|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-222 |
6.14e-113 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 348.96 E-value: 6.14e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAyRYATRIVTLADGKITDDS 222
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELA-ARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-218 |
6.76e-108 |
|
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: 335.23 E-value: 6.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAyRYATRIVTLADGKI 218
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
5.20e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 251.16 E-value: 5.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwday 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDV--ARDRLVIMVTHNPELAYRYATRIVTLAD--GKITDD 221
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
1.34e-74 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 246.51 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVelaltLTG-VGH------------AERRQRARKALEAVGLGEHVDKRPSQLSGGQM 147
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTNV-----LAGrLGRtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 148 QRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
1.20e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 240.34 E-value: 1.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:COG2884 1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:COG2884 78 RR-RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTtVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.26e-71 |
|
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: 237.72 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDA- 79
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG---QDLFALDEDAr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 --YRNNRIGFVFQSYNLIPHQSILENVELALTLtgVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:COG4181 85 arLRARHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR---LVImVTHNPELAYRyATRIVTLADGKITDDS 222
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERgttLVL-VTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-213 |
5.73e-71 |
|
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: 235.44 E-value: 5.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwdayR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDRL--VIMVTHNPELAYRYATRIVTL 213
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGktVLLVTHDIDEAVFLADRVVVL 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-224 |
8.40e-69 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 230.27 E-value: 8.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkDFNDRDWDAY 80
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVELALTLT-GVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:COG1126 76 RR-KVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMtMVVVTHEMGFAREVADRVVFMDGGRIVEEGPP 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
3.78e-67 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.98 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRDWDA- 79
Cdd:COG3842 5 ALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTGl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 ---YRNnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARAL 156
Cdd:COG3842 73 ppeKRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 157 INDPEIVLADEPTGALDSTTSVQVMDLLKDVARdRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQR-ELgitFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-224 |
7.57e-67 |
|
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: 224.75 E-value: 7.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQSYNLIPHQS 99
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR-QIGMIFQQFNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELAL--------TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:cd03256 95 VLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 172 LDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:cd03256 175 LDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
1.69e-63 |
|
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: 214.31 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtQSftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDrdWDAYR 81
Cdd:cd03259 1 LELKGLSKTY--GS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG---RDVTG--VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03259 72 RN-IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-221 |
2.58e-62 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 212.36 E-value: 2.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAY 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG---RPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSY--NLIPHQSILENVELALTLTGVGhaERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALI 157
Cdd:COG1124 78 RR-RVQMVFQDPyaSLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-218 |
5.99e-62 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 215.01 E-value: 5.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtQSFTqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLidgistkdFNDRDWDAY- 80
Cdd:COG1118 3 IEVRNISKRF--GSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIV--------LNGRDLFTNl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 --RNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIN 158
Cdd:COG1118 71 ppRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 159 DPEIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
7.25e-62 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 214.56 E-value: 7.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDI-NRELgltIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
12-213 |
4.63e-61 |
|
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: 207.08 E-value: 4.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQ 90
Cdd:TIGR03608 4 ISKKFgDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:TIGR03608 84 NFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1469307064 171 ALDSTTSVQVMDLLKDVA-RDRLVIMVTHNPELAYRyATRIVTL 213
Cdd:TIGR03608 164 SLDPKNRDEVLDLLLELNdEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-218 |
1.22e-60 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 206.23 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkDFNDRDWDAYRNnRIGFVFQ 90
Cdd:cd03262 6 LHKSFgDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQ-KVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELAL-TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03262 84 QFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-224 |
1.49e-60 |
|
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: 206.80 E-value: 1.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayRNnRIGFVFQSYNlipHQ 98
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLREL---RR-KVGLVFQNPD---DQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 ----SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:COG1122 88 lfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 175 TTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG1122 168 RGRRELLELLKRLNKEGKtVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
3.95e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 207.23 E-value: 3.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFND---RDw 77
Cdd:COG3839 3 SLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDlppKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 78 dayRNnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:COG3839 75 ---RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARdRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHR-RLgttTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-218 |
9.48e-59 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 202.13 E-value: 9.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQ 90
Cdd:COG1127 11 LTKSFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRR-RIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALT-LTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:COG1127 90 GGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 170 GALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG1127 170 AGLDPITSAVIDELIREL-RDELgltSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-218 |
1.13e-58 |
|
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: 201.31 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDrdWDAYR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITN--LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03300 72 RP-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 162 IVLADEPTGALD----STTSVQVMDLLKDVARDrlVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03300 151 VLLLDEPLGALDlklrKDMQLELKRLQKELGIT--FVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-217 |
1.79e-58 |
|
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: 200.17 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGV---AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:TIGR02673 78 RR-RIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
2.25e-58 |
|
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: 200.42 E-value: 2.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfNDRDWDAY 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLK-LSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVFQ-SYN-LIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLG---EHVDKRPSQLSGGQMQRVAIARA 155
Cdd:cd03257 80 RRKEIQMVFQdPMSsLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDvARDRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKK-LQEELgltLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-224 |
2.32e-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: 210.14 E-value: 2.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDA 79
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 YRNnRIGFVFQSYN--LIPHQSILENVELALTLTGVG-HAERRQRARKALEAVGLG-EHVDKRPSQLSGGQMQRVAIARA 155
Cdd:COG1123 340 LRR-RVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-218 |
6.77e-58 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 199.34 E-value: 6.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
12-224 |
6.16e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.44 E-value: 6.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndRDWDAYRNnRIGFVFQ 90
Cdd:COG1131 6 LTKRYgDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVRR-RIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 171 ALDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG1131 161 GLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
6.23e-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: 196.75 E-value: 6.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYNLIPHQSILENV---ELAL-----TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAI 152
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVlhgRLGYkptwrSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 153 ARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVAR-DRLVIMVT-HNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKeDGITVIINlHQVDLAKKYADRIVGLKAGEIVFDGAP 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-266 |
1.04e-56 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 208.42 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVaRDR--LVIMVTHNPELAYRyATRIVTLADGKITDDSDPFDAAEAARREAKPT 238
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTEPVV 241
|
250 260 270
....*....|....*....|....*....|....
gi 1469307064 239 ------RKTSMSFVTALGLSARNLMTKKGRTAMT 266
Cdd:PRK10535 242 ntasgwRQFVSGFREALTMAWRAMAANKMRTLLT 275
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-218 |
4.54e-56 |
|
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: 195.55 E-value: 4.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQSYNLIPHQ 98
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1469307064 179 QVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03294 198 EMQDELLRLQAElqKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-217 |
9.86e-56 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 192.30 E-value: 9.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVF 89
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE----LRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QSynliP-HQ----SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:cd03225 82 QN----PdDQffgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGK 217
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-218 |
3.87e-55 |
|
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: 191.75 E-value: 3.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSF--TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfndRDWDAYRNNR-IG 86
Cdd:cd03295 4 ENVTKRYggGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-----REQDPVELRRkIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGL--GEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
5.97e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 191.07 E-value: 5.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTqsfTQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwday 80
Cdd:PRK09493 1 MIEFKNVSKHFGP---TQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRI--GFVFQSYNLIPHQSILENVELA-LTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:PRK09493 73 RLIRQeaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMtMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
6.11e-55 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 192.00 E-value: 6.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS-TKDFNDRdwda 79
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 yrnnriGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:COG4525 79 ------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLAD--GKIT 219
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-217 |
2.79e-53 |
|
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: 183.93 E-value: 2.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYR 81
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 nnRIGFVFQSYNLIPHQSILENVELALtltgvghaerrqrarkaleavglgehvdkrpsqlSGGQMQRVAIARALINDPE 161
Cdd:cd03229 77 --RIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGK 217
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSL-QAQLgitVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-218 |
1.84e-52 |
|
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: 182.99 E-value: 1.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQSYNLIPHQ 98
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:cd03292 94 NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 179 QVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03292 174 EIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-218 |
4.35e-52 |
|
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: 182.70 E-value: 4.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQ 90
Cdd:cd03261 6 LTKSFgGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRR-RMGMLFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELAL-TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03261 85 SGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 170 GALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03261 165 AGLDPIASGVIDDLIRSL-KKELgltSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
7.79e-52 |
|
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: 181.30 E-value: 7.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDrdWDAYR 81
Cdd:cd03301 1 VELENVTKRFGNV----TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG---RDVTD--LPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03301 72 RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-224 |
1.37e-51 |
|
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: 181.22 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHF-----DSGDLLIDGistKDFNDRDWDAYR-NNRIGFVFQSYN 93
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDG---KDIYDLDVDVLElRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPhQSILENVELALTLTGV-GHAERRQRARKALEAVGLGEHVDKR--PSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03260 92 PFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:cd03260 171 ALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-218 |
2.58e-51 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 181.40 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQSYNLIPHQSI 100
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE----LARRIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELA----LTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTT 176
Cdd:COG1120 93 RELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1469307064 177 SVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG1120 173 QLEVLELLRRLARErgRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-218 |
1.73e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 178.02 E-value: 1.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFtqvaldSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRDWDAY 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL------RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG--------QDLTAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNR--IGFVFQSYNLIPHQSILENVELALT----LTgvghAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIAR 154
Cdd:COG3840 67 PPAErpVSMLFQENNLFPHLTVAQNIGLGLRpglkLT----AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 155 ALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-221 |
1.96e-50 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 178.09 E-value: 1.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYaTRIVTLADGKITDD 221
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
2.61e-50 |
|
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: 186.65 E-value: 2.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFD---SGDLLIDGISTKDFNDRDw 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 78 dayRNNRIGFVFQS--YNLIPHqSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARA 155
Cdd:COG1123 81 ---RGRRIGMVFQDpmTQLNPV-TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-224 |
3.70e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.07 E-value: 3.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 6 VICKRYVTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFND-----RDwda 79
Cdd:PRK09452 14 LVELRGISKSFdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG---QDITHvpaenRH--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 yrnnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:PRK09452 88 -----VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARdRL---VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQR-KLgitFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-211 |
6.73e-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: 179.48 E-value: 6.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL---DHFDSGDLLIDGISTKDFNDRDW 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 78 DAYRNNRIGFVFQ----SYNliPHQSILENVELALTL-TGVGHAERRQRARKALEAVGL---GEHVDKRPSQLSGGQMQR 149
Cdd:COG0444 81 RKIRGREIQMIFQdpmtSLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 150 VAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR-L-VIMVTHNPELAYRYATRIV 211
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLaILFITHDLGVVAEIADRVA 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-218 |
3.35e-48 |
|
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: 171.75 E-value: 3.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 7 ICKRYvtQSFtqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDwdaYRNNRIG 86
Cdd:cd03296 8 VSKRF--GDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVP---VQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQSYNLIPHQSILENVELALTLTGVGH----AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEI 162
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 163 VLADEPTGALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRL-HDELhvtTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-226 |
4.27e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 173.02 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 16 FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQsYnli 95
Cdd:TIGR04521 16 FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRK-KVGLVFQ-F--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 P-HQ----SILENVELALTLTGVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:TIGR04521 91 PeHQlfeeTVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYlERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-224 |
1.06e-47 |
|
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: 173.45 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 36 ILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFndrdwdAYRNNRIGFVFQSYNLIPHQSILENVELALTLTGVGH 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV------PPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 116 AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARdRL--- 192
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQE-QLgit 153
|
170 180 190
....*....|....*....|....*....|..
