQLSGGQQQRVSIARSLIYRPAILLADE 167
Cdd:PRK09536 92 FDVRQVVEMgrtPHRsrfdtwteTDRAAV--ERAMERTGVAQFADR----PvTSLSGGERQRVLLARALAQATPVLLLDE 165
|
....*.
gi 497574098 168 PTGNLD 173
Cdd:PRK09536 166 PTASLD 171
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-214 |
1.38e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.34 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRP----TSGKIYVEDTEISSLKE 76
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EALAVFRRRKVGLIYQ--FYNLIPTLDVRKNIL--LP------MLLDKRKVDEDRFSEIVSILGLSDR---LNHLPSQLS 143
Cdd:COG4170 81 RERRKIIGREIAMIFQepSSCLDPSAKIGDQLIeaIPswtfkgKWWQRFKWRKKRAIELLHRVGIKDHkdiMNSYPHELT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 144 GGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTM 214
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWADTITVL 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-185 |
1.88e-19 |
|
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: 82.41 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavfRRRKVGLIYQFYNLIPTL 100
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNI-LLPMLLDKRKVDEDRFSEIVSILGLSDRLNHlpsQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNsee 179
Cdd:TIGR01189 89 SALENLhFWAAIHGGAQRTIEDALAAVGLTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG--- 162
|
....*.
gi 497574098 180 iVDLLN 185
Cdd:TIGR01189 163 -VALLA 167
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-201 |
2.40e-19 |
|
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: 85.76 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslkeealavfrrRKV 87
Cdd:TIGR03719 9 RVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG---------------IKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTLDVRKNILLPMLLDKRKVDedRFSEIVSILG---------------LSDRLNH--------------- 137
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALD--RFNEISAKYAepdadfdklaaeqaeLQEIIDAadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 138 ---LP------SQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDrknsEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:TIGR03719 149 alrCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
3.44e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 3.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPT---SGKIYVEDTEI--SSLKEE 77
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELqaSNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 alavfRRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKV-DED----RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:PRK13549 80 -----ERAGIAIIHQELALVKELSVLENIFLGNEITPGGImDYDamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 153 ARSLIYRPAILLADEPTGNLDRKnseEIVDLLNLSN--KRFNQTILLITH--DEKIALeANRIVTMEDG 217
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTES---ETAVLLDIIRdlKAHGIACIYISHklNEVKAI-SDTICVIRDG 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-173 |
5.01e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.58 E-value: 5.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPTSGKIYVEDTEISSLKEEALAVFR------RRKVGLI--YQFY 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHRaylsqqQSPPFAMpvFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 95 NLiptldvrkniLLPMLLDKRKVdEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIY-------RPAILLADE 167
Cdd:COG4138 91 AL----------HQPAGASSEAV-EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
....*.
gi 497574098 168 PTGNLD 173
Cdd:COG4138 160 PMNSLD 165
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-201 |
3.72e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.29 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfRRRKVGLIYQ--FYNLIPT 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA-VRSDIQMIFQdpLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 LDVRKNILLPML-----LDKRKVdEDRFSEIVSILGLSDRL-NHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK15079 115 MTIGEIIAEPLRtyhpkLSRQEV-KDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*...
gi 497574098 174 RKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-222 |
6.44e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.34 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVD--RPTSGKIYVEDTEISSLKEEALAv 81
Cdd:cd03217 1 LEIKDLHVSVGGKEI----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frRRKVGLIYQFYNLIPtlDVRKNILLpmlldkRKVDEDrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03217 76 --RLGIFLAFQYPPEIP--GVKNADFL------RYVNEG---------------------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLN-LSNKrfNQTILLITHDEKIA--LEANRIVTMEDGVIVSE 222
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINkLREE--GKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKS 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-200 |
9.75e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLL-----GGVDRptSGKIYVEDTEISslkeealAVFRRRKVGLIYQFYNLI 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspKGVKG--SGSVLLNGMPID-------AKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 PTLDVRKN-ILLPMLLDKRKVDED----RFSEIVSILGLSDRLNHL---PSQ---LSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:TIGR00955 112 PTLTVREHlMFQAHLRMPRRVTKKekreRVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|....*
gi 497574098 167 EPTGNLDRKNSEEIVDLL-NLSNKRfnQTILLITH 200
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLkGLAQKG--KTIICTIH 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-215 |
3.12e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFR 83
Cdd:PRK13539 3 LEGEDLACVRGG----RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKVGLIyqfynliPTLDVRKNILLpmLLDKRKVDEDRFSEIVSILGLSDrLNHLPSQ-LSGGQQQRVSIARSLIYRPAI 162
Cdd:PRK13539 79 GHRNAMK-------PALTVAENLEF--WAAFLGGEELDIAAALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 163 LLADEPTGNLDRkNSEEIvdLLNLSNKRFNQ--TILLITHdEKIALEANRIVTME 215
Cdd:PRK13539 149 WILDEPTAALDA-AAVAL--FAELIRAHLAQggIVIAATH-IPLGLPGARELDLG 199
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-220 |
4.40e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.31 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 1 MEILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVD----RPTSGKIYVEDTEISSLKE 76
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 77 EAlavfRRRKVG----LIYQFYN--LIPTLDVRKNIL--LPMLLDK---------RKvdeDRFSEIVSILGLSDR---LN 136
Cdd:PRK15093 81 RE----RRKLVGhnvsMIFQEPQscLDPSERVGRQLMqnIPGWTYKgrwwqrfgwRK---RRAIELLHRVGIKDHkdaMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 137 HLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTME 215
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLY 233
|
....*
gi 497574098 216 DGVIV 220
Cdd:PRK15093 234 CGQTV 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-184 |
4.49e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 25 NVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEalavFRRRkvgLIY------------Q 92
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQD---LLYlghqpgikteltA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 FYNLiptldvrkNILLPMlldKRKVDEDRFSEIVSILGLSDRLnHLP-SQLSGGQQQRVSIARSLIYRPAILLADEPTGN 171
Cdd:PRK13538 92 LENL--------RFYQRL---HGPGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170
....*....|...
gi 497574098 172 LDRKNSEEIVDLL 184
Cdd:PRK13538 160 IDKQGVARLEALL 172
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-217 |
6.71e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEI--SSLKeEALAVfrrrKVGLIYQFYNLI 97
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTT-AALAA----GVAIIYQELHLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 PTLDVRKNILLPMLLDKRK-VDEDRFSEIVsilglSDRLNHL-----PSQ----LSGGQQQRVSIARSLIyRPAILLA-D 166
Cdd:PRK11288 92 PEMTVAENLYLGQLPHKGGiVNRRLLNYEA-----REQLEHLgvdidPDTplkyLSIGQRQMVEIAKALA-RNARVIAfD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 167 EPTGNLDRKNSEE---IVDLLNLSNKrfnqTILLITH--DEKIALeANRIVTMEDG 217
Cdd:PRK11288 166 EPTSSLSAREIEQlfrVIRELRAEGR----VILYVSHrmEEIFAL-CDAITVFKDG 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-220 |
9.47e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 9.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRrKVGLIYQ--FYNLI 97
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 PTLDVRKNILLPML---LDKRKVDEDRFSEIVSILGLsdRLNH---LPSQLSGGQQQRVSIARSLIYRPAILLADEPTGN 171
Cdd:PRK10261 416 PRQTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGL--LPEHawrYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 172 LDRKNSEEIVDLLNLSNKRFNQTILLITHD----EKIaleANRIVTMEDGVIV 220
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDmavvERI---SHRVAVMYLGQIV 543
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-201 |
1.12e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteissLKEEALavfrrrK 86
Cdd:PRK09544 8 ENVSVSFGQRRV----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKL------R 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDedrfseivsILGLSDRLN--HL---PSQ-LSGGQQQRVSIARSLIYRP 160
Cdd:PRK09544 69 IGYVPQKLYLDTTLPLTVNRFLRLRPGTKKED---------ILPALKRVQagHLidaPMQkLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-217 |
1.85e-16 |
|
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: 75.06 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 13 YGSNqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQ 92
Cdd:cd03290 10 WGSG---LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 FYNLIpTLDVRKNILLPMLLDKRkvdedRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRVSIARSLIYRPA 161
Cdd:cd03290 87 KPWLL-NATVEENITFGSPFNKQ-----RYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 162 ILLADEPTGNLDRKNS-----EEIVDLLNlSNKRfnqTILLITHDEKIALEANRIVTMEDG 217
Cdd:cd03290 161 IVFLDDPFSALDIHLSdhlmqEGILKFLQ-DDKR---TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-220 |
2.14e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIY-----VEDTEISSLkeealavfrRRKVGLIYQFYNL 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldghdLRDYTLASL---------RNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTlDVRKNILLPMlldkrkvdEDRFS--EIVS----------ILGLSDRLNHLPSQ----LSGGQQQRVSIARSLIYRP 160
Cdd:PRK11176 429 FND-TIANNIAYAR--------TEQYSreQIEEaarmayamdfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIV 557
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-222 |
2.68e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAvfrrRKVGLIYQFYNLIPTL 100
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNILL---P---MLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDR 174
Cdd:PRK10575 101 TVRELVAIgryPwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 175 KNSEEIVDLLN-LSNKRfNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK10575 181 AHQVDVLALVHrLSQER-GLTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-201 |
5.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRpTSGKIYVE-DTEI--SSLKEEALA 80
Cdd:PRK14258 8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEgRVEFfnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VFR-RRKVGLIYQFYNLIPtLDVRKNILLPMLLD--KRKVDEDRFSEivSILGLSD-------RLNHLPSQLSGGQQQRV 150
Cdd:PRK14258 83 LNRlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwRPKLEIDDIVE--SALKDADlwdeikhKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-217 |
6.00e-16 |
|
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: 76.59 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYgsNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIsslkEEALAVFRRrK 86
Cdd:TIGR01257 932 KNLVKIF--EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQ-S 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFsEIVSIL---GLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAIL 163
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQL-EMEAMLedtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 164 LADEPTGNLDRKNSEEIVDLlnLSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDL--LLKYRSGRTIIMSTHHmDEADLLGDRIAIISQG 1136
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-220 |
8.83e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVED---TEISSLKEEALAVFrrrkvgLIYQFYNL 96
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQLGIY------LVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTLDVRKNILLPmlLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKN 176
Cdd:PRK15439 98 FPNLSVKENILFG--LPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 177 SE----EIVDLLNLsnkrfNQTILLITHD-EKIALEANRIVTMEDGVIV 220
Cdd:PRK15439 176 TErlfsRIRELLAQ-----GVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-202 |
9.67e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 75.67 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 25 NVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGkiyvedteisslkeealAVFRRRKVGLIYQFYNLIPTLDVRK 104
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-----------------TVFRSAKVRMAVFSQHHVDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 105 NILLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPS-QLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDL 183
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQG 669
|
170
....*....|....*....
gi 497574098 184 LNLsnkrFNQTILLITHDE 202
Cdd:PLN03073 670 LVL----FQGGVLMVSHDE 684
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-221 |
1.37e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKI-YVEDTEISSL-----KEEALAVFRRRKVGLIYQ---- 92
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARLqqdppRNVEGTVYDFVAEGIEEQaeyl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 -FYNLIPTL---DVRKNILLPMLLDKRKVD-------EDRFSEIVSILGLSDrlNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:PRK11147 99 kRYHDISHLvetDPSEKNLNELAKLQEQLDhhnlwqlENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 162 ILLADEPTGNLDRKNSEEIVDLLnlsnKRFNQTILLITHDEK-IALEANRIVTMEDGVIVS 221
Cdd:PRK11147 177 VLLLDEPTNHLDIETIEWLEGFL----KTFQGSIIFISHDRSfIRNMATRIVDLDRGKLVS 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-220 |
1.51e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 17 QTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQfynl 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQ---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTL---DVRKNILLpmllDKRKVDEDRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRVSIARSLIYRPAI 162
Cdd:PRK10789 397 TPFLfsdTVANNIAL----GRPDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 163 LLADEPTGNLDRKNSEEIvdLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PRK10789 473 LILDDALSAVDGRTEHQI--LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-219 |
1.89e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 25 NVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfrRRKVGLIY-----QFYNLIPT 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 LDVRKNIL-----LPMLLDKRKVDEDRFSEIVSILGLsdRLNHlPSQ----LSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK15439 356 APLAWNVCalthnRRGFWIKPARENAVLERYRRALNI--KFNH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 171 NLDRKNSEEIVDLLNlSNKRFNQTILLITHD-EKIALEANRIVTMEDGVI 219
Cdd:PRK15439 433 GVDVSARNDIYQLIR-SIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEI 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-220 |
1.90e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTS--GKIYVEDTEISSlkeealAVFRRrkVGLIYQFYNLIP 98
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK------QILKR--TGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TLDVRKNIL------LPMLLDKRkvDEDRFSE-IVSILGLSDRLNHLPSQ-----LSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:PLN03211 154 HLTVRETLVfcsllrLPKSLTKQ--EKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 167 EPTGNLDRKNSEEIV-DLLNLSNKrfNQTILLITHDekialEANRIVTMEDGVIV 220
Cdd:PLN03211 232 EPTSGLDATAAYRLVlTLGSLAQK--GKTIVTSMHQ-----PSSRVYQMFDSVLV 279
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-201 |
2.04e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.38 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslkeealavfrrRKV 87
Cdd:PRK11819 11 RVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG---------------IKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIYQFYNLIPTLDVRKNILLPMLLDKRKVDedRFSEIVSILG---------------LSDRLNH--------------- 137
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEEGVAEVKAALD--RFNEIYAAYAepdadfdalaaeqgeLQEIIDAadawdldsqleiamd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 138 ---LP------SQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDrknsEEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK11819 151 alrCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-217 |
3.21e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPT---SGKIYVEDTEISslkeeal 79
Cdd:NF040905 1 ILEMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGEVCR------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 avFR------RRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKV---DE--DRFSEIVSILGLSDRLNHLPSQLSGGQQQ 148
Cdd:NF040905 69 --FKdirdseALGIVIIHQELALIPYLSIAENIFLGNERAKRGVidwNEtnRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKlNEIRRVADSITVLRDG 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-220 |
4.20e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.64 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVD--RPTSGKIYVEDTEISSLK-EEalavfrRRKVGLIYQF------ 93
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSpDE------RARAGIFLAFqypvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 -----YNLIPT-LDVRKNILLPMLLDKRKVDEdrfseIVSILGLS----DR-LNhlpSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:COG0396 90 pgvsvSNFLRTaLNARRGEELSAREFLKLLKE-----KMKELGLDedflDRyVN---EGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 163 LLADEPTGNLD----RKNSEEIVDLlnlsnKRFNQTILLITHDEKI--ALEANRIVTMEDGVIV 220
Cdd:COG0396 162 AILDETDSGLDidalRIVAEGVNKL-----RSPDRGILIITHYQRIldYIKPDFVHVLVDGRIV 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-200 |
4.28e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 70.74 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdRPTSGKIYVEDTEISSLKEEALavf 82
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITGEILINGRPLDKNF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQFYNLIPTLDVRKNIllpmlldkrkvdedRFSEIVSILGLSDRlnhlpsqlsggqqQRVSIARSLIYRPAI 162
Cdd:cd03232 78 -QRSTGYVEQQDVHSPNLTVREAL--------------RFSALLRGLSVEQR-------------KRLTIGVELAAKPSI 129
|
170 180 190
....*....|....*....|....*....|....*....