gi 1469307064 193 VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-218 |
2.41e-47 |
|
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: 168.24 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 32 EFVAILGPSGSGKTTMLNVIGGLDHFDSGDLlidgistkDFNDRDWDAYRNN--------RIGFVFQSYNLIPHQSILEN 103
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTI--------VLNGTVLFDSRKKinlppqqrKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 104 VELALTltGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDL 183
Cdd:cd03297 96 LAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1469307064 184 LKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03297 174 LKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-218 |
2.69e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.07 E-value: 2.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNnRIGFVFQSyNLIPHQSI 100
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG---KPLSAMPPPEWRR-QVAYVPQE-PALWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTLTGVghAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:COG4619 91 RDNLPFPFQLRER--KFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 180 VMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4619 169 VEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-222 |
3.81e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.11 E-value: 3.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwdayRNNRIGFVFQSYNLIPH 97
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---------ARRRIGYVPQRAEVDWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 Q--SILENVELALT----LTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:COG1121 90 FpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 172 LDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDS 222
Cdd:COG1121 170 VDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-222 |
7.25e-47 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 167.65 E-value: 7.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 9 KRYVTQSFTQVA-LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGF 87
Cdd:PRK10584 13 KKSVGQGEHELSiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 88 VFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK10584 93 VFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 168 PTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRyATRIVTLADGKITDDS 222
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-216 |
2.54e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 167.18 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNdrdwdAY 80
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RnnriGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:PRK11248 72 R----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADG 216
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-218 |
4.00e-46 |
|
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: 165.80 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndRDWDAYRnNRIGFVFQSYNLIPHQ 98
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREAR-RQIGVLPDERGLYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:COG4555 90 TVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 179 QVMDLLKDVA-RDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4555 170 LLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-219 |
4.01e-46 |
|
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: 164.67 E-value: 4.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFrDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndRDWDAYRNnRIGFVFQ 90
Cdd:cd03264 6 LTKRYgKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLRR-RIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-217 |
4.64e-46 |
|
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: 162.94 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayr 81
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNRIGFVFQSyNLIPHQSILENVelaltltgvghaerrqrarkaleavglgehvdkrpsqLSGGQMQRVAIARALINDPE 161
Cdd:cd03228 75 RKNIAYVPQD-PFLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGK 217
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-224 |
1.04e-45 |
|
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: 173.79 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQ-SYnlIP 96
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQnPY--LF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVELAltltgvGHAERRQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:COG4988 424 AGTIRENLRLG------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGKITDDSDP 224
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTH 555
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-219 |
7.00e-45 |
|
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: 159.91 E-value: 7.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQsynliphq 98
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE----LARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 silenvelaltltgvghaerrqrarkALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1469307064 179 QVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:cd03214 135 ELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-225 |
1.12e-44 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 161.72 E-value: 1.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGiSTKDF----NDRDWDAYRNNrIGFVFQSYNLI 95
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG-NHFDFsktpSDKAIRELRRN-VGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILEN-VELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:PRK11124 95 PHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 175 TTSVQVMDLLKDVARDRLV-IMVTHNPELAYRYATRIVTLADGKITD--DSDPF 225
Cdd:PRK11124 175 EITAQIVSIIRELAETGITqVIVTHEVEVARKTASRVVYMENGHIVEqgDASCF 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-218 |
1.22e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 164.97 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARdRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINR-ELgltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-218 |
2.24e-44 |
|
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: 160.01 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNdrdwdayrnNRIGFVFQSYNlIPH 97
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYVPQRRS-IDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 Q---SILENVELALTLTGVGH----AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03235 82 DfpiSVRDVVLMGLYGHKGLFrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-221 |
2.53e-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: 172.33 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayRNNrIGFVFQSYNLIpHQS 99
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQ-IGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENveLALTLTGVGhaerRQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:COG2274 565 IREN--ITLGDPDAT----DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGKITDD 221
Cdd:COG2274 639 TSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVED 690
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-224 |
2.94e-44 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 161.12 E-value: 2.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDfnDRDWDAYRNN---------RIGFVF 89
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLKP--DRDGELVPADrrqlqrirtRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QSYNLIPHQSILENV-ELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:COG4598 102 QSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG4598 182 TSALDPELVGEVLKVMRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-218 |
6.69e-44 |
|
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: 159.14 E-value: 6.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLidgistkdFNDRD---WDAYRNNRIGFV--FQSYN 93
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL--------FDGEDitgLPPHEIARLGIGrtFQIPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPHQSILENVELALTLTGVGH----------AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:cd03219 86 LFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGItVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
7.27e-44 |
|
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: 155.88 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNnRIGFVFQSYNLIPHQSI 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG---QDLTDDERKSLRK-EIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 101 LENVELALTLTGVGHAERRQRARKALEAVGLG----EHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-219 |
7.42e-44 |
|
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: 163.35 E-value: 7.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVickryvTQSFTQVALDsVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRDW-DA 79
Cdd:COG4148 2 MLEVDF------RLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--------EVLqDS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 YRN-------NRIGFVFQSYNLIPHQSILENVELALTLTGvgHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAI 152
Cdd:COG4148 67 ARGiflpphrRRIGYVFQEARLFPHLSVRGNLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 153 ARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVaRDRL---VIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILPYLERL-RDELdipILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-223 |
1.75e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.25 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS---TKDFNDRDWD 78
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AYRNNrIGFVFQSYNLIPHQSILEN-VELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:COG4161 79 LLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLV-IMVTHNPELAYRYATRIVTLADGKITDDSD 223
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-218 |
1.91e-43 |
|
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: 157.27 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSFTqvaldsVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGI--STKDFNDRDwda 79
Cdd:cd03298 1 VRLDKIRFSYGEQPMH------FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvTAAPPADRP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 yrnnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:cd03298 72 -----VSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-224 |
2.22e-43 |
|
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: 157.88 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtqsfTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdayr 81
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03299 70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-218 |
8.82e-43 |
|
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: 155.36 E-value: 8.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfNDRDwDAYR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRK-AARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:cd03263 76 S--LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-218 |
1.43e-42 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.48 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF--TQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayrnNRIGFVF 89
Cdd:PRK10851 8 IKKSFgrTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD------RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QSYNLIPHQSILENVELALTLTgvghaERRQRARKA---------LEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVL-----PRRERPNAAaikakvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 161 EIVLADEPTGALDSttsvQVMDLLKDVARdRL-------VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK10851 156 QILLLDEPFGALDA----QVRKELRRWLR-QLheelkftSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-218 |
4.29e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 158.65 E-value: 4.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 4 LRVICKRYVTqsfTQVALDsVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDwDAYRNn 83
Cdd:PRK11000 6 LRNVTKAYGD---VVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVP-PAERG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 84 rIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK11000 77 -VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 164 LADEPTGALDSTTSVQvMDLlkDVAR-----DRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11000 156 LLDEPLSNLDAALRVQ-MRI--EISRlhkrlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-220 |
7.53e-42 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.14 E-value: 7.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFT-QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSG-----DLLIDGisTKDFNDRDwDAYRNNR- 84
Cdd:PRK11264 9 LVKKFHgQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDT--ARSLSQQK-GLIRQLRq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 85 -IGFVFQSYNLIPHQSILENV-ELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEI 162
Cdd:PRK11264 86 hVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 163 VLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
12-218 |
9.21e-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: 150.63 E-value: 9.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRnnRIGFVFQ 90
Cdd:cd03230 6 LSKRYgKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG---KDIKKEPEEVKR--RIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELaltltgvghaerrqrarkaleavglgehvdkrpsqlSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03230 125 GLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-217 |
9.49e-42 |
|
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: 150.09 E-value: 9.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 4 LRVICKRYvtqsFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNn 83
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG---KDIAKLPLEELRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 84 RIGFVFQsynliphqsilenvelaltltgvghaerrqrarkaleavglgehvdkrpsqLSGGQMQRVAIARALINDPEIV 163
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
1.97e-41 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 152.89 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRY--VTqsftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRD-- 76
Cdd:COG0411 4 LLEVRGLTKRFggLV------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG--------RDit 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 77 -WDAYRNNRIGFV--FQSYNLIPHQSILENVELA-------------LTLTGVGHAER--RQRARKALEAVGLGEHVDKR 138
Cdd:COG0411 70 gLPPHRIARLGIArtFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEReaRERAEELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 139 PSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRL--VIMVTHNPELAYRYATRIVTLADG 216
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGitILLIEHDMDLVMGLADRIVVLDFG 229
|
..
gi 1469307064 217 KI 218
Cdd:COG0411 230 RV 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-218 |
3.69e-41 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 155.26 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtqsFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRdwdAYR 81
Cdd:PRK11432 7 VVLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHR---SIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVaRDRLVIM---VTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIREL-QQQFNITslyVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-205 |
3.94e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 152.11 E-value: 3.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL-DHFD----SGDLLIDGistKDFNDRDWDAY---RnnRIGFVFQS 91
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDG---EDIYDPDVDVVelrR--RVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPHqSILENVELALTLTGV-GHAERRQRARKALEAVGLGEHV----DKRPSQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:COG1117 101 PNPFPK-SIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMD 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYR 205
Cdd:COG1117 180 EPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAAR 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-224 |
2.48e-40 |
|
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: 150.27 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfNDRDWDAYRnnRIGFVFQsyNliP 96
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EENLWEIRK--KVGMVFQ--N--P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 -HQSI-----------LENVelaltltGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:TIGR04520 87 dNQFVgatveddvafgLENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAyRYATRIVTLADGKITDDSDP 224
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTP 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-224 |
2.50e-40 |
|
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: 158.01 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAyrnnRIGFVFQSynliPH-- 97
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR----RIAVVPQR----PHlf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 -QSILENveLALTLTGVGHAErrqrARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:COG4987 422 dTTLREN--LRLARPDATDEE----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGKITDDSDP 224
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTH 553
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
20-224 |
2.67e-40 |
|
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: 149.37 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL-DHFD----SGDLLIDGISTKDfNDRDWDAYRNnRIGFVFQSYNL 94
Cdd:TIGR00972 16 ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQDIYD-KKIDVVELRR-RVGMVFQKPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IPhQSILENVELALTLTGV-GHAERRQRARKALEAVGLGEHV----DKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:TIGR00972 94 FP-MSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDEVkdrlHDSALGLSGGQQQRLCIARALAVEPEVLLLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:TIGR00972 173 SALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPT 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-224 |
2.68e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 148.96 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 25 SLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfNDRDWDAYRNNRIGFVFQSYNLIPHQSILENV 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 105 EL----ALTLTGVGHAERRQRARKaleaVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQV 180
Cdd:PRK10771 93 GLglnpGLKLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469307064 181 MDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK10771 169 LTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPT 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-218 |
3.99e-40 |
|
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: 156.77 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 3 DLRVickRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKT-TMLNVIGGL---DHFDSGDLLIDGISTKDFNDRDWD 78
Cdd:COG4172 11 DLSV---AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLpdpAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AYRNNRIGFVFQ----SYNliPHQSILENVELALTL-TGVGHAERRQRARKALEAVGLGE---HVDKRPSQLSGGQMQRV 150
Cdd:COG4172 88 RIRGNRIAMIFQepmtSLN--PLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 151 AIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-216 |
4.88e-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: 148.00 E-value: 4.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRDWDAYRNNRIgFVFQSYNLIPHQSI 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG--------KQITEPGPDRM-VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELAL--TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469307064 179 QVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADG 216
Cdd:TIGR01184 152 NLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-217 |
6.45e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.77 E-value: 6.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfnDRDWDAYRNnRIGFVFQSYNLIPHQSI 100
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRR-RLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTLTGVGHAerRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQV 180
Cdd:COG4133 93 RENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1469307064 181 MDLLKD-VARDRLVIMVTHNPeLAYRyATRIVTLADGK 217
Cdd:COG4133 171 AELIAAhLARGGAVLLTTHQP-LELA-AARVLDLGDFK 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
5.02e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 143.30 E-value: 5.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS-TKdfndrdWD 78
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTK------LP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AY-RNNRIGFVFQ--SYNLIPHQSILENVELAL------TLTGVGHAERRQRARKALEAVGLG--EHVDKRPSQLSGGQM 147
Cdd:COG1101 75 EYkRAKYIGRVFQdpMMGTAPSMTIEENLALAYrrgkrrGLRRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 148 QRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKD-VARDRL-VIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKiVEENNLtTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-223 |
5.87e-38 |
|
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: 141.54 E-value: 5.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 25 SLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFndrdwdAYRNNRIGFVFQSYNLIPHQSILENV 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL------APYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 105 ELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLL 184
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 185 KDVA--RDRLVIMVTHNPELAYRYATRIVTLADGKITDDSD 223
Cdd:TIGR01277 172 KQLCseRQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-218 |
2.16e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.22 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRY--VTQsftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFNDRD 76
Cdd:PRK11650 3 GLKLQAVRKSYdgKTQ-----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 77 wdayrnnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARAL 156
Cdd:PRK11650 78 --------IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 157 INDPEIVLADEPTGALDSTTSVQvMDL-LKDVARdRL---VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHR-RLkttSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-220 |
2.84e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 140.82 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 6 VICKRYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFD-----SGDLLIDGistKDFNDRDWDA 79
Cdd:PRK14247 3 KIEIRDLKVSFGQVeVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDG---QDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 YRNnRIGFVFQSYNLIPHQSILENVELALTLTGV--GHAERRQRARKALEAVGLGEHVDKR----PSQLSGGQMQRVAIA 153
Cdd:PRK14247 80 LRR-RVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 154 RALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-218 |
3.82e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 140.58 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdayr 81
Cdd:PRK11247 13 LLLNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 nnrIGFVFQSYNLIPHQSILENVELALTltgvGHAerRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPE 161
Cdd:PRK11247 83 ---TRLMFQDARLLPWKKVIDNVGLGLK----GQW--RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-215 |
4.90e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 138.77 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL--DHFD-SGDLLIDG--ISTKDFNDRdwdayrnnRIGFVFQSYNLI 95
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGrrLTALPAEQR--------RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTlTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:COG4136 89 PHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1469307064 176 TSVQVMDLLKDVARDR--LVIMVTHNPELAyRYATRIVTLAD 215
Cdd:COG4136 168 LRAQFREFVFEQIRQRgiPALLVTHDEEDA-PAAGRVLDLGN 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-221 |
5.35e-37 |
|
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: 138.65 E-value: 5.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkDFNDRDWDAY 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RnnRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:cd03266 78 R--RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
7.59e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 140.21 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFT-----QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDR 75
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 76 DWDAYRNNrIGFVFQ----SYNliPHQSILENVELALT-LTGVGHAERRQRARKALEAVGLG-EHVDKRPSQLSGGQMQR 149
Cdd:PRK10419 83 QRKAFRRD-IQMVFQdsisAVN--PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 150 VAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-192 |
1.21e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 141.41 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQ----SYNli 95
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVFQdpyaSLN-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTLTGVG-HAERRQRARKALEAVGLG-EHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:COG4608 110 PRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180
....*....|....*....|.