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITH 200
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLkKLADS--GQAILCTIH 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-223 |
5.39e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 73.29 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslkEEALAVFRRrkvgLI-------YQFY 94
Cdd:COG4615 347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQ----LFsavfsdfHLFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 95 NLI----PTLDVRKNILLPML-LD-KRKVDEDRFSEIvsilglsdrlnhlpsQLSGGQQQRVsiarSLIY-----RPaIL 163
Cdd:COG4615 420 RLLgldgEADPARARELLERLeLDhKVSVEDGRFSTT---------------DLSQGQRKRL----ALLValledRP-IL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 164 LADE------PTgnLDRKNSEEIVDLLnlsnKRFNQTILLITHDEKIALEANRIVTMEDGVIVSEK 223
Cdd:COG4615 480 VFDEwaadqdPE--FRRVFYTELLPEL----KARGKTVIAISHDDRYFDLADRVLKMDYGKLVELT 539
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-179 |
7.83e-15 |
|
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: 70.21 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavfrRRKVGLIYQFYNLIPTL 100
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-----ARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 101 DVRKNILLPMLLDKRKVDEDRFSEiVSILGLSDRLNHlpsQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDrKNSEE 179
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALAR-VGLNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVA 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-212 |
7.91e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVfrRRKVGLIYQ------FYNL 96
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL--RQQVATVFQdpeqqiFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTlDVR---KNILLPMLLDKRKVDEdrfseivsILGLSD--RLNHLPSQ-LSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK13638 95 IDS-DIAfslRNLGVPEAEITRRVDE--------ALTLVDaqHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497574098 171 NLDRKNSEEIVDLLNLSNKRFNQtILLITHDEKIALEANRIV 212
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAV 206
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-219 |
7.97e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.70 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlavFRRRKVGLIYQFYnliptld 101
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED---YRKLFSAVFTDFH------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 vrkniLLPMLLDKRK--VDEDRFSEIVSILGLSDRLNH-----LPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD- 173
Cdd:PRK10522 408 -----LFDQLLGPEGkpANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDp 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 174 ---RKNSEEIVDLLNLSNKrfnqTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:PRK10522 483 hfrREFYQVLLPLLQEMGK----TIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-173 |
1.17e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 26 VNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPTSGKIYVEDTEISSLKEEALAVFRrrkvGLIYQFYNLIPTLDVRKN 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 106 ILLpMLLDKRKVD--EDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARS-LIYRPAI------LLADEPTGNLD 173
Cdd:PRK03695 90 LTL-HQPDKTRTEavASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-220 |
1.45e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.12 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeISSLKEEAlavfrrrkvgliyqfynLIPTLDV 102
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-IAYVPQQA-----------------WIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILlpmLLDKRkvDEDRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRVSIARSLIYRPAILLADEPTGN 171
Cdd:PTZ00243 738 RGNIL---FFDEE--DAARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497574098 172 LDRKNSEEIVDLLNLSNKRfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PTZ00243 813 LDAHVGERVVEECFLGALA-GKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-185 |
2.96e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTkIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDR-PTSGKIYVEDTEIS-SLKEEAL 79
Cdd:PRK13549 258 VILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKiRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 80 A-----VFRRRKVgliyqfYNLIPTLDVRKNILLPMLldkrkvdeDRFS---------EIVSILGLSDRLN------HLP 139
Cdd:PRK13549 337 AqgiamVPEDRKR------DGIVPVMGVGKNITLAAL--------DRFTggsriddaaELKTILESIQRLKvktaspELA 402
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 140 -SQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN 185
Cdd:PRK13549 403 iARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-221 |
3.51e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSnqtrVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIY-----VEDTEISSlkeealav 81
Cdd:NF033858 270 RGLTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIAT-------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frRRKVGLIYQFYNLIPTLDVRKNILL-------PMLLDKRKVDE--DRFseivsilGLSDRLNHLPSQLSGGQQQRVSI 152
Cdd:NF033858 338 --RRRVGYMSQAFSLYGELTVRQNLELharlfhlPAAEIAARVAEmlERF-------DLADVADALPDSLPLGIRQRLSL 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 153 ARSLIYRPAILLADEPTGNLD---RKNSEEIvdLLNLSNKRfNQTILLITH--DEkiALEANRIVTMEDG-VIVS 221
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDpvaRDMFWRL--LIELSRED-GVTIFISTHfmNE--AERCDRISLMHAGrVLAS 478
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-202 |
1.08e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.28 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIsslkEEALAVFrRRKVGLIYQFYNLIPTLDV 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTY-QKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMLLDKRKVDEDrfsEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVD 182
Cdd:PRK13540 92 RENCLYDIHFSPGAVGIT---ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|
gi 497574098 183 LLNLSNKRfNQTILLITHDE 202
Cdd:PRK13540 169 KIQEHRAK-GGAVLLTSHQD 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-226 |
1.09e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdrptsgkIYVEDT-EISSLKEEalAVFRRRK------VGLIYQ 92
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG--------IYTRDAgSILYLGKE--VTFNGPKssqeagIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 93 FYNLIPTLDVRKNILL------PM-LLDKRKVDEDRfSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLA 165
Cdd:PRK10762 87 ELNLIPQLTIAENIFLgrefvnRFgRIDWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 166 DEPTgnlDRKNSEEIVDLLNLSNKRFNQT--ILLITHDEKIALE-ANRIVTMEDGVIVSEKVVK 226
Cdd:PRK10762 166 DEPT---DALTDTETESLFRVIRELKSQGrgIVYISHRLKEIFEiCDDVTVFRDGQFIAEREVA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-222 |
2.02e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLK-EEALAVfrrrkvGLIY-----QFYNL 96
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLAN------GIVYisedrKRDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTLDVRKNILLPML--LDKRKVDEDRFSEIVSILGLSDRLN-HLPSQ------LSGGQQQRVSIARSLIYRPAILLADE 167
Cdd:PRK10762 342 VLGMSVKENMSLTALryFSRAGGSLKHADEQQAVSDFIRLFNiKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 168 PTGNLDRKNSEEIVDLLNlsnkRFNQ---TILLITHD--EKIALeANRIVTMEDGVIVSE 222
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLIN----QFKAeglSIILVSSEmpEVLGM-SDRILVMHEGRISGE 476
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-217 |
2.46e-13 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 67.57 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYvedteisslkeealavfRRRKVGLIYQFYNLIPTlDV 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------------HSGRISFSSQFSWIMPG-TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMlldkrKVDEDRFSEIVSILGLSDRLNHLPSQ-----------LSGGQQQRVSIARSlIYRPAIL-LADEPTG 170
Cdd:cd03291 115 KENIIFGV-----SYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARA-VYKDADLyLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 171 NLDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:cd03291 189 YLDVFTEKEIFESC-VCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-222 |
2.50e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 26 VNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVeDTEISSLKEEALAVFR--------RRKVGliyqfynLI 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL-DGKPIDIRSPRDAIRAgimlcpedRKAEG-------II 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 PTLDVRKNI---------LLPMLLDKRKVDE--DRFSEIVSILGLSDRlnHLPSQLSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:PRK11288 344 PVHSVADNInisarrhhlRAGCLINNRWEAEnaDRFIRSLNIKTPSRE--QLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 167 EPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITHD--EKIALeANRIVTMEDGVIVSE 222
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIyELAAQ--GVAVLFVSSDlpEVLGV-ADRIVVMREGRIAGE 477
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-217 |
2.85e-13 |
|
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: 68.31 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSNqTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLH-LLGGVDRPTSGKIYVEDTEISsLKEEALA 80