gi 1469307064 174 stTSV--QVMDLLKDVaRDRL 192
Cdd:COG4608 190 --VSIqaQVLNLLEDL-QDEL 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-224 |
3.55e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 141.51 E-value: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFT-QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFndrdwDAYRNNrIGFV 88
Cdd:PRK11607 23 RNLTKSFDgQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRP-INMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 89 FQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 169 TGALDST----TSVQVMDLLKDVARDrlVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK11607 177 MGALDKKlrdrMQLEVVDILERVGVT--CVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-219 |
3.66e-36 |
|
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: 135.85 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDwdayRNNRIGFVFQSYNlipHQSI 100
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKE----RRKSIGYVMQDVD---YQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQV 180
Cdd:cd03226 86 TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469307064 181 MDLLKDVA-RDRLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:cd03226 166 GELIRELAaQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-218 |
5.51e-36 |
|
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: 134.99 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 3 DLRVICKRYVTQSFTQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL--DHFDSGDLLIDGISTKDFNDRdwday 80
Cdd:cd03213 8 NLTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFR----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 rnNRIGFVFQSYNLIPHQSILENVELALTLTGvghaerrqrarkaleavglgehvdkrpsqLSGGQMQRVAIARALINDP 160
Cdd:cd03213 82 --KIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNP-ELAYRYATRIVTLADGKI 218
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-219 |
7.93e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.54 E-value: 7.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFndrDWDAYRNnRIGFVFQSYNLIpHQS 99
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLRR-QIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELaltltGVGHAERrQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:COG1132 430 IRENIRY-----GRPDATD-EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGKIT 219
Cdd:COG1132 504 TSALDTETEALIQEALERLMKGRTTIVIAHRLSTI-RNADRILVLDDGRIV 553
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-226 |
8.19e-36 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.07 E-value: 8.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQ-VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSG-----DLLIDGISTKDFNDRDWDAYRNNrI 85
Cdd:PRK09984 10 LAKTFNQhQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRLARDIRKSRAN-T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 86 GFVFQSYNLIPHQSILENVEL-ALTLTGVGHA-------ERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:PRK09984 89 GYIFQQFNLVNRLSVLENVLIgALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVAR-DRLVIMVT-HNPELAYRYATRIVTLADGKITDD--SDPFD 226
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTlHQVDYALRYCERIVALRQGHVFYDgsSQQFD 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-213 |
3.26e-35 |
|
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: 141.66 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAyrnnRIGFVFQSYNLIP 96
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD----QIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 hQSILENVELALTltGVGHAERRQRARKA-----LEAVGLGEH--VDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:TIGR02857 410 -GTIAENIRLARP--DASDAEIREALERAgldefVAALPQGLDtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRyATRIVTL 213
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-224 |
4.28e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.71 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRD-----WDAYR----NNRIGFVFQS 91
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvADKNQlrllRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPHQSILENV-ELALTLTGVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 170 GALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-221 |
5.87e-35 |
|
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: 133.10 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQSYNLIpH 97
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD----LRRNIGYVPQDVTLF-Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELaltltGVGHAERrQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:cd03245 92 GTLRDNITL-----GAPLADD-ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELaYRYATRIVTLADGKITDD 221
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSL-LDLVDRIIVMDSGRIVAD 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-219 |
7.22e-35 |
|
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: 136.78 E-value: 7.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDsVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQSYNLIPHQS 99
Cdd:TIGR02142 13 SLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVghAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:TIGR02142 92 VRGNLRYGMKRARP--SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1469307064 180 VMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:TIGR02142 170 ILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-226 |
1.18e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 134.83 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLnvigglDHFDSgdLLIDGISTKDFNDRDWDAYRNN---------------- 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFI------EHLNA--LLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 84 ------------RIGFVFQ--SYNLIpHQSILENVELALTLTGVGHAERRQRARKALEAVGLGE-HVDKRPSQLSGGQMQ 148
Cdd:PRK13651 94 fkkikkikeirrRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 149 RVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-219 |
1.26e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 132.31 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQSYNLIPHQS 99
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 180 VMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:PRK10908 176 ILRLFEEFNRVGVtVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-218 |
1.40e-34 |
|
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: 139.82 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFdSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQ----SYNl 94
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQdpfgSLS- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 iPHQSILENVE--LALTLTGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:COG4172 377 -PRMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 172 LDSTTSVQVMDLLKDVARDR----LVImvTHNpeLAY-RY-ATRIVTLADGKI 218
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHglayLFI--SHD--LAVvRAlAHRVMVMKDGKV 504
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-218 |
2.00e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.93 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYR-----NNRIGFVFqsynli 95
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 phqSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI-------NDPEIVLADEP 168
Cdd:COG4559 91 ---TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4559 168 TSALDLAHQHAVLRLARQLARRGGgVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
12-218 |
2.00e-34 |
|
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: 131.25 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGiSTKDFNDRdwdayrnNRIGFVFQ 90
Cdd:cd03269 6 VTKRFGRVtALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDIAAR-------NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
17-221 |
2.89e-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: 141.16 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfndRDWD-AYRNNRIGFVFQSYNLI 95
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI-----RQIDpADLRRNIGYVPQDPRLF 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 pHQSILENVELaltltGVGHAERrQRARKALEAVGLGEHVDKRPS-----------QLSGGQMQRVAIARALINDPEIVL 164
Cdd:TIGR03375 552 -YGTLRDNIAL-----GAPYADD-EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELaYRYATRIVTLADGKITDD 221
Cdd:TIGR03375 625 LDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSL-LDLVDRIIVMDNGRIVAD 680
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-218 |
2.90e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 130.95 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndRDWDAYRNnRIGFVFQSYNLIPHQ 98
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRR-RIGIVFQDLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:cd03265 89 TGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1469307064 179 QVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03265 169 HVWEYIEKLKEefGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-216 |
3.10e-34 |
|
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: 131.40 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYV--TQSFTQ-VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVI-------GGLDHFDSGDLLIDgISTK 70
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVD-LAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 71 DfnDRDWDAYRNNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQR 149
Cdd:COG4778 83 S--PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 150 VAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADG 216
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
5.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.45 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 16 FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLI-DGISTKDFNDRDWDAYRNnRIGFVFQsynl 94
Cdd:PRK13634 18 FERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLKPLRK-KVGIVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IP-HQSILENVELALTLT----GVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:PRK13634 93 FPeHQLFEETVEKDICFGpmnfGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
8.36e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.07 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRY--VTqsftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwd 78
Cdd:COG1129 4 LLEMRGISKSFggVK------ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AyRNNRIGFVFQSYNLIPHQSILENVELALTLTGVG---HAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARA 155
Cdd:COG1129 76 A-QAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHN-PELaYRYATRIVTLADGKITDDSD 223
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLkAQGVAIIYISHRlDEV-FEIADRVTVLRDGRLVGTGP 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-224 |
3.03e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.17 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 16 FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRnnRIGFVFQ--SYN 93
Cdd:PRK13637 18 FEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRK--KVGLVFQypEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIpHQSILENVELALTLTGVGHAERRQRARKALEAVGLG--EHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:PRK13637 96 LF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 172 LDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-221 |
7.69e-33 |
|
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: 127.89 E-value: 7.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGlDHF--DSGDLLIDGistKDFNDRDWDAYRNnRIGFV---FQSYnLI 95
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPptYGNDVRLFG---ERRGGEDVWELRK-RIGLVspaLQLR-FP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVelaltLTG----VGH-----AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:COG1119 93 RDETVLDVV-----LSGffdsIGLyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRL--VIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAptLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-218 |
9.75e-33 |
|
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: 127.00 E-value: 9.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFD---SGDLLIDG--ISTKDFNDRdwdayrnnrIGFVFQSYNLI 95
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGqpRKPDQFQKC---------VAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTLTGvgHAERRQRARKALEAVGLGEHV------DKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03234 94 PGLTVRETLTYTAILRL--PRKSSDAIRKKRVEDVLLRDLaltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 170 GALDSTTSVQVMDLLKDVA-RDRLVIMVTHNP--ELaYRYATRIVTLADGKI 218
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLArRNRIVILTIHQPrsDL-FRLFDRILLLSSGEI 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-224 |
1.03e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQSYNLIPHQ 98
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 179 QVMD-LLKDVAR-DRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK10070 202 EMQDeLVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-218 |
1.96e-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: 126.50 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTmlnVIGGLDHF---DSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQSYNLIPh 97
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERFydpTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTltgVGHAERRQRARKALEAV--------GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03249 91 GTIAENIRYGKP---DATDEEVEEAAKKANIHdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRLVIMVTHNpeL-AYRYATRIVTLADGKI 218
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIVIAHR--LsTIRNADLIAVLQNGQV 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
5.87e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.36 E-value: 5.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYV--TQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdWD 78
Cdd:PRK13633 4 MIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL-WD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AyrNNRIGFVFQSY-NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI 157
Cdd:PRK13633 83 I--RNKAGMVFQNPdNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRyATRIVTLADGKITDDSDP 224
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-224 |
7.91e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.10 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 15 SFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS-TKDFNDRDWDAYRNnRIGFVFQ-SY 92
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHiTPETGNKNLKKLRK-KVSLVFQfPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:PRK13641 96 AQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 172 LDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-218 |
9.00e-32 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 125.33 E-value: 9.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSF-----TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFnd 74
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDY-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 75 rdwdAYRNNRIGFVFQSYN--LIPHQSILENVELALTL-TGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRV 150
Cdd:COG4167 83 ----KYRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 151 AIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLV--IMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-218 |
2.49e-31 |
|
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: 122.33 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwDAYRNNRIGFVFQ 90
Cdd:cd03268 6 LTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK------NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVghaeRRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-218 |
2.96e-31 |
|
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: 122.72 E-value: 2.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFndrDWDAYRNNrIGFVFQSYNLIpHQS 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ-IGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVelALTLTGVGHAErrqrARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:cd03251 92 VAENI--AYGRPGATREE----VEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRLVIMVTHnpELA-YRYATRIVTLADGKI 218
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNRTTFVIAH--RLStIENADRIVVLEDGKI 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
3.16e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 123.41 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSgDLLIDG---ISTKDFNDRDWDAYR-NNRIGFVFQSYNLIP 96
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNE-EARVEGevrLFGRNIYSPDVDPIEvRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVELALTLTGV--GHAERRQRARKALEAVGLGEHVDKR----PSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-218 |
6.33e-31 |
|
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: 119.63 E-value: 6.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkDFNDRDWDAYRnNRIGFVFQSYNLIPhQSI 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA---DISQWDPNELG-DHVGYLPQDDELFS-GSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVelaltltgvghaerrqrarkaleavglgehvdkrpsqLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQV 180
Cdd:cd03246 93 AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 1469307064 181 MDLLKDV-ARDRLVIMVTHNPELAyRYATRIVTLADGKI 218
Cdd:cd03246 136 NQAIAALkAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-224 |
7.37e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 7.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdFNDRDWDAYRNnRIGFVFQSY-NLIPH 97
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRK-TVGIVFQNPdDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:PRK13639 94 PTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 178 VQVMDLLKDVARDRLVIMV-THNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13639 174 SQIMKLLYDLNKEGITIIIsTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
7.47e-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: 119.07 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRY--VtqsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkDFNDRdWDA 79
Cdd:cd03216 1 LELRGITKRFggV------KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASP-RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 yRNNRIGFVFQsynliphqsilenvelaltltgvghaerrqrarkaleavglgehvdkrpsqLSGGQMQRVAIARALIND 159
Cdd:cd03216 73 -RRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLrAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
1.27e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 123.81 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNN------------RIG 86
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYskkiknfkelrrRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQ--SYNLIpHQSILENVELALTLTGVGHAERRQRARKALEAVGLGE-HVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK13631 120 MVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-224 |
1.29e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfnDRDWDAYRnnRIGFVF 89
Cdd:PRK13635 14 RYPDAA--TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRR--QVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QSY-NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:PRK13635 88 QNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRyATRIVTLADGKITDDSDP 224
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-190 |
1.71e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.54 E-value: 1.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTT---MLNVIgglDHFDSGDLLIDGISTKDfNDRDWDAYRNNRIGFVFQS-Y-NL 94
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMI---ETPTGGELYYQGQDLLK-ADPEAQKLLRQKIQIVFQNpYgSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IPHQ---SILEnvELALTLTGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:PRK11308 106 NPRKkvgQILE--EPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180
....*....|....*....|
gi 1469307064 171 ALDSTTSVQVMDLLKDVARD 190
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQE 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-218 |
3.04e-30 |
|
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: 119.64 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkDFNDRDWDAYRNnRIGFVFQSYNLIPhQS 99
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI---DIRDISRKSLRS-MIGVVLQDTFLFS-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELAltltgvghaerRQRAR-----KALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIV 163
Cdd:cd03254 93 IMENIRLG-----------RPNATdeeviEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADGKI 218
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDGKI 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-221 |
5.72e-30 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 119.13 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkDFNDRDWDAYRNnRIGFVFQSyNLIPHQ 98
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGH---DLALADPAWLRR-QVGVVLQE-NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAV-----GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 174 STTSVQVMDLLKDVARDRLVIMVTHNPElAYRYATRIVTLADGKITDD 221
Cdd:cd03252 171 YESEHAIMRNMHDICAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQ 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-200 |
8.80e-30 |
|
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: 125.55 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAyrnnRIGFVFQSYNLIpH 97
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTltGVGHAErrqrARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:TIGR02868 423 TTVRENLRLARP--DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNP 200
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-221 |
4.21e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.89 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLD-----HFDSGDLLIDGISTkdFNDRDWDAYRNnRIGFVFQSY 92
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSI--FNYRDVLEFRR-RVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 NLIPhQSILENVELALTLTG-VGHAERRQRARKALEAVGLGEHVDKR----PSQLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRlsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 168 PTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-218 |
4.56e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.18 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLdhfdsGDLLIDGISTK--DFNDRDWDAYRNN------RIGFVFQS 91
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM-----NDLNPEVTITGsiVYNGHNIYSPRTDtvdlrkEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPhQSILENVELALTLTGVGHAERRQRA-RKALEAVGLGEHVDKRPSQ----LSGGQMQRVAIARALINDPEIVLAD 166
Cdd:PRK14239 95 PNPFP-MSIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-218 |
4.87e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 115.99 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFndRDWDAYRNNR--IGFVFQSYNLIPH 97
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG---RDI--TGLPPHERARagIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELAltltgvGHAERRQRARKALEAV-----GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:cd03224 90 LTVEENLLLG------AYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469307064 173 DSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGRV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
6.91e-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: 122.60 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLID-GISTKDFNDRDWD 78
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AY-RNNR-IGFVFQSYNLIPHQSILENVELALTLTGVGHAERRqRARKALEAVGLGEH-----VDKRPSQLSGGQMQRVA 151
Cdd:TIGR03269 359 GRgRAKRyIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARM-KAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 152 IARALINDPEIVLADEPTGALDSTTSVQVMD-LLKdvARDRL---VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILK--AREEMeqtFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
9.91e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 122.63 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQsfTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDrdwDAYR 81
Cdd:PRK11160 339 LTLNNVSFTYPDQ--PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 NNrIGFVFQSYNLIPHqSILENVELALtltgvgHAERRQRARKALEAVGLGEHVDKRPS----------QLSGGQMQRVA 151
Cdd:PRK11160 414 QA-ISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 152 IARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNpELAYRYATRIVTLADGKI 218
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHR-LTGLEQFDRICVMDNGQI 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
1.78e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.90 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRY--VtqsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRD-W 77
Cdd:COG3845 5 ALELRGITKRFggV------VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSpR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 78 DAyRNNRIGFVFQSYNLIPHQSILENVELALTLTGvGHAERRQRARKALEAV----GLGEHVDKRPSQLSGGQMQRVAIA 153
Cdd:COG3845 76 DA-IALGIGMVHQHFMLVPNLTVAENIVLGLEPTK-GGRLDRKAARARIRELseryGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 154 RALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKsIIFITHKLREVMAIADRVTVLRRGKVVGTVDT 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-218 |
1.82e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 121.88 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGldhFDS--GDLLIDGISTKDFNDRDWdayRNNrIGFVFQSYNLi 95
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG---FLPyqGSLKINGIELRELDPESW---RKH-LSWVGQNPQL- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELAltltgvGHAERRQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVL 164
Cdd:PRK11174 435 PHGTLRDNVLLG------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATrIVTLADGKI 218
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQ-IWVMQDGQI 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.91e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSftQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdaY 80
Cdd:PRK13632 7 MIKVENVSFSYPNSE--NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE---I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNrIGFVFQSynliP-HQSILENVE--LALTLtgvghaERRQRARKAL--------EAVGLGEHVDKRPSQLSGGQMQR 149
Cdd:PRK13632 82 RKK-IGIIFQN----PdNQFIGATVEddIAFGL------ENKKVPPKKMkdiiddlaKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 150 VAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVA--RDRLVIMVTHNPELAYRyATRIVTLADGKITDDSDPFD 226
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKE 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-226 |
2.24e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 115.25 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYR-----NNRIGFVFqsynli 95
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRavlpqHSSLSFPF------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 phqSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALI------NDPEIVLADEPT 169
Cdd:PRK13548 92 ---TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13548 169 SALDLAHQHHVLRLARQLAHERglAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
18-219 |
4.91e-28 |
|
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: 111.64 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdayRNNRIGFVFQSynliPH 97
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQR----PY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 ---QSILENvelaltltgvghaerrqrarkaleavgLGEhvdkrpsQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:cd03247 86 lfdTTLRNN---------------------------LGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 175 TTSVQVMDLLKDVARDRLVIMVTHNpELAYRYATRIVTLADGKIT 219
Cdd:cd03247 132 ITERQLLSLIFEVLKDKTLIWITHH-LTGIEHMDKILFLENGKII 175
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
6.86e-28 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 113.64 E-value: 6.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwday 80
Cdd:COG4604 1 MIEIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 rnnrigfvfqsynLIPHQSIL--EN-VELALT---LTGVG---H------AERRQRARKALEAVGLGEHVDKRPSQLSGG 145
Cdd:COG4604 73 -------------LAKRLAILrqENhINSRLTvreLVAFGrfpYskgrltAEDREIIDEAIAYLDLEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 146 QMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
1.17e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 113.22 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG---ISTKDFNDRDWDAYRNnRIGFVFQSYNLIPH 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlYFGKDIFQIDAIKLRK-EVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHA-ERRQRARKALEAVGLGEHVDKR----PSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 173 DSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-218 |
1.45e-27 |
|
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: 119.05 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQSYNLIpHQS 99
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL----RRQVALVSQDVVLF-NDT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVghaerRQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:TIGR02203 422 IANNIAYGRTEQAD-----RAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRLVIMVTHNPElAYRYATRIVTLADGKI 218
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-226 |
1.51e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.69 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 16 FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS-TKDFNDRDWDAYRNnRIGFVFQ-SYN 93
Cdd:PRK13649 18 FEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQIRK-KVGLVFQfPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK13649 97 QLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 173 DSTTSVQVMDLLKDVARDRLVI-MVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIvLVTHLMDDVANYADFVYVLEKGKLVLSGKPKD 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
1.62e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDwday 80
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 rNNRIGFVFQSYNLIPHQSILENVE-LAlTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:COG4152 70 -RRRIGYLPEERGLYPKMKVGEQLVyLA-RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 160 PEIVLADEPTGALDsttSVQVmDLLKDV-----ARDRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4152 148 PELLILDEPFSGLD---PVNV-ELLKDVirelaAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-224 |
1.89e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.34 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 11 YVTQS---FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIS----TKDFNDRDWdayrNN 83
Cdd:PRK13646 10 YTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRPV----RK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 84 RIGFVFQsynlIPHQSILE-NVELALTLT----GVGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALI 157
Cdd:PRK13646 86 RIGMVFQ----FPESQLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKD--VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-213 |
4.78e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 109.25 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndrdwdayrNNRIGFVFQSYNLIPH 97
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 --QSILENVELAL----TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:NF040873 70 lpLTVRDLVAMGRwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1469307064 172 LDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAyRYATRIVTL 213
Cdd:NF040873 150 LDAESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-224 |
5.38e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.26 E-value: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQSYnLIPHQ-S 99
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL----ARRLALLPQHH-LTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELA----LTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK11231 93 VRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 176 TSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK11231 173 HQVELMRLMRELnTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-224 |
6.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdaYRNNRIGFVFQSYN-LIPHQ 98
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK----WVRSKVGLVFQDPDdQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469307064 179 QVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13647 176 TLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-224 |
9.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.98 E-value: 9.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGisTKDFNDRDWDAYRnnRIGFVFQSY-NLI 95
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG--DLLTEENVWDIRH--KIGMVFQNPdNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK13650 95 VGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 176 TSVQVMDLLKDVARDR--LVIMVTHN-PELAyrYATRIVTLADGKITDDSDP 224
Cdd:PRK13650 175 GRLELIKTIKGIRDDYqmTVISITHDlDEVA--LSDRVLVMKNGQVESTSTP 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-222 |
2.06e-26 |
|
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: 108.96 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkdfndRDWDAYRN--NRIGFVF-QSYNLI 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-------VPWKRRKKflRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 176 TSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDS 222
Cdd:cd03267 188 AQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-218 |
2.30e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 108.86 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIggLDHFD--SGDLLIDGIstkDFNDRDWDAYRnNRIGFVFQSYNLIpHQ 98
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLL--FRFYDvsSGSILIDGQ---DIREVTLDSLR-RAIGVVPQDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELA-LTLTGVGHAERRQRARKALEAVGLGEH----VDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:cd03253 90 TIGYNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGydtiVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 174 STTSVQVMDLLKDVARDRLVIMVTHNPELAYRyATRIVTLADGKI 218
Cdd:cd03253 170 THTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRI 213
|
|
| LolE |
COG4591 |
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall ... |
864-1084 |
3.42e-26 |
|
ABC-type transport system involved in lipoprotein release, permease component LolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443648 [Multi-domain] Cd Length: 283 Bit Score: 109.63 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 864 DLSSLMMSYAKASKLtyennlatLGYADEADPISVKIFPrdfeakervLDHIDAYNKQVKAAGHDEQAISYTDymgiIMG 943
Cdd:COG4591 82 DGSLVYVPLETAQEL--------LGLGDQVSGILVKLKD---------GADAEAVAAALEAALPGLEVKTWRE----LNA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 944 SVTDIVNTISLVLIAFVSISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAETFIEGLI---------- 1013
Cdd:COG4591 141 ALFSALKTEKLILLLILLLILLVAAFNIVNTLLMSVLERTREIGILKALGASRRQIRRIFLLEGLLLGLIggllglllgl 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 1014 ------AGVFAIVVVVAVSLPVnawalaakqvpnlmSLPVQDALVLIAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:COG4591 221 llalllNALLGILLPFIFALPV--------------SLSPSDVLLALLLALLISLLASLYPARRAARLDPVEALRGE 283
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-219 |
4.61e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.12 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQVALDsVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQS 91
Cdd:PRK11144 6 FKQQLGDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPHQSILENVelaltLTGVGHAERRQRArKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:PRK11144 85 ARLFPHYKVRGNL-----RYGMAKSMVAQFD-KIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 172 LDSTTSVQVMDLLKDVARD-RLVIM-VTHNPELAYRYATRIVTLADGKIT 219
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREiNIPILyVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-184 |
5.12e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 108.72 E-value: 5.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICK--RYVTQSF---TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFn 73
Cdd:PRK15112 4 LLEVRNLSKtfRYRTGWFrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 74 drdwdAYRNNRIGFVFQ--SYNLIPHQSILENVELALTL-TGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQR 149
Cdd:PRK15112 83 -----SYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1469307064 150 VAIARALINDPEIVLADEPTGALDSTTSVQVMDLL 184
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-218 |
5.54e-26 |
|
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: 107.56 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 11 YVTQSFTQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdaYRNNRIGFVFQ 90
Cdd:cd03248 21 YPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPhQSILENVelALTLTGVGHAERRQRARKA-------LEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:cd03248 96 EPVLFA-RSLQDNI--AYGLQSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRyATRIVTLADGKI 218
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-223 |
8.14e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 113.26 E-value: 8.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 5 RVICKRYVTQsftQVALDSVSLSFRDNEFVAILGPSGSGKTT----MLNVIGGldhfdSGDLLIDGISTKDFNDRDWDAY 80
Cdd:PRK15134 289 KGILKRTVDH---NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNnRIGFVFQSYN--LIPHQSILENVELAL-----TLTGvghAERRQRARKALEAVGLGEHVDKR-PSQLSGGQMQRVAI 152
Cdd:PRK15134 361 RH-RIQVVFQDPNssLNPRLNVLQIIEEGLrvhqpTLSA---AQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 153 ARALINDPEIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLV-IMVTHNPELAYRYATRIVTLADGKITDDSD 223
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-221 |
8.22e-26 |
|
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: 106.85 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFNdrdwdayrnnrIGFVfqsynliPH 97
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLG-----------GGFN-------PE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 178 VQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:cd03220 179 EKCQRRLRElLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-226 |
8.27e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.09 E-value: 8.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQSYNLIPHQSI 100
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA----ASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALT-----LTGVGHAERRQrARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK09536 95 RQVVEMGRTphrsrFDTWTETDRAA-VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 176 TSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK09536 174 HQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-218 |
1.70e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.75 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNviggLDH--FD--SGDLLIDGISTKDFNDRdwdAYRNNrIGFVFQSYNLI 95
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLIN----LLQrvFDpqSGRILIDGTDIRTVTRA---SLRRN-IAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 pHQSILENveLALTLTGVGHAERRqRARKALEAV--------GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK13657 422 -NRSIEDN--IRVGRPDATDEEMR-AAAERAQAHdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 168 PTGALDSTTSVQVMDLLKDVARDRLVIMVTHnpELA-YRYATRIVTLADGKI 218
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAH--RLStVRNADRILVFDNGRV 547
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-224 |
4.29e-25 |
|
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: 110.66 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFT-QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHF--DSGDLLID----------GISTK-------- 70
Cdd:TIGR03269 6 LTKKFDgKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyvERPSKvgepcpvc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 71 ---------DFNDRDwDAYRNN---RIGFVFQ-SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDK 137
Cdd:TIGR03269 86 ggtlepeevDFWNLS-DKLRRRirkRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 138 RPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMV--THNPELAYRYATRIVTLAD 215
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSHWPEVIEDLSDKAIWLEN 244
|
....*....