Cdd:TIGR02633 256 VILEARNLTCWDVIN-PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD-IRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 81 VfrRRKVGLI---YQFYNLIPTLDVRKNILLPML---LDKRKVDEDRFSEIV--SILGLSDRLNH--LP-SQLSGGQQQR 149
Cdd:TIGR02633 334 I--RAGIAMVpedRKRHGIVPILGVGKNITLSVLksfCFKMRIDAAAELQIIgsAIQRLKVKTASpfLPiGRLSGGNQQK 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-218 |
4.79e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteisslkeealavfrrRKVGLIY---QFYNLIPT 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------------KHSGRISfspQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 lDVRKNILLPMlldkrKVDEDRFSEIVSILGLSDRLNHLPSQ-----------LSGGQQQRVSIARSLIYRPAILLADEP 168
Cdd:TIGR01271 502 -TIKDNIIFGL-----SYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 169 TGNLDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALEANRIVTMEDGV 218
Cdd:TIGR01271 576 FTHLDVVTEKEIFESC-LCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-219 |
5.63e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKI----------YVEDTEiss 73
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyYAQDHA--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 74 lkeealavfrrrkvgliYQFYNLIPTLDvrknillpmLLDKRKVDEDRFSEIVSILGL----SDRLNHLPSQLSGGQQQR 149
Cdd:PRK15064 393 -----------------YDFENDLTLFD---------WMSQWRQEGDDEQAVRGTLGRllfsQDDIKKSVKVLSGGEKGR 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLDRknseEIVDLLNLSNKRFNQTILLITHD-EKIALEANRIVTM-EDGVI 219
Cdd:PRK15064 447 MLFGKLMMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDrEFVSSLATRIIEItPDGVV 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
6.51e-13 |
|
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: 67.28 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLH-LLGGVDRpTSGKIYVEDTeISSLKEEALavfrrrkvgliyqfynlIPTLD 101
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-VAYVPQQAW-----------------IQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 102 VRKNILLpmlldKRKVDEDRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:TIGR00957 715 LRENILF-----GKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497574098 171 NLDRKNSEEIVD-LLNLSNKRFNQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:TIGR00957 790 AVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-201 |
1.13e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.12 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 15 SNQTRVTALNNVNLSVQKGDF-----VSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISslkeealavfrrrkvgl 89
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 90 iYQFYNLIPTLDVRKNILLpMLLDKRKVDEDRF-SEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEP 168
Cdd:cd03237 65 -YKPQYIKADYEGTVRDLL-SSITKDFYTHPYFkTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 497574098 169 TGNLDrknSEEIVdLLNLSNKRF----NQTILLITHD 201
Cdd:cd03237 143 SAYLD---VEQRL-MASKVIRRFaennEKTAFVVEHD 175
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
21-201 |
1.61e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQFYNLIPTL 100
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNI-LLPMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEE 179
Cdd:PRK15056 101 VMMGRYgHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180
....*....|....*....|...
gi 497574098 180 IVDLL-NLSNKrfNQTILLITHD 201
Cdd:PRK15056 181 IISLLrELRDE--GKTMLVSTHN 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
5-216 |
1.64e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.21 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 5 KCENLTKIYGSN-----QTR--VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEisSLKEE 77
Cdd:PTZ00265 376 KLKDIKKIQFKNvrfhyDTRkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 ALAvFRRRKVGLI----------------YQFYNL--------------------------------------IPTLDvr 103
Cdd:PTZ00265 454 NLK-WWRSKIGVVsqdpllfsnsiknnikYSLYSLkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTD-- 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 104 KNILLPMLLDKRKVDEdrfSEIVSI---LGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYRPAILLADEPT 169
Cdd:PTZ00265 531 SNELIEMRKNYQTIKD---SEVVDVskkVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEAT 607
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 497574098 170 GNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALEANRIVTMED 216
Cdd:PTZ00265 608 SSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-227 |
1.78e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIS-SLKEEALavfrRRKVGLIYQFYNLIP 98
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEAL----ENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 99 TLDVRKNILL------PMLLDKRKVDEDRfSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNL 172
Cdd:PRK10982 87 QRSVMDNMWLgryptkGMFVDQDKMYRDT-KAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 173 DRKNSEEIVDLLNLSNKRfNQTILLITHD-EKIALEANRIVTMEDGVIVSEKVVKK 227
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKER-GCGIVYISHKmEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-173 |
7.09e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.48 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 14 GSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdRPTSGkiYVE-DTEISSL--KEEALAvfrrRKVGLI 90
Cdd:PLN03140 887 GVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEgDIRISGFpkKQETFA----RISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 91 YQFYNLIPTLDVRKNIL------LPMLLDKRK----VDEdrFSEIVSILGLSDRLNHLP--SQLSGGQQQRVSIARSLIY 158
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIysaflrLPKEVSKEEkmmfVDE--VMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170
....*....|....*
gi 497574098 159 RPAILLADEPTGNLD 173
Cdd:PLN03140 1037 NPSIIFMDEPTSGLD 1051
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-173 |
8.88e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 30 VQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVeDTEISSLKEealavfRRRKVGLIYQFYNLIPTLDVRKNILLP 109
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGD------RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 110 MLLDKRKVDEDRfSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARsLIYRPAIL-LADEPTGNLD 173
Cdd:PRK13543 107 CGLHGRRAKQMP-GSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLD 169
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-222 |
1.43e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdrptsgkiyvedtEISSLkeEALAVFRRRKVGLIYQFyNLIPTLDV 102
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHA--ETSSVVIRGSVAYVPQV-SWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLpmlldKRKVDEDRFSEIVSILGLSDRLNHLPSQ-----------LSGGQQQRVSIARSLIYRPAILLADEPTGN 171
Cdd:PLN03232 696 RENILF-----GSDFESERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 172 LDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PLN03232 771 LDAHVAHQVFDSC-MKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-222 |
1.57e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVedteisslkeealavfRRRKVGLIYQFyNLIPTLDV 102
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----------------IRGTVAYVPQV-SWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMlldkrKVDEDRFSEIVSILGLSDRLNHLPS-----------QLSGGQQQRVSIARSLIYRPAILLADEPTGN 171
Cdd:PLN03130 696 RDNILFGS-----PFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 172 LDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIALEANRIVTMEDGVIVSE 222
Cdd:PLN03130 771 LDAHVGRQVFDKC-IKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-217 |
2.48e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdRPTSGkiYVEDTEISSLKEEALAVFRRRkVGLIYQFYNLIPTLDV 102
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTG--VITGGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMLLDK----RKVDEDRFSE-IVSILGL---SDRLNHLPSQ-LSGGQQQRVSIARSLIYRPAILL-ADEPTGNL 172
Cdd:TIGR00956 854 RESLRFSAYLRQpksvSKSEKMEYVEeVIKLLEMesyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497574098 173 DRKNSEEIVDLL-NLSNKrfNQTILLITHDEKIAL--EANRIVTMEDG 217
Cdd:TIGR00956 934 DSQTAWSICKLMrKLADH--GQAILCTIHQPSAILfeEFDRLLLLQKG 979
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-220 |
2.83e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.46 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTL-LHLLGGVDRpTSGKIYVEDTEISSLKEEALavf 82
Cdd:cd03288 20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rRRKVGLIYQfynlIPTL---DVRKNillpmLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQL-----------SGGQQQ 148
Cdd:cd03288 94 -RSRLSIILQ----DPILfsgSIRFN-----LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKnSEEIVDLLNLSnKRFNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMT-AFADRTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-173 |
3.11e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslkeealavf 82
Cdd:TIGR03719 322 VIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrrkVGLIY--QFYNlipTLDVRKNI-------LLPMLLDKRKVDE----DRFSeivsiLGLSDRlNHLPSQLSGGQQQR 149
Cdd:TIGR03719 385 ----VKLAYvdQSRD---ALDPNKTVweeisggLDIIKLGKREIPSrayvGRFN-----FKGSDQ-QKKVGQLSGGERNR 451
|
170 180
....*....|....*....|....