gi 1469307064 216 GKITDDSDP 224
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-219 |
8.12e-25 |
|
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: 104.29 E-value: 8.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRD---WDAYRNNR--IGFVFQSYNL 94
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG--------EDitgLPPHRIARlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IPHQSILENVELALTLTGvghaeRRQRARKALEAVG-----LGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:COG0410 90 FPSLTVEENLLLGAYARR-----DRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 170 GAL-----DsttsvQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:COG0410 165 LGLaplivE-----EIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-207 |
1.10e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.86 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDhfdsgDLL----IDGIST---KDFNDRDWDAYR-NNRIGFVFQ 90
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLN-----DLIpgfrVEGKVTfhgKNLYAPDVDPVEvRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPhQSILENVELALTLTGVgHAERRQRARKALEAVGLGEHVDKRPSQ----LSGGQMQRVAIARALINDPEIVLAD 166
Cdd:PRK14243 99 KPNPFP-KSIYDNIAYGARINGY-KGDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYA 207
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVS 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.22e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFNDRdwda 79
Cdd:PRK13537 8 IDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRARHAR---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 yrnNRIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:PRK13537 80 ---QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-224 |
1.23e-24 |
|
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: 103.78 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTqsfTQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--ISTKDFNDRdwdA 79
Cdd:cd03218 1 LRAENLSKRYGK---RKV-VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqdITKLPMHKR---A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 YRNnrIGFVFQSYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLgEHVDKRP-SQLSGGQMQRVAIARALIN 158
Cdd:cd03218 74 RLG--IGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKaSSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 159 DPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVT-HNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-217 |
1.28e-24 |
|
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: 102.55 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLlidgistkdfndrdwdaYRNNRIGFVFQSyNLIPHQS 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-----------------SVPGSIAYVSQE-PWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELaltltgvGHAERRQRARKALEAVGLGEHVDKRPSQ-----------LSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:cd03250 82 IRENILF-------GKPFDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 169 TGALDSTTSVQVMD--LLKDVARDRLVIMVTHNPELAyRYATRIVTLADGK 217
Cdd:cd03250 155 LSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-226 |
1.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.09 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNR-IGFVFQ--SYNLIp 96
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLRKeIGLVFQfpEYQLF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKR-PSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 176 TSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13645 185 GEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-226 |
1.49e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 15 SFT-----QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL---DHFDSGDLLIDGISTKDfnDRDWDAyrNNRIG 86
Cdd:PRK13640 12 SFTypdskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDI--REKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQSY-NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:PRK13640 88 IVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAyRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVE 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-218 |
3.77e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 108.60 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNViggLDHFDSGDLLIDGISTkdFNDRDWDAYRNNRI-GFVFQSYNLIPHQS 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNA---LAFRSPKGVKGSGSVL--LNGMPIDAKEMRAIsAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTL---TGVGHAERRQRARKALEAVGLGEHVDKR---PSQ---LSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:TIGR00955 116 VREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 171 ALDSTTSVQVMDLLKDVA-RDRLVIMVTHNP--ELaYRYATRIVTLADGKI 218
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAqKGKTIICTIHQPssEL-FELFDKIILMAEGRV 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-219 |
6.10e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDgistkdfndrdwdayRNNRIGFVFQ 90
Cdd:COG0488 4 LSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALT----------------------LTGVGHAERR----------QRARKALEAVGLGEHV-DK 137
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAelraleaeleeleaklaepdedLERLAELQEEfealggweaeARAEEILSGLGFPEEDlDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 138 RPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTsvqVM---DLLKDvaRDRLVIMVTHNpelayRY-----ATR 209
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwleEFLKN--YPGTVLVVSHD-----RYfldrvATR 218
|
250
....*....|
gi 1469307064 210 IVTLADGKIT 219
Cdd:COG0488 219 ILELDRGKLT 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-217 |
1.23e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 14 QSFTQVALDSVSLSFRDNEFVAILGPSGSGKT-TMLNVIGGLDH----FDSGDLLIDGISTKDFNDRDWDAYRNNRIGFV 88
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESLLHASEQTLRGVRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 89 FQSynliPHQSI--LENVELALTLTGVGH-AERRQRAR----KALEAVGLgEHVDKR----PSQLSGGQMQRVAIARALI 157
Cdd:PRK15134 98 FQE----PMVSLnpLHTLEKQLYEVLSLHrGMRREAARgeilNCLDRVGI-RQAAKRltdyPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 158 NDPEIVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-226 |
2.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 16 FTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLI-DGISTKDFNDRDWDAYRNnRIGFVFQ-SYN 93
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRK-KVGVVFQfPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLG-EHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 173 DSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSD 230
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-224 |
4.03e-23 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 99.27 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 7 ICKRYVTQSftqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdFNDRDWDAYRNNR-- 84
Cdd:TIGR04406 7 LIKSYKKRK----VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDG-----QDITHLPMHERARlg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 85 IGFVFQSYNLIPHQSILENVELALTLTG-VGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARDRLVIMVT-HNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-218 |
4.29e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.50 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFV---FQSYNLIP 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVELaltltgvghaerrqrarkaleavglgehvdkrPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTT 176
Cdd:cd03215 92 DLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1469307064 177 SVQVMDLLKDVARDRL-VIMV-THNPELaYRYATRIVTLADGKI 218
Cdd:cd03215 140 KAEIYRLIRELADAGKaVLLIsSELDEL-LGLCDRILVMYEGRI 182
|
|
| SalY |
COG0577 |
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms]; |
941-1084 |
3.14e-22 |
|
ABC-type antimicrobial peptide transport system, permease component [Defense mechanisms];
Pssm-ID: 440342 [Multi-domain] Cd Length: 339 Bit Score: 99.20 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 941 IMGSVTDIVNTISLVLIAFVSISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAE----TFIEGLIagv 1016
Cdd:COG0577 202 ILAALYGVLRTLTLLLGAIAGLALLVACIGIMNLMLASVTERTREIGIRKALGASRRDILRQFLTEalllALLGGLL--- 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1017 faivvvvavSLPVNAWA--LAAKQVPNLMSLPVQDALVLIAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:COG0577 279 ---------GLLLALLLlrLLAALLGLPVSLDPWVLLLALALSLLVGLLAGLYPARRAARLDPVEALRSE 339
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFtqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGiSTKDFNDRDWDAY 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-KPIDYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNrIGFVFQSY-NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLgEHVDKRPSQ-LSGGQMQRVAIARALIN 158
Cdd:PRK13636 81 RES-VGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 159 DPEIVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-218 |
1.03e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.76 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQsftqVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVI-------GGLDHFDSGDLLIDGISTKDFN 73
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsarlapdAGEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 74 DR------DWdayrnnriGFVFQS--YNLIPHQSILENVELALTLTGVGHAER-RQRARKALEAVGLG-EHVDKRPSQLS 143
Cdd:PRK11701 82 ERrrllrtEW--------GFVHQHprDGLRMQVSAGGNIGERLMAVGARHYGDiRATAGDWLERVEIDaARIDDLPTTFS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 144 GGQMQRVAIARALINDPEIVLADEPTGALDstTSVQ--VMDLLKDVARD-RL-VIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLD--VSVQarLLDLLRGLVRElGLaVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-224 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDrdWDAYRNnRIGFVFQSynliPH-Q 98
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRK-LVGIVFQN----PEtQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTL----TGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:PRK13644 90 FVGRTVEEDLAFgpenLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 175 TTSVQVMDLLKDVARD-RLVIMVTHNPElAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13644 170 DSGIAVLERIKKLHEKgKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEP 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-199 |
1.29e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 97.49 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 3 DLRVickRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL---DHFDSGDLLIDGISTKDFNDRDWDA 79
Cdd:PRK09473 17 DLRV---TFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 80 YRNNRIGFVFQ----SYNliPHQSILENVELALTL-TGVGHAERRQRARKALEAVGLGEhVDKR----PSQLSGGQMQRV 150
Cdd:PRK09473 94 LRAEQISMIFQdpmtSLN--PYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPE-ARKRmkmyPHEFSGGMRQRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 151 AIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHN 199
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITHD 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-216 |
1.87e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.88 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDgistkdfndrdwdayRNNRIGFVFQ-SYnlIPHQS 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLPQrPY--LPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILEnvelALTLTGVGHAERRQRARKALEAVGLGEHVDK------RPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:COG4178 442 LRE----ALLYPATAEAFSDAELREALEAVGLGHLAERldeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1469307064 174 STTSVQVMDLLKDVARDRLVIMVTHNPELAyRYATRIVTLADG 216
Cdd:COG4178 518 EENEAALYQLLREELPGTTVISVGHRSTLA-AFHDRVLELTGD 559
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-168 |
4.64e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYvtqSFTQVaLDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDG--IStkdfndrDWD 78
Cdd:COG1137 3 TLEAENLVKSY---GKRTV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedIT-------HLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 79 AYRNNR--IGF------VFQsyNLiphqSILENVELALTLTGVGHAERRQRARKALEAVGLgEHVDKRP-SQLSGGQMQR 149
Cdd:COG1137 72 MHKRARlgIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKaYSLSGGERRR 144
|
170
....*....|....*....
gi 1469307064 150 VAIARALINDPEIVLADEP 168
Cdd:COG1137 145 VEIARALATNPKFILLDEP 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-226 |
8.82e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 8.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndrdwdayrnnRIGFV------FQsy 92
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------------RVSALlelgagFH-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 nliPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDkRP-SQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:COG1134 101 ---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 172 LDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:COG1134 177 GDAAFQKKCLARIRElRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-220 |
1.30e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 94.42 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKT-TMLNVIGGLDHfdSGDLLIDGIStkdFNDRDWDAY----RNNRIG----FVFQ 90
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDY--PGRVMAEKLE---FNGQDLQRIsekeRRNLVGaevaMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 S--YNLIPHQSILENVELALTL-TGVGHAERRQRARKALEAVGL---GEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:PRK11022 97 DpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-225 |
1.32e-20 |
|
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: 98.93 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFnDRDWDAYRNNrIGFVFQSYNLIPHQS 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDI-ETNLDAVRQS-LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469307064 180 VMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDPF 225
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPL 1145
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-184 |
1.34e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 94.20 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL---------D--HFDSGDLLidGIST 69
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhvtaDrfRWNGIDLL--KLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 70 KD---FNDRDwdayrnnrIGFVFQ--SYNLIPHQSILENVELAL---TLTGV---GHAERRQRARKALEAVGLGEHVDKR 138
Cdd:COG4170 81 RErrkIIGRE--------IAMIFQepSSCLDPSAKIGDQLIEAIpswTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 139 ---PSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLL 184
Cdd:COG4170 153 nsyPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLL 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-224 |
2.35e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.97 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 22 DSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQ----------- 90
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE----VARRIGLLAQnattpgditvq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 ---SYNLIPHQSILENvelaltltgvGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK10253 100 elvARGRYPHQPLFTR----------WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 168 PTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-190 |
2.60e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.62 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNrIGFVFQ----SYNli 95
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQdplaSLN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELALTL--TGVGHAERRQRARKALEAVGLGEHVDKR-PSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK15079 113 PRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170
....*....|....*...