gi 497574098 150 VSIARSLIYRPAILLADEPTGNLD 173
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-217 |
3.35e-11 |
|
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: 62.34 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 2 EILKCENLTKIYGSnqTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEAlav 81
Cdd:TIGR01257 1936 DILRLNELTKVYSG--TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 frRRKVGLIYQFYNLIPTLDVRKNILLPMLLdkRKVDEDRFSEI----VSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:TIGR01257 2011 --HQNMGYCPQFDAIDDLLTGREHLYLYARL--RGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574098 158 YRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD-EKIALEANRIVTMEDG 217
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTI-VSIIREGRAVVLTSHSmEECEALCTRLAIMVKG 2146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-222 |
4.49e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvDRPTS---------GKIYVEDTEISSLKEEALAvfRRRKVgLIYQF 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLA--RLRAV-LPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 YNLIPtLDVRKNILLPMLLDKRKV------DEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSL---------IY 158
Cdd:PRK13547 93 QPAFA-FSAREIVLLGRYPHARRAgalthrDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 159 RPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKIALE-ANRIVTMEDGVIVSE 222
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAH 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-169 |
7.59e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGsnqtRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSlkeealAVFRRRK 86
Cdd:NF033858 5 EGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYqfY-------NLIPTLDVRKNI-----LLPmlLDKRkvdeDRFSEIVSIL---GLSDRLNHLPSQLSGGQQQRVS 151
Cdd:NF033858 75 CPRIA--YmpqglgkNLYPTLSVFENLdffgrLFG--QDAA----ERRRRIDELLratGLAPFADRPAGKLSGGMKQKLG 146
|
170
....*....|....*...
gi 497574098 152 IARSLIYRPAILLADEPT 169
Cdd:NF033858 147 LCCALIHDPDLLILDEPT 164
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-220 |
1.05e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTrvtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvdRP----TSGKIYVEDTEISSLKEEA 78
Cdd:CHL00131 7 ILEIKNLHASVNENEI----LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 79 LAvfrRRKVGLIYQFYNLIPTLDvrkNILLPML--------LDKRKVDEDRFSEIVS----ILGLSDRLNH--LPSQLSG 144
Cdd:CHL00131 81 RA---HLGIFLAFQYPIEIPGVS---NADFLRLaynskrkfQGLPELDPLEFLEIINeklkLVGMDPSFLSrnVNEGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 145 GQQQRVSIARSLIYRPAILLADEPTGNLD----RKNSEEIVDLLNLSNkrfnqTILLITHDEKIaLE---ANRIVTMEDG 217
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDidalKIIAEGINKLMTSEN-----SIILITHYQRL-LDyikPDYVHVMQNG 228
|
...
gi 497574098 218 VIV 220
Cdd:CHL00131 229 KII 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-201 |
1.22e-10 |
|
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: 59.30 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 33 GDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVE---DTEISSLKEEALAVFRRR------KVGLIYQFYNLIPTlDVR 103
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwDEILDEFRGSELQNYFTKllegdvKVIVKPQYVDLIPK-AVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 104 KNILLpmlLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD---RKNSEEI 180
Cdd:cd03236 105 GKVGE---LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAARL 181
|
170 180
....*....|....*....|.
gi 497574098 181 VDLLNLSNKrfnqTILLITHD 201
Cdd:cd03236 182 IRELAEDDN----YVLVVEHD 198
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-219 |
2.38e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVgliyqfyNLIPTLDV 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKI-------TIIPQDPV 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 RKNILLPMLLD--KRKVDED--------RFSEIVSilGLSDRLNHLPSQ----LSGGQQQRVSIARSLIYRPAILLADEP 168
Cdd:TIGR00957 1371 LFSGSLRMNLDpfSQYSDEEvwwalelaHLKTFVS--ALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497574098 169 TGNLDRKNSEEIVDLLnlsNKRFNQ-TILLITHDEKIALEANRIVTMEDGVI 219
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTI---RTQFEDcTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-176 |
2.54e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGvDRPTSgkiYVEDteisslkeeaLAVF-RRRKVG-LIYQFYNLIPT- 99
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG---YSND----------LTLFgRRRGSGeTIWDIKKHIGYv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 100 -----LDVR-----KNILLPMLLDK----RKV-DEDRF--SEIVSILGLSDRLNHLPSQ-LSGGQQQRVSIARSLIYRPA 161
Cdd:PRK10938 342 ssslhLDYRvstsvRNVILSGFFDSigiyQAVsDRQQKlaQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPT 421
|
170
....*....|....*
gi 497574098 162 ILLADEPTGNLDRKN 176
Cdd:PRK10938 422 LLILDEPLQGLDPLN 436
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-216 |
3.03e-10 |
|
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: 57.16 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 4 LKCENLTKIYGSNQTRVtalNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteISSLKEEALAVFR 83
Cdd:cd03223 1 IELENLSLATPDGRVLL---KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 84 RRKvgliyqfynlIPTLDVRKNILLPmlLDKRkvdedrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPAIL 163
Cdd:cd03223 72 RPY----------LPLGTLREQLIYP--WDDV--------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLnlsnKRFNQTILLITHDEKIALEANRIVTMED 216
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-217 |
4.40e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIygsNQTrvtALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEE----- 77
Cdd:PRK10982 250 ILEVRNLTSL---RQP---SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainh 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 78 --ALAVFRRRKVGlIY-----QFYNLIPTLDVRKNILlpMLLDKRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRV 150
Cdd:PRK10982 324 gfALVTEERRSTG-IYayldiGFNSLISNIRNYKNKV--GLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGSLSGGNQQKV 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLN-LSNKrfNQTILLITHDEKIALE-ANRIVTMEDG 217
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAeLAKK--DKGIIIISSEMPELLGiTDRILVMSNG 467
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-201 |
4.57e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTK---IYGSNQTRVT-------------ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyVEDTE 70
Cdd:PRK13546 8 KNVTKeyrIYRTNKERMKdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-DRNGE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 71 ISSLKEEAlavfrrrkvGLIYQFYNLiptldvrKNILLPMLLD--KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQ 148