gi 1469307064 173 DSTTSVQVMDLLKDVARD 190
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQRE 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-213 |
2.81e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 14 QSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRnNRIGFVFQSYN 93
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG---EDISTLKPEIYR-QQVSYCAQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIpHQSILENVELALTLTgvGHAERRQRARKALEAVGLGEHV-DKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK10247 92 LF-GDTVYDNLIFPWQIR--NQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1469307064 173 DSTTSVQVMDLLKDVARDR--LVIMVTHNPElAYRYATRIVTL 213
Cdd:PRK10247 169 DESNKHNVNEIIHRYVREQniAVLWVTHDKD-EINHADKVITL 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-218 |
3.39e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdFNDRdwDAYRnNRIGFVF-QSYNLIPHQ 98
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP--FKRR--KEFA-RRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1469307064 179 QVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4586 192 AIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-226 |
3.67e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndRDWDAYRnnRIGFVFQ 90
Cdd:PRK13536 47 VSKSYgDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLARA--RIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 171 ALDSTTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13536 202 GLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-217 |
3.92e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwDAYrNNRIGFVFQ 90
Cdd:PRK11288 10 IGKTFPGVkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT--AAL-AAGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTGVGHAERRQ---RARKALEavGLGEHVDkrPSQ----LSGGQMQRVAIARALINDPEIV 163
Cdd:PRK11288 87 ELHLVPEMTVAENLYLGQLPHKGGIVNRRLlnyEAREQLE--HLGVDID--PDTplkyLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-218 |
4.41e-20 |
|
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: 90.25 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayRnNRIGFVFQS-------- 91
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---R-SRISIIPQDpvlfsgti 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 -YNLIPHqSILENVELaltltgvghaerrqraRKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALIND 159
Cdd:cd03244 95 rSNLDPF-GEYSDEEL----------------WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHnpelayRYAT-----RIVTLADGKI 218
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLDTiidsdRILVLDKGRV 215
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-224 |
5.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.31 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGisTKDFNDRDWDAYRnnRIGFVFQSY-NLIPHQS 99
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG--ELLTAENVWNLRR--KIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 180 VMDLLKDVaRDRL---VIMVTHNPELAYRyATRIVTLADGKITDDSDP 224
Cdd:PRK13642 179 IMRVIHEI-KEKYqltVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-200 |
1.63e-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: 87.80 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWD--AYRNNRIGfvfqsynLIP 96
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEniLYLGHLPG-------LKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENvelaLTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTT 176
Cdd:TIGR01189 87 ELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*
gi 1469307064 177 SVQVMDLLKD-VARDRLVIMVTHNP 200
Cdd:TIGR01189 163 VALLAGLLRAhLARGGIVLLTTHQD 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-220 |
1.64e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.15 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNrIGFVFQS--YNLIPH 97
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHAER-RQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAaAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469307064 176 TSVQVMDLLKDVARDRLV--IMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-219 |
2.27e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRD-WDAYRNnRIGFV---FQSYNLI 95
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSpRDAIRA-GIAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELAL--TLTGVG---HAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:COG1129 343 LDLSIRENITLASldRLSRGGlldRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 170 -----GAldsttSVQVMDLLKDVARDRL-VIMVTHN-PELAyRYATRIVTLADGKIT 219
Cdd:COG1129 423 rgidvGA-----KAEIYRLIRELAAEGKaVIVISSElPELL-GLSDRILVMREGRIV 473
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-200 |
2.84e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.17 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 22 DSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndRDWDAYRnnrigfvfqsYNL--IPHQ- 98
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDEYH----------QDLlyLGHQp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 ------SILENVELALTLTGVGHAErrqRARKALEAVGLG--EHVdkrP-SQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PRK13538 84 giktelTALENLRFYQRLHGPGDDE---ALWEALAQVGLAgfEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|...
gi 1469307064 170 GALDsTTSVQVMD--LLKDVARDRLVIMVTHNP 200
Cdd:PRK13538 158 TAID-KQGVARLEalLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
14-226 |
3.75e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.65 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 14 QSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQS-Y 92
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQNpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:PRK13648 94 NQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 173 DSTTSVQVMDLLKDVARDRLV--IMVTHNPELAYRyATRIVTLADGKITDDSDPFD 226
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEHNItiISITHDLSEAME-ADHVIVMNKGTVYKEGTPTE 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-217 |
3.83e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.30 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL-DHFD-SGDLLIDGISTKDFNDRDWDAyrnNRIG 86
Cdd:PRK13549 9 KNITKTFGGVkALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyPHGTyEGEIIFEGEELQASNIRDTER---AGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQSYNLIPHQSILENVELALTLTGVG---HAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGimdYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-202 |
5.31e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.28 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 22 DSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNnRIGFVFQSYNLIPHQSIL 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 102 ENVELAL-TLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS--- 177
Cdd:PRK11831 103 DNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMgvl 182
|
170 180
....*....|....*....|....*.
gi 1469307064 178 VQVMDLLKDvARDRLVIMVTHN-PEL 202
Cdd:PRK11831 183 VKLISELNS-ALGVTCVVVSHDvPEV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-218 |
5.93e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.48 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 11 YVTQSFTQVaLDSVSLSFRDNEFVAILGPSGSGKTTmlnVIGGLDHF---DSGDLLIDGISTKDFNDRdwdaYRNNRIGF 87
Cdd:TIGR00958 488 YPNRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNLyqpTGGQVLLDGVPLVQYDHH----YLHRQVAL 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 88 VFQSYNLIpHQSILENVELALTLTGvgHAERRQRARKALEAVGLGE-------HVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:TIGR00958 560 VGQEPVLF-SGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEfpngydtEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKdvARDRLVIMVTHNPELAYRyATRIVTLADGKI 218
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-226 |
6.75e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.96 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGlDHFDS---------GDLLIDGISTKDFNDRDWDAYR-----NNR 84
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 85 IGFVFQSYNLI-----PHQSilenvelaltLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARAL--- 156
Cdd:PRK13547 94 PAFAFSAREIVllgryPHAR----------RAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 157 ------INDPEIVLADEPTGALDSTTSVQVMDLLKDVARD-RL-VIMVTHNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-223 |
7.08e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 87.45 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTtmLNVIGGLDHFD------SGDLLIDGISTKDfndrdwDAYRNNRIGFVFQ 90
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPagvrqtAGRVLLDGKPVAP------CALRGRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 ----SYNliPHQSILEN-VElalTLTGVGHAERRQRARKALEAVGLGEhvDKR-----PSQLSGGQMQRVAIARALINDP 160
Cdd:PRK10418 87 nprsAFN--PLHTMHTHaRE---TCLALGKPADDATLTAALEAVGLEN--AARvlklyPFEMSGGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARDRL--VIMVTHNPELAYRYATRIVTLADGKITDDSD 223
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-220 |
7.26e-19 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 91.64 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFnDRDwdaYRNNRIGFVFQSYNLIPh 97
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRE---TFGKHIGYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVelaltltgvGHAERRQRARKALEAVGL-GEH-------------VDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:TIGR01842 406 GTVAENI---------ARFGENADPEKIIEAAKLaGVHelilrlpdgydtvIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELaYRYATRIVTLADGKITD 220
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSL-LGCVDKILVLQDGRIAR 533
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-219 |
8.12e-19 |
|
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: 86.81 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDrdWDAYRNNR--IGFVFQSYNLIPH 97
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG---EDITK--LPPHERARagIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHAERRQRARkALEAVgLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:TIGR03410 90 LTVEENLLTGLAALPRRSRKIPDEIY-ELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1469307064 178 VQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:TIGR03410 168 KDIGRVIRRLRAEGgmAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-199 |
1.06e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.01 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDsGDLLIDGiSTKDFNDRDWDAYRN-NR----IGFVFQS 91
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEG-RVEFFNQNIYERRVNlNRlrrqVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPhQSILENVELALTLTG-VGHAERRQRARKALEAVGLGEHVD----KRPSQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVA-RDRL-VIMVTHN 199
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRlRSELtMVIVSHN 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-217 |
1.18e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDrdwdaYRNNRIGFV--FQSYNLIPH 97
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-----HQIARMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELA-------------LTLTGVGHAERR--QRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEI 162
Cdd:PRK11300 95 MTVIENLLVAqhqqlktglfsglLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 163 VLADEPTGALDSTTSVQVMDLLkDVARDRL---VIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELI-AELRNEHnvtVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
2.53e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTqsfTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAY 80
Cdd:PRK13652 3 LIETRDLCYSYSG---SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 rnnrIGFVFQ-SYNLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:PRK13652 80 ----VGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARD--RLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-216 |
2.88e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFVFQ 90
Cdd:PRK09700 11 IGKSFGPVhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKLDHKLAAQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELALTLTG-------VGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK09700 88 ELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADG 216
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-224 |
8.87e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGiSTKDFNDRDWDAYRNnRIGFVFQSynliPHQSI 100
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALRQ-QVATVFQD----PEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 L-----ENVELALTLTGVGHAERRQRARKALEAVGlGEHVDKRPSQ-LSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:PRK13638 91 FytdidSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 175 TTSVQVMDLLKD-VARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK13638 170 AGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-217 |
2.08e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 86.80 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGL-DHFD-SGDLLIDGISTKDFNDRDWDAyrnNRIG 86
Cdd:TIGR02633 5 KGIVKTFGGVkALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyPHGTwDGEIYWSGSPLKASNIRDTER---AGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVFQSYNLIPHQSILENVELA--LTLTG--VGHAERRQRARKALEAVGLGEHVDKRP-SQLSGGQMQRVAIARALINDPE 161
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 162 IVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-220 |
2.34e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIdGISTKdfndrdwdayrnnrIGFVFQSY-NLIPHQS 99
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------------IGYFDQHQeELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENvelaltLTGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDsTTSV 178
Cdd:COG0488 396 VLDE------LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-IETL 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469307064 179 QVM-DLLKD---VardrlVIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:COG0488 469 EALeEALDDfpgT-----VLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
17-219 |
3.60e-17 |
|
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: 86.34 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayRNNRIGFVFQSYNLIP 96
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE----LGRHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 hQSILEN-----------VELALTLTGVgHaerrqrarkalEAV-----GLGEHVDKRPSQLSGGQMQRVAIARALINDP 160
Cdd:COG4618 420 -GTIAENiarfgdadpekVVAAAKLAGV-H-----------EMIlrlpdGYDTRIGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDV-ARDRLVIMVTHNPELAyRYATRIVTLADGKIT 219
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLL-AAVDKLLVLRDGRVQ 545
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-202 |
4.08e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.08 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQ-VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndrdwdayrNNRIGFVFQ 90
Cdd:PRK09544 10 VSVSFGQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPhqSILENVELALTLT-GVghaeRRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PRK09544 75 KLYLDT--TLPLTVNRFLRLRpGT----KKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1469307064 170 GALDSTTSVQVMDLLkDVARDRL---VIMVTHNPEL 202
Cdd:PRK09544 149 QGVDVNGQVALYDLI-DQLRRELdcaVLMVSHDLHL 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-200 |
7.22e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 26 LSFR--DNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGfvfqsynLIPHQSILEN 103
Cdd:PRK13539 21 LSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNA-------MKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 104 VELALTLTGvghaERRQRARKALEAVGLGeHVDKRPSQ-LSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMD 182
Cdd:PRK13539 94 LEFWAAFLG----GEELDIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
170
....*....|....*....