Cdd:PRK13546 87 VSVIAISA---------GLSGQLTGI-------ENIEFKMLCMgfKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHD 201
Cdd:PRK13546 151 KLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI-YEFKEQNKTIFFVSHN 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-214 |
4.91e-10 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 57.27 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTLL---------------------HLLGGVDRPTSGKIyvedTEIS---SL 74
Cdd:cd03270 7 REHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSI----EGLSpaiAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 75 KEEALAVFRRRKVGLIYQFYNLIPTLDVRKNIL--LPMLLDkrkvdedrfseivsiLGLSD-RLNHLPSQLSGGQQQRVS 151
Cdd:cd03270 83 DQKTTSRNPRSTVGTVTEIYDYLRLLFARVGIRerLGFLVD---------------VGLGYlTLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 152 IARSL-------IYrpaILlaDEPTGNLDRKNSEEIVDLL----NLSNkrfnqTILLITHDEKIALEANRIVTM 214
Cdd:cd03270 148 LATQIgsgltgvLY---VL--DEPSIGLHPRDNDRLIETLkrlrDLGN-----TVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-222 |
4.95e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 24 NNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEIS------SLKEE-ALAVFRRRKVGliyqfynL 96
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKGmAYITESRRDNG-------F 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IPTLDVRKNI-LLPMLLDKR---------KVDEDRFSE----IVSILGLSdrLNHLPSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:PRK09700 353 FPNFSIAQNMaISRSLKDGGykgamglfhEVDEQRTAEnqreLLALKCHS--VNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 163 LLADEPTGNLDRKNSEEIVDLL-NLSNKrfNQTILLITHD--EKIALeANRIVTMEDGVIVSE 222
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMrQLADD--GKVILMVSSElpEIITV-CDRIAVFCEGRLTQI 490
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-201 |
1.03e-09 |
|
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: 57.87 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 31 QKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyveDTEISslKEEALAVFR--------------RRKVGLIYQFYNL 96
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPS--WDEVLKRFRgtelqdyfkklangEIKVAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 97 IP---TLDVRKnillpmLLdkRKVDE-DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNL 172
Cdd:COG1245 172 IPkvfKGTVRE------LL--EKVDErGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 497574098 173 D---RKNSEEIVDllNLSNKrfNQTILLITHD 201
Cdd:COG1245 244 DiyqRLNVARLIR--ELAEE--GKYVLVVEHD 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-173 |
2.03e-09 |
|
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: 56.72 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 29 SVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYvEDTEISslkeealavfrrrkvgliY--QFYNLIPTLDVRKNI 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIS------------------YkpQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 107 llpmlldkRKVDEDRF------SEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIyRPA-ILLADEPTGNLD 173
Cdd:COG1245 423 --------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS-RDAdLYLLDEPSAHLD 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-201 |
3.82e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 21 TALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVedteisSLKEEaLAVFRRRKVgliyqfynlipTL 100
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC------GTKLE-VAYFDQHRA-----------EL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DVRKNILLPMLLDKRKVD---EDRfseivSILG-LSDRLNHlPSQ-------LSGGQQQRVSIARsLIYRPAILLA-DEP 168
Cdd:PRK11147 395 DPEKTVMDNLAEGKQEVMvngRPR-----HVLGyLQDFLFH-PKRamtpvkaLSGGERNRLLLAR-LFLKPSNLLIlDEP 467
|
170 180 190
....*....|....*....|....*....|...
gi 497574098 169 TGNLDRKNSEEIVDLLNlsnkRFNQTILLITHD 201
Cdd:PRK11147 468 TNDLDVETLELLEELLD----SYQGTVLLVSHD 496
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-214 |
3.92e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.25 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 16 NQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLhllggvdrptSGKIYvedTEISSLKEEALAVFRRRKVGLIYQFYN 95
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLY---ASGKARLISFLPKFSRNKLIFIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 96 LIptlDVRKNILlpmlldkrkvdedrfseivsilglsdRLNHLPSQLSGGQQQRVSIARSLIYRP--AILLADEPTGNLD 173
Cdd:cd03238 71 LI---DVGLGYL--------------------------TLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497574098 174 ----RKNSEEIVDLLNLSNkrfnqTILLITHDEKIALEANRIVTM 214
Cdd:cd03238 122 qqdiNQLLEVIKGLIDLGN-----TVILIEHNLDVLSSADWIIDF 161
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-200 |
3.97e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 22 ALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDT----EISSlkeealavfrrrkvGLIYQFYNLi 97
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaaliAISS--------------GLNGQLTGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 98 ptldvrKNILLP---MLLDKRKVDEdRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDR 174
Cdd:PRK13545 104 ------ENIELKglmMGLTKEKIKE-IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180
....*....|....*....|....*.
gi 497574098 175 KNSEEIVDLLNlSNKRFNQTILLITH 200
Cdd:PRK13545 177 TFTKKCLDKMN-EFKEQGKTIFFISH 201
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-181 |
5.13e-09 |
|
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: 54.19 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTRVTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdrpTSGKIYVEdTEISSLKEEALAVFRRRKV 87
Cdd:cd03233 8 NISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVE-GDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 88 GLIY--QFYNLIPTLDVRKNIllpmlldkrkvdedRFSeivsilgLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLA 165
Cdd:cd03233 84 EIIYvsEEDVHFPTLTVRETL--------------DFA-------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170
....*....|....*.
gi 497574098 166 DEPTGNLDRKNSEEIV 181
Cdd:cd03233 143 DNSTRGLDSSTALEIL 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-173 |
5.31e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 30 VQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslKEEALAVFRrrkvGLIYQ--FYNLiptldVRKNI- 106
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPS-----WDEVLKRFR----GTELQnyFKKL-----YNGEIk 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 107 ---------LLPMLLDK------RKVDE-DRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTG 170
Cdd:PRK13409 162 vvhkpqyvdLIPKVFKGkvrellKKVDErGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
...