gi 1469307064 183 LLKD-VARDRLVIMVTHNP 200
Cdd:PRK13539 169 LIRAhLAQGGIVIAATHIP 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-217 |
8.24e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKT-TMLNVIGGLDH----FDSGDLLI-----DGISTKDFNDRDWDAYRNNRIGFVF 89
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQagglVQCDKMLLrrrsrQVIELSEQSAAQMRHVRGADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QS--YNLIPHQSILENVELALTL-TGVGHAERRQRARKALEAVGLGEH---VDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVARDRL--VIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
10-217 |
8.74e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.84 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDS--GDLLIDGiSTKDFND-RDwdayrNNRI 85
Cdd:NF040905 5 RGITKTFPGVkALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG-EVCRFKDiRD-----SEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 86 GFVF--QSYNLIPHQSILENVELaltltGVGHAER--------RQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARA 155
Cdd:NF040905 79 GIVIihQELALIPYLSIAENIFL-----GNERAKRgvidwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDVaRDRLV--IMVTH--NpELAyRYATRIVTLADGK 217
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGItsIIISHklN-EIR-RVADSITVLRDGR 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-226 |
1.12e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLID--GISTKDFNDRdwdAYRNnrIGFVFQSYNLIPHQ 98
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHAR---ARRG--IGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQ-RARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 178 VQVMDLLKDVARDRLVIMVT-HNPELAYRYATRIVTLADGKITDDSDPFD 226
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-224 |
1.32e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQSYNLIPHQSI 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVEL-------ALTLTGvghAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:PRK10575 103 RELVAIgrypwhgALGRFG---AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 174 STTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADGKITDDSDP 224
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-218 |
1.73e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 84.10 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNnRIGFVFQS---YNliph 97
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG---QDIRDVTQASLRA-AIGIVPQDtvlFN---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVelALTLTGVGHAERRQRARKA-----LEAV--GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:COG5265 446 DTIAYNI--AYGRPDASEEEVEAAARAAqihdfIESLpdGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDR--LVImvthnpelAYR-----YATRIVTLADGKI 218
Cdd:COG5265 524 ALDSRTERAIQAALREVARGRttLVI--------AHRlstivDADEILVLEAGRI 570
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-225 |
2.46e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwdAYRNNRIGFVFQS 91
Cdd:PRK15056 14 VTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-------ALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPHQSILenVELALTLTGVGH--------AERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK15056 87 EEVDWSFPVL--VEDVVMMGRYGHmgwlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVaRD--RLVIMVTHN----------------------P----------ELAYRYATR 209
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLREL-RDegKTMLVSTHNlgsvtefcdytvmvkgtvlasgPtettftaenlELAFSGVLR 243
|
250
....*....|....*....
gi 1469307064 210 IVTLADGK---ITDDSDPF 225
Cdd:PRK15056 244 HVALNGSEesiITDDERPF 262
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-218 |
2.94e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.54 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDrdWDAYRNNR--IGFVFQSYNLIPH 97
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDITD--WQTAKIMReaVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELaltltGVGHAERRQRARKALEAVGLGEHVDKRPSQ----LSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:PRK11614 95 MTVEENLAM-----GGFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469307064 174 STTSVQVMDLLKDVARDRLVI-MVTHNPELAYRYATRIVTLADGKI 218
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQGMTIfLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-200 |
3.16e-16 |
|
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: 78.30 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGisTKDFNDRDWDAyrnnrigfvfQSYNLIPHQ 98
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--GPLDFQRDSIA----------RGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 -------SILENVELALTLTGvghaerRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:cd03231 82 pgikttlSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190
....*....|....*....|....*....|
gi 1469307064 172 LDSTTSVQVMDLLKD-VARDRLVIMVTHNP 200
Cdd:cd03231 156 LDKAGVARFAEAMAGhCARGGMVVLTTHQD 185
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-218 |
3.89e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.14 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGIstkDFNDRDWDAYRNNrIGFVFQSYNLIpHQS 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH---DLRDYTLASLRNQ-VALVSQNVHLF-NDT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTltgvGHAERRQ--RARKALEAVGLGEHVDK--------RPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PRK11176 433 IANNIAYART----EQYSREQieEAARMAYAMDFINKMDNgldtvigeNGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRLVIMVTHnpelayRYAT-----RIVTLADGKI 218
Cdd:PRK11176 509 SALDTESERAIQAALDELQKNRTSLVIAH------RLSTiekadEILVVEDGEI 556
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-200 |
4.02e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 77.67 E-value: 4.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFD--SGDLLIDGIS-TKDFndrdwdayrNNRIGFVFQSYNLIPH 97
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPlDKNF---------QRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGVGHAERRqrarkaleavglgehvdkrpsqlsggqmqRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:cd03232 94 LTVREALRFSALLRGLSVEQRK-----------------------------RLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|....
gi 1469307064 178 VQVMDLLKDVARDRLVIMVT-HNP 200
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTiHQP 168
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-218 |
6.85e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHF--DSGDLLIDGistKDFNDrdWDAY-RNNR-IGFVFQS----- 91
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDG---EDILE--LSPDeRARAgIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 ----YNLIpHQSILENVELALTLtgvghAERRQRARKALEAVGLGEHVDKRP--SQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:COG0396 91 gvsvSNFL-RTALNARRGEELSA-----REFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 166 DEPTGALDsttsvqvMDLLKDVAR--------DRLVIMVTHNPE-LAYRYATRIVTLADGKI 218
Cdd:COG0396 165 DETDSGLD-------IDALRIVAEgvnklrspDRGILIITHYQRiLDYIKPDFVHVLVDGRI 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-226 |
7.48e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.23 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 1 MLDLRVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLD-----------HFDSGDLLidgist 69
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvtadrmRFDDIDLL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 70 kDFNDRDWDAYRNNRIGFVFQSYN--LIPHQSILENVELAL---TLTGVGHAERRQRARKALE---AVGLGEHVD---KR 138
Cdd:PRK15093 77 -RLSPRERRKLVGHNVSMIFQEPQscLDPSERVGRQLMQNIpgwTYKGRWWQRFGWRKRRAIEllhRVGIKDHKDamrSF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 139 PSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDR--LVIMVTHNPELAYRYATRIVTLADG 216
Cdd:PRK15093 156 PYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINVLYCG 235
|
250
....*....|
gi 1469307064 217 KITDDSDPFD 226
Cdd:PRK15093 236 QTVETAPSKE 245
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-218 |
7.55e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 7.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDS----VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFdSGDLLIDGISTkdfndRDWDAYRNNRigfvFQSY 92
Cdd:COG4138 4 NDVAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPL-----SDWSAAELAR----HRAY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 nLIPHQSILENVE----LALTLTGVGHAERRQRARKAL-EAVGLGEHVDKRPSQLSGGQMQRVAIARAL------IN-DP 160
Cdd:COG4138 74 -LSQQQSPPFAMPvfqyLALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEG 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKI 218
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-217 |
1.01e-14 |
|
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: 72.48 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDgistkdfndrdwdayRNNRIGFVfqsynliphqsi 100
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------STVKIGYF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 lenvelaltltgvghaerrqrarkaleavglgehvdkrpSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQV 180
Cdd:cd03221 69 ---------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*..
gi 1469307064 181 MDLLKDVarDRLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:cd03221 110 EEALKEY--PGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-224 |
1.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFV---FQSYNLI 95
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG---EDITGLSPRERRRLGVAYIpedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENveLALTLTGVG---------HAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:COG3845 349 PDMSVAEN--LILGRYRRPpfsrggfldRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDvARDR----LVImvthNPEL--AYRYATRIVTLADGKITDDSDP 224
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLE-LRDAgaavLLI----SEDLdeILALSDRIAVMYEGRIVGEVPA 486
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-173 |
1.76e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.73 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 26 LSFRDNEFVAIL--GPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDfndrdwdAYRNNRIGFVFQSYNLIPHQSILEN 103
Cdd:PRK13543 30 LDFHVDAGEALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-------GDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 104 VELALTLTGVgHAerRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALD 173
Cdd:PRK13543 103 LHFLCGLHGR-RA--KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-175 |
3.62e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkDFND-RDwdaYRNNRIGFVF 89
Cdd:PRK10762 10 IDKAFPGVkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGpKS---SQEAGIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 QSYNLIPHQSILENV----ELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:PRK10762 86 QELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIM 165
|
170
....*....|
gi 1469307064 166 DEPTGALDST 175
Cdd:PRK10762 166 DEPTDALTDT 175
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-217 |
6.63e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 32 EFVAILGPSGSGKTTMLNVIGGLDHFDS--GDLLIdgistkdfNDRDWDAYRNNRIGFVFQSYNLIPHQSILEN------ 103
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILA--------NNRKPTKQILKRTGFVTQDDILYPHLTVRETlvfcsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 104 VELALTLTgvgHAERRQRARKALEAVGLGEHVDKRPSQ-----LSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:PLN03211 167 LRLPKSLT---KQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 179 QVMDLLKDVA-RDRLVIMVTHNP-ELAYRYATRIVTLADGK 217
Cdd:PLN03211 244 RLVLTLGSLAqKGKTIVTSMHQPsSRVYQMFDSVLVLSEGR 284
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-169 |
7.19e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.32 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRdwdAYRNN---RIGFVFQSY-- 92
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMADA---RHRRAvcpRIAYMPQGLgk 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 93 NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDkRPS-QLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:NF033858 88 NLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFAD-RPAgKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-219 |
1.28e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.99 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDgistKDFN-DR-DWDAYRNNRiGFVF--------- 89
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIvARlQQDPPRNVE-GTVYdfvaegiee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 90 -----QSYNLIPHQ----------SILENVELALTLTGVGHAErrQRARKALEAVGLgeHVDKRPSQLSGGQMQRVAIAR 154
Cdd:PRK11147 94 qaeylKRYHDISHLvetdpseknlNELAKLQEQLDHHNLWQLE--NRINEVLAQLGL--DPDAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 155 ALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDrlVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS--IIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-215 |
1.30e-13 |
|
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: 69.88 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDllidgistkdfndrdWDAYRNNRIGFVFQ-SYnlIP 96
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR---------------IGMPEGEDLLFLPQrPY--LP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 hqsilenvelALTLtgvghaerRQRARKALEAVglgehvdkrpsqLSGGQMQRVAIARALINDPEIVLADEPTGALDSTT 176
Cdd:cd03223 77 ----------LGTL--------REQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 177 SVQVMDLLKdvarDRL--VIMVTHNPELAyRYATRIVTLAD 215
Cdd:cd03223 127 EDRLYQLLK----ELGitVISVGHRPSLW-KFHDRVLDLDG 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-217 |
1.72e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFVFQ 90
Cdd:PRK10982 4 ISKSFPGVkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SYNLIPHQSILENVELA-LTLTG--VGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrYPTKGmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 168 PTGALdstTSVQVMDLLKDVA--RDR--LVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK10982 161 PTSSL---TEKEVNHLFTIIRklKERgcGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-218 |
1.85e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.36 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIggLDHFD--SGDLLIDGISTKDFNDRDWDAyrnnRIGFVFQSYNL 94
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI--QRHFDvsEGDIRFHDIPLTKLQLDSWRS----RLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IPhQSILENVelALTLTGVGHAERRQRARkaLEAV---------GLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLA 165
Cdd:PRK10789 401 FS-DTVANNI--ALGRPDATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPElAYRYATRIVTLADGKI 218
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLS-ALTEASEILVMQHGHI 527
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
941-1084 |
2.63e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 74.45 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 941 IMGSVTDIVNTISLVLIAFVSISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAETFIEGLIAGVFAIV 1020
Cdd:COG3127 692 ILDQVRDILDQVSLAVEFLAGFALLAGLLVLAAALAASRDERTREAALLRTLGASRRQLRRALALEFALLGLLAGLLAAL 771
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 1021 VVVAVslpvnAWALaAKQVPNL-MSLPVQDALVLIAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:COG3127 772 LAELA-----GWAL-ARFVFDLpFSPPWWLWLAGLLGGALLVLLAGLLGARRVLRQPPLEVLREE 830
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-218 |
2.85e-13 |
|
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: 69.86 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHF--DSGDLLIDGISTKDF--NDRdwdayRNNRIGFVFQSYNLIP 96
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLppEER-----ARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 hqsilenvelaltltGVghaerrqRARKALEAVGLGehvdkrpsqLSGGQMQRVAIARALINDPEIVLADEPTGALDstt 176
Cdd:cd03217 91 ---------------GV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD--- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 177 svqvMDLLKDVAR--------DRLVIMVTHNPELA-YRYATRIVTLADGKI 218
Cdd:cd03217 137 ----IDALRLVAEvinklreeGKSVLIITHYQRLLdYIKPDRVHVLYDGRI 183
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-198 |
2.85e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.07 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 29 RDNEFVAILGPSGSGKTTMLNVIGG-----LDHFDSGDllidgistkdfndrDWD----AYRnnriGFVFQSY------- 92
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGelipnLGDYEEEP--------------SWDevlkRFR----GTELQNYfkklyng 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 -----------NLIPHQ------SILENVElaltltgvghaeRRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARA 155
Cdd:PRK13409 159 eikvvhkpqyvDLIPKVfkgkvrELLKKVD------------ERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTH 198
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH 269
|
|
| FtsX |
pfam02687 |
FtsX-like permease family; This is a family of predicted permeases and hypothetical ... |
957-1077 |
4.28e-13 |
|
FtsX-like permease family; This is a family of predicted permeases and hypothetical transmembrane proteins. Swiss:P57382 has been shown to transport lipids targeted to the outer membrane across the inner membrane. Both Swiss:P57382 and Swiss:O54500 have been shown to require ATP. This region contains three transmembrane helices.