gi 497574098 171 NLD 173
Cdd:PRK13409 242 YLD 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-216 |
5.51e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 5.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574098 142 LSGGQQQRVSIARSLIYRPAILLADEPTGNLDrKNSEEIVD--LLNLSNKRfNQTILLITHDEKIALEANRIVTMED 216
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEktIVDIKDKA-DKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-217 |
1.39e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.70 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 8 NLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLH-LLGGVDrpTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:cd03289 7 DLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVPLQKW----RKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYnLIPTLDVRKNillpmlLDKR-KVDEDRFSEIVSILGLSDRLNHLPSQL-----------SGGQQQRVSIAR 154
Cdd:cd03289 79 FGVIPQKV-FIFSGTFRKN------LDPYgKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497574098 155 SLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDG 217
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-201 |
1.48e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 18 TRVTaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGG--------------------------VDRPTSGKIYVEDTEI 71
Cdd:PRK10636 13 VRVL-LDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsytfpgnwqlawvnqetpaLPQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 72 SSLkEEALAVFRRRKVGliyqfyNLIPTLDVRKNILLPMLLDKRKvdedrfSEIVSILGLS-DRLNHLPSQLSGGQQQRV 150
Cdd:PRK10636 92 RQL-EAQLHDANERNDG------HAIATIHGKLDAIDAWTIRSRA------ASLLHGLGFSnEQLERPVSDFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497574098 151 SIARSLIYRPAILLADEPTGNLDRknseEIVDLLNLSNKRFNQTILLITHD 201
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHD 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-215 |
1.77e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVtaLNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVdRPTSGKIYVEDTEISSLKEEALavfrRRK 86
Cdd:TIGR01271 1221 QGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTW----RKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIYQFYnLIPTLDVRKNillpmlLD--KRKVDEDRFsEIVSILGLSDRLNHLPSQL-----------SGGQQQRVSIA 153
Cdd:TIGR01271 1294 FGVIPQKV-FIFSGTFRKN------LDpyEQWSDEEIW-KVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 154 RSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTME 215
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLECQQFLVIE 1425
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-173 |
2.73e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNQTRVTALnnvnlSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyVEDTEISslkeealavf 82
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVEGG-----EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKIS---------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrrkvgliYQFYNLIPTLDVRKNILLpmlldkRKVDED-----RFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLI 157
Cdd:PRK13409 404 --------YKPQYIKPDYDGTVEDLL------RSITDDlgssyYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
170
....*....|....*..
gi 497574098 158 yRPA-ILLADEPTGNLD 173
Cdd:PRK13409 470 -RDAdLYLLDEPSAHLD 485
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-220 |
2.88e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQF--------- 93
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQSpvlfsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 YNLIPTLDVRKNILLPMLldKRKVDEDRFSEivSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PLN03232 1328 FNIDPFSEHNDADLWEAL--ERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 174 RKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PLN03232 1404 VRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
20-227 |
2.91e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 20 VTALNNVNLSVQKGDFVSIVGASGSG--KSTLLHLLGGVD---RPTSGKIYVEDTEisSLKEeALAVFRRRKVGLIYQFY 94
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrRPWRF*TWCANRR--ALRR-TIG*HRPVR*GRRESFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 95 NliptldvRKNI-LLPMLLD-KRKVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNL 172
Cdd:NF000106 103 G-------RENLyMIGR*LDlSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 173 DRKNSEEIVDLLNlSNKRFNQTILLIT-HDEKIALEANRIVTMEDGVIVSEKVVKK 227
Cdd:NF000106 176 DPRTRNEVWDEVR-SMVRDGATVLLTTqYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-214 |
4.04e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 4.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574098 141 QLSGGQQQRVSIA-----RSLIYRPAILLaDEPTGNLDRKNSEEIVDLLNLSNKRFNQTIlLITHDEKIALEANRIVTM 214
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVI-VITHLPELAELADKLIHI 153
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-222 |
1.85e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGG--VDRPTSGKIYVEDTEI--SSLKEE-----ALAVFRRRKVGLiyqf 93
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVdvSTVSDAidaglAYVTEDRKGYGL---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 94 yNLIPtlDVRKNILLPML--LDKRKV-DEDRfsEIVSILGLSDRLN-HLPS------QLSGGQQQRVSIARSLIYRPAIL 163
Cdd:NF040905 352 -NLID--DIKRNITLANLgkVSRRGViDENE--EIKVAEEYRKKMNiKTPSvfqkvgNLSGGNQQKVVLSKWLFTDPDVL 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574098 164 LADEPTGNLDRKNSEEIVDLLN-LSNKrfNQTILLITHD--EKIALeANRIVTMEDGVIVSE 222
Cdd:NF040905 427 ILDEPTRGIDVGAKYEIYTIINeLAAE--GKGVIVISSElpELLGM-CDRIYVMNEGRITGE 485
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-185 |
2.06e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTkiYGSNQTRVTALNnvnLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKeealavf 82
Cdd:PRK13541 1 MLSLHQLQ--FNIEQKNLFDLS---ITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrrKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIvSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAI 162
Cdd:PRK13541 69 ---KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAI-HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180
....*....|....*....|...
gi 497574098 163 LLADEPTGNLDRKNSeeivDLLN 185
Cdd:PRK13541 145 WLLDEVETNLSKENR----DLLN 163
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-173 |
2.15e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTeisslkeealavfrrrk 86
Cdd:PRK11819 328 ENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET----------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 VGLIY--QFYNlipTLDVRKNIllpmlldkrkvdedrFSEIvsilglSDRLNHL-------PS----------------- 140
Cdd:PRK11819 387 VKLAYvdQSRD---ALDPNKTV---------------WEEI------SGGLDIIkvgnreiPSrayvgrfnfkggdqqkk 442
|
170 180 190
....*....|....*....|....*....|....*
gi 497574098 141 --QLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PRK11819 443 vgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-220 |
2.81e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISSLKEEALavfrRRKVGLIYQfynlIPTL-- 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQ----APVLfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 -DVRKNIllpmlldkrkvdeDRFSE-----------------IV--SILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRP 160
Cdd:PLN03130 1327 gTVRFNL-------------DPFNEhndadlweslerahlkdVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 161 AILLADEPTGNLDRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEANRIVTMEDGVIV 220
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFK--SCTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-201 |
4.20e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 27 NLSVQ--KGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTE-ISSLKEEALAvfrrrkvgliYQFYNLIPTLDV- 102
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErLGKLRQDQFA----------FEEFTVLDTVIMg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 103 ----------RKNIL-LPMLL--DKRKVD--------------EDRFSEIVSILGLSDRLNHLP-SQLSGGQQQRVSIAR 154
Cdd:PRK15064 89 htelwevkqeRDRIYaLPEMSeeDGMKVAdlevkfaemdgytaEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497574098 155 SLIYRPAILLADEPTGNLDrKNSeeIVDLLNLSNKRfNQTILLITHD 201
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLD-INT--IRWLEDVLNER-NSTMIIISHD 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-173 |
4.78e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 3 ILKCENLTKIYGSNqtrvTALNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteisslkeeALAvf 82
Cdd:PRK10636 312 LLKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLA-- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 rrRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIVSILGLS-DRLNHLPSQLSGGQQQRVSIARSLIYRPA 161
Cdd:PRK10636 373 --KGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170
....*....|..
gi 497574098 162 ILLADEPTGNLD 173
Cdd:PRK10636 451 LLLLDEPTNHLD 462
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-203 |
7.44e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 7.44e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 141 QLSGGQQqrvsIARSLIYRPA----------ILLADEPTGNLDRKNSEE-IVDLLNLSNKRFNQTILLITHDEK 203
Cdd:cd03240 115 RCSGGEK----VLASLIIRLAlaetfgsncgILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHDEE 184
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-219 |
1.75e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVEDTEISS--LKEealavFRRrkvgliyQFyNLIPTl 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAygLRE-----LRR-------QF-SMIPQ- 1391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 101 DvrknillPMLLDKR-KVDEDRFSEIVS--------ILGLSDRLNHLP-----------SQLSGGQQQRVSIARSLIYR- 159
Cdd:PTZ00243 1392 D-------PVLFDGTvRQNVDPFLEASSaevwaaleLVGLRERVASESegidsrvleggSNYSVGQRQLMCMARALLKKg 1464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574098 160 PAILLADEPTGN----LDRKNSEEIVDLLNlsnkrfNQTILLITHDEKIALEANRIVTMEDGVI 219
Cdd:PTZ00243 1465 SGFILMDEATANidpaLDRQIQATVMSAFS------AYTVITIAHRLHTVAQYDKIIVMDHGAV 1522
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-220 |
9.03e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 9 LTKIYGSNQTR-VTALNNVNLSVQKGDFVSIVGASGSGKSTLLhllggvdRPTSGKIY----VEDTEIS--SLKEEALAV 81
Cdd:TIGR00956 62 FRKLKKFRDTKtFDILKPMDGLIKPGELTVVLGRPGSGCSTLL-------KTIASNTDgfhiGVEGVITydGITPEEIKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 82 FRRRKVGLIYQFYNLIPTLDVRKNI----------LLPMLLDKRKVDEDRFSEIVSILGLSDRL-----NHLPSQLSGGQ 146
Cdd:TIGR00956 135 HYRGDVVYNAETDVHFPHLTVGETLdfaarcktpqNRPDGVSREEYAKHIADVYMATYGLSHTRntkvgNDFVRGVSGGE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 147 QQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHD--EKIALEANRIVTMEDGVIV 220
Cdd:TIGR00956 215 RKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQcsQDAYELFDKVIVLYEGYQI 290
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-209 |
9.22e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 32 KGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIYVedteisslkeealavfrrrkvgliyqfynliptldvrknillpml 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 112 ldkrkVDEDRFSEIVSILGLSDRLNHLPSQLSGGQQQRVSIARSLIYRPAILLADEPTGNLDRKNSEEIVDLLNL----- 186
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllll 110
|
170 180
....*....|....*....|...
gi 497574098 187 SNKRFNQTILLITHDEKIALEAN 209
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPAL 133
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
119-173 |
1.69e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 497574098 119 EDRFSEIVSILGLSDRLNHLPS-QLSGGQQQRVSIARSLIYRPAILLADEPTGNLD 173
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-201 |
1.87e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 7 ENLTKIYGSNQTRVTALNnvnlsVQKGDFVSIVGASGSGKSTLLHLLGGVDRPTSGKIyvedteisslkeealavfrrrk 86
Cdd:cd03222 4 PDCVKRYGVFFLLVELGV-----VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 87 vgliyqfynlipTLDVRKNILLPMLLDkrkvdedrfseivsilglsdrlnhlpsqLSGGQQQRVSIARSLIYRPAILLAD 166
Cdd:cd03222 57 ------------EWDGITPVYKPQYID----------------------------LSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190
....*....|....*....|....*....|....*...
gi 497574098 167 EPTGNLD---RKNSEEIVDLLNLSNKRfnqTILLITHD 201
Cdd:cd03222 97 EPSAYLDieqRLNAARAIRRLSEEGKK---TALVVEHD 131
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
23-51 |
4.45e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.45e-04
10 20
....*....|....*....|....*....
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLH 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
23-51 |
1.67e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.67e-03
10 20
....*....|....*....|....*....
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLH 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-212 |
1.82e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 1.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574098 142 LSGGQQQRVSIAR----SLIYRPAILlaDEPTGNLDRKNSEEIVDLLNLSNKRFNqTILLITHDEKIALEANRIV 212
Cdd:PRK00635 477 LSGGEQERTALAKhlgaELIGITYIL--DEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMISLADRII 548
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-51 |
1.91e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.36 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|...
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTLLH 51
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-215 |
2.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 139 PSQLSGGQQQRVSIA-RSLIYR-------------PAILlaDEPTGNLDRKNSEEIVDLLNLSNKRFNQTILLITHDEKI 204
Cdd:PRK02224 779 PEQLSGGERALFNLSlRCAIYRllaegiegdaplpPLIL--DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDEL 856
|
90
....*....|.
gi 497574098 205 ALEANRIVTME 215
Cdd:PRK02224 857 VGAADDLVRVE 867
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
74-214 |
2.77e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 74 LKEEALAV---------FRRRKVGLIYQFYNLIPTLDVRKNILLPMLldkrkvdedrfSEIVSILG-LSD------RLNH 137
Cdd:TIGR00630 416 LKPEALAVtvggksiadVSELSIREAHEFFNQLTLTPEEKKIAEEVL-----------KEIRERLGfLIDvgldylSLSR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 138 LPSQLSGGQQQRVSIARSL-------IYrpaILlaDEPTGNL-DRKNSEEIVDLLNLSNKrfNQTILLITHDEKIALEAN 209
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIgsgltgvLY---VL--DEPSIGLhQRDNRRLINTLKRLRDL--GNTLIVVEHDEDTIRAAD 557
|
....*
gi 497574098 210 RIVTM 214
Cdd:TIGR00630 558 YVIDI 562
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
149-204 |
4.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.10 E-value: 4.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 149 RVSIARSLIYRPAILLADEPTGNLDRKNSEE----IVDLLNLSNKRFNQTILLITHDEKI 204
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVITHDEDF 1272
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-51 |
4.54e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 4.54e-03
10 20
....*....|....*....|....*....
gi 497574098 23 LNNVNLSVQKGDFVSIVGASGSGKSTLLH 51
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
38-205 |
5.43e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.86 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 38 IVGASGSGKSTLLH-----LLGGVdrPTSGKIYVEDTEISSLKEEALAVFRRRKVGLIYQfynliptldVRKnillpmll 112
Cdd:cd03279 33 ICGPTGAGKSTILDaityaLYGKT--PRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKYR---------VER-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 113 dKRKVDEDRFSEIVsIL--GLSDRLNHLP-SQLSGGQQQRVSIA----------RSLIYRPAILLADEPTGNLDRKNSEE 179
Cdd:cd03279 94 -SRGLDYDQFTRIV-LLpqGEFDRFLARPvSTLSGGETFLASLSlalalsevlqNRGGARLEALFIDEGFGTLDPEALEA 171
|
170 180
....*....|....*....|....*.
gi 497574098 180 IVDLLNLSnKRFNQTILLITHDEKIA 205
Cdd:cd03279 172 VATALELI-RTENRMVGVISHVEELK 196
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-212 |
5.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 134 RLNHLP-----SQLSGGQQQRVSIARSLIY---RPAILLADEPTGNLDRKNSEEIVDLLnLSNKRFNQTILLITHDEKIA 205
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVL-QSLTHQGHTVVIIEHNMHVV 875
|
....*..
gi 497574098 206 LEANRIV 212
Cdd:PRK00635 876 KVADYVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-49 |
5.85e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|.
gi 497574098 19 RVTALNNVNLSVQKGDFVSIVGASGSGKSTL 49
Cdd:TIGR00630 8 REHNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
38-201 |
6.81e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 38 IVGASGSGKSTLLH-----LLGGVDRPTS----------------------GKIYV------EDTEISSLKEEAL--AVF 82
Cdd:COG0419 28 IVGPNGAGKSTILEairyaLYGKARSRSKlrsdlinvgseeasvelefehgGKRYRierrqgEFAEFLEAKPSERkeALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574098 83 RRRKVGLIYQFYNLIPTLDVRKNILLPMLLDKRKVDEDRFSEIvsiLGLSDrlnhlPSQLSGGQQQRVSIARSLiyrPAI 162
Cdd:COG0419 108 RLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQL---SGLDP-----IETLSGGERLRLALADLL---SLI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 497574098 163 LlaDepTGNLDRKNSEEIVDLLNlsnkrfnqTILLITHD 201
Cdd:COG0419 177 L--D--FGSLDEERLERLLDALE--------ELAIITHV 203
|
|
| |