Pssm-ID: 460652 [Multi-domain] Cd Length: 120 Bit Score: 66.89 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 957 IAFVSISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAETFIEGLIAGVFAIVVVVAVSLPVNAWALAA 1036
Cdd:pfam02687 1 ILFSLLILLLAVLIILLLLSISISERRREIGILRALGASRKQIFKLLLLEALLIGLIGLVIGLLLGLLLAKLIAILLYSS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1469307064 1037 KQVPNlMSLPVQDALVLIAVSVLLTVVAGLLPARSASKKDP 1077
Cdd:pfam02687 81 GISLP-ILVPPLSILIALLLALLIALLASLLPALRIRKINP 120
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-198 |
1.01e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.75 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 58 DSGDLLIDGISTKDFNDRDWdayrNNRIGFVFQSYNLIpHQSILENVELaltltGVGHAERrQRARKALEAVGLGEHVDK 137
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLF-NMSIYENIKF-----GKEDATR-EDVKRACKFAAIDEFIES 1343
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 138 RPSQ-----------LSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDV--ARDRLVIMVTH 198
Cdd:PTZ00265 1344 LPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAH 1417
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-219 |
1.05e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 24 VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRD-WDAYRNNrIGFVFQSY---NLIPHQS 99
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSpLDAVKKG-MAYITESRrdnGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELA--LTLTGVG-------HAERRQRARKALEAVGLGEH-VDKRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PRK09700 358 IAQNMAISrsLKDGGYKgamglfhEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 170 GALDSTTSVQVMDLLKDVARD-RLVIMVTHN-PELaYRYATRIVTLADGKIT 219
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDgKVILMVSSElPEI-ITVCDRIAVFCEGRLT 488
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-218 |
1.15e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 6 VICKRYVTQSFTQVA-LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYrnnR 84
Cdd:PRK15439 11 LLCARSISKQYSGVEvLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL---G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 85 IGFVFQSYNLIPHQSILENVELALTltgvGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 165 ADEPTGALdstTSVQVMDLLKDV----ARDRLVIMVTHN-PELaYRYATRIVTLADGKI 218
Cdd:PRK15439 164 LDEPTASL---TPAETERLFSRIrellAQGVGIVFISHKlPEI-RQLADRISVMRDGTI 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-202 |
1.63e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLdhfdsgdllIDGISTKDFNDRDWDAYRNNRigfvfqsynlip 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA---------LKGTPVAGCVDVPDNQFGREA------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 hqSILENVELALTLTgvghaerrqRARKALEAVGLGEHVD--KRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:COG2401 101 --SLIDAIGRKGDFK---------DAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190
....*....|....*....|....*....|
gi 1469307064 175 TTSVQVMDLLKDVARDRLV--IMVTHNPEL 202
Cdd:COG2401 170 QTAKRVARNLQKLARRAGItlVVATHHYDV 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-206 |
2.79e-12 |
|
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: 70.73 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDhfdsgdllidgistKDFNDRDWDAyRNNRIGFVFQSYNLIPHQSI 100
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD--------------KDFNGEARPQ-PGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELaltltGVGH-------------------------AERRQRARKALEAVGLGEHV---------------DKRPS 140
Cdd:TIGR03719 86 RENVEE-----GVAEikdaldrfneisakyaepdadfdklAAEQAELQEIIDAADAWDLDsqleiamdalrcppwDADVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 141 QLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDrlVIMVTHNpelayRY 206
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGT--VVAVTHD-----RY 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-217 |
2.96e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFdSGDLLIDGISTKDFNDRDWDAYRnnrigfvfqSYnLIPHQSI 100
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR---------AY-LSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVE----LALTL-TGVGHAERRQRARKALEAVGLGehvDK--RP-SQLSGGQMQRVAIARALIN-DPEI------VLA 165
Cdd:PRK03695 81 PFAMPvfqyLTLHQpDKTRTEAVASALNEVAEALGLD---DKlgRSvNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGK 217
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGK 210
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-198 |
3.10e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRdwdAYRNNrIGFVfQSYNLIPH 97
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQG-VAMV-QQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELaltltgvGHAERRQRARKALEAVGLGEHVDKRP-----------SQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:PRK10790 429 DTFLANVTL-------GRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190
....*....|....*....|....*....|..
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARDRLVIMVTH 198
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-216 |
6.44e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 6.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKdfndrdwdayrnNRIGFVFQSYNLIPHQS 99
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL------------TNISDVHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 IL-------ENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGAL 172
Cdd:TIGR01257 2022 AIddlltgrEHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 173 DSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADG 216
Cdd:TIGR01257 2102 DPQARRMLWNTIVSIIREgRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-191 |
6.56e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRnnRIGFVFQSYNLIPHQ 98
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDIATRR--RVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSttsv 178
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP---- 430
|
170
....*....|...
gi 1469307064 179 qvmdllkdVARDR 191
Cdd:NF033858 431 --------VARDM 435
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-174 |
8.07e-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: 66.66 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 27 SFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfndrdwdAYRNNRIGFVFQSynliphqsileNVEL 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---------SYKPQYIKADYEG-----------TVRD 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 107 ALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:cd03237 81 LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-220 |
8.20e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLN-VIGGLDHFDsGDLLIDGistkdfndrdwdayrnnrigfvfqSYNLIPHQS 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVHMKG------------------------SVAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTgVGHAERRQRARKALEAVGLGEHVDKRPS-----------QLSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:TIGR00957 709 WIQNDSLRENIL-FGKALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 169 TGALDSTTSVQVMDLL---KDVARDRLVIMVTHNpeLAYRYATR-IVTLADGKITD 220
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHG--ISYLPQVDvIIVMSGGKISE 841
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-220 |
4.01e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 24 VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDwdayRNNRI--GFVF-----QSYNLIP 96
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALS----TAQRLarGLVYlpedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVeLALTLTGVGHAERRQRARKALE----AVGLG-EHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGA 171
Cdd:PRK15439 355 DAPLAWNV-CALTHNRRGFWIKPARENAVLEryrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 172 LDSTTSVQVMDLLKDVARDRL-VIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEISG 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-199 |
4.24e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 64.70 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQVALDSVslsfRDNEFVAILGPSGSGKTTMLNVIGG-----LDHFDSGDllidgistkdfndrDWD----AY 80
Cdd:cd03236 9 RYGPNSFKLHRLPVP----REGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPP--------------DWDeildEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 81 RNNRIGFVF--------------QSYNLIPHQsILENVELALTLTgvghaERRQRARKALEAVGLGEHVDKRPSQLSGGQ 146
Cdd:cd03236 71 RGSELQNYFtkllegdvkvivkpQYVDLIPKA-VKGKVGELLKKK-----DERGKLDELVDQLELRHVLDRNIDQLSGGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1469307064 147 MQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHN 199
Cdd:cd03236 145 LQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHD 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-198 |
5.33e-11 |
|
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: 66.73 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 34 VAILGPSGSGKTTMLNVIGG-----LDHFDsgdllidgistkdfNDRDWDA----YRNNRIGFVFQS-YN---------- 93
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGelkpnLGDYD--------------EEPSWDEvlkrFRGTELQDYFKKlANgeikvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 ---LIPHQ------SILENVElaltltgvghaeRRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:COG1245 168 yvdLIPKVfkgtvrELLEKVD------------ERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*
gi 1469307064 165 ADEPTGALDSTTSVQVMDLLKDVAR-DRLVIMVTH 198
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEH 270
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-215 |
7.48e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 24 VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLI-DGISTKDFNDRDWdayrNNRIGFVFQSyNLIPHQSILE 102
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWW----RSKIGVVSQD-PLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 103 NVELAL---------------------------------------------TLTGVGHAERRQRARKALEAVGLGEHV-- 135
Cdd:PTZ00265 479 NIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVSKKVli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 136 --------DK-------RPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVA--RDRLVIMVTH 198
Cdd:PTZ00265 559 hdfvsalpDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAH 638
|
250
....*....|....*..
gi 1469307064 199 NPElAYRYATRIVTLAD 215
Cdd:PTZ00265 639 RLS-TIRYANTIFVLSN 654
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-216 |
1.05e-10 |
|
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: 62.73 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIGFVFQSYNLIpHQSI 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELaltltgvGHAERRQRARKALEAVGLGEHVD-----------KRPSQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03290 96 EENITF-------GSPFNKQRYKAVTDACSLQPDIDllpfgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 170 GALDSTTSVQVMD--LLKDVARD-RLVIMVTHnpELAY-RYATRIVTLADG 216
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDkRTLVLVTH--KLQYlPHADWIIAMKDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-219 |
1.10e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGG-LDHFDS--GDLLIDGISTKDFNDRdwdaYRNNRIgFVFQSYNLIPH 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVSveGDIHYNGIPYKEFAEK----YPGEII-YVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTLTGvghaerrqrarkaleavglGEHVDKrpsqLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTS 177
Cdd:cd03233 98 LTVRETLDFALRCKG-------------------NEFVRG----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 178 ---VQVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:cd03233 155 leiLKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-167 |
1.33e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYVTQSFtqvALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYR 81
Cdd:PRK10522 323 LELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG---KPVTAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 nNRIGFVFQSYNLIPHqsilenvelalTLTGVGHAERRQRARKALEAVGLG---EHVDKRPS--QLSGGQMQRVAIARAL 156
Cdd:PRK10522 397 -KLFSAVFTDFHLFDQ-----------LLGPEGKPANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLAL 464
|
170
....*....|.
gi 1469307064 157 INDPEIVLADE 167
Cdd:PRK10522 465 AEERDILLLDE 475
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
952-1084 |
2.19e-10 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 64.84 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 952 ISLVLIAFVSISLVVSSIMI-GIITYiSVLERKKEIGILRAIGASKRNVANVFNAETF---IEGLIAgvfaivvvvavSL 1027
Cdd:TIGR03434 677 LALLLGLFAALALLLAAIGLyGVLAY-SVAQRTREIGIRMALGAQRGDVLRLVLRQGLrlaAAGLAI-----------GL 744
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 1028 PVnAWALAakqvpNLMS-----LPVQDALVLIAVSVLLTVV---AGLLPARSASKKDPVEALRSE 1084
Cdd:TIGR03434 745 AA-ALALA-----RLLAsllfgVSPTDPLTFAAVAALLLAVallACYLPARRAARVDPMIALRAE 803
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-224 |
3.24e-10 |
|
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: 64.05 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 24 VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNrigF--VFQSYNLIPHqsil 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG---QPVTADNREAYRQL---FsaVFSDFHLFDR---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 102 envelaltLTGVGHAERRQRARKALEAVGLGEHV---DKRPS--QLSGGQMQRVAIARALINDPEIVLADE--------- 167
Cdd:COG4615 421 --------LLGLDGEADPARARELLERLELDHKVsveDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdpef 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 168 ---------PtgaldsttsvqvmdLLKdvARDRLVIMVTHNPelayRY---ATRIVTLADGKITDDSDP 224
Cdd:COG4615 493 rrvfytellP--------------ELK--ARGKTVIAISHDD----RYfdlADRVLKMDYGKLVELTGP 541
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-224 |
3.49e-10 |
|
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: 60.89 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayrnnrigfVFQSYNLIPHQS 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-----------LRSSLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQrARKALEAVGLGEHvdkrpsqLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDEE-IYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 180 VMDLLKDVARDRLVIMVTHNPELAYRYAtRIVTLADGKITDDSDP 224
Cdd:cd03369 164 IQKTIREEFTNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-198 |
3.81e-10 |
|
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: 64.04 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 29 RDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLID-GISTK------DFNDRDWDAYRNNRIGFVFQSYnliphqsil 101
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlKISYKpqyispDYDGTVEEFLRSANTDDFGSSY--------- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 102 ENVELAltltgvghaerrqrarkalEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVM 181
Cdd:COG1245 435 YKTEII-------------------KPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170
....*....|....*....
gi 1469307064 182 DLLKDVA--RDRLVIMVTH 198
Cdd:COG1245 496 KAIRRFAenRGKTAMVVDH 514
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-201 |
6.69e-10 |
|
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: 61.41 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDsGDLLIDGISTKDFNDRDWDayrnnrigfvfQSYNLIPHQSI 100
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-----------KAFGVIPQKVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTLTGVGHaERRQRARKALEAVGLGEHVDKRPSQL-----------SGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03289 88 IFSGTFRKNLDPYGK-WSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|..
gi 1469307064 170 GALDSTTSVQVMDLLKDVARDRLVIMVTHNPE 201
Cdd:cd03289 167 AHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-218 |
9.15e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 13 TQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGG-LDHF---DSGDLLIDGISTKDFNDRdwdaYRNNRIgFV 88
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFhigVEGVITYDGITPEEIKKH----YRGDVV-YN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 89 FQSYNLIPHQSILENVELALTLTGVGH----AERRQRARK----ALEAVGLGEHVDKRPSQ-----LSGGQMQRVAIARA 155
Cdd:TIGR00956 144 AETDVHFPHLTVGETLDFAARCKTPQNrpdgVSREEYAKHiadvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEA 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 156 LINDPEIVLADEPTGALDSTTSVQVMDLLKDVAR--DRLVIMVTHNP-ELAYRYATRIVTLADGKI 218
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCsQDAYELFDKVIVLYEGYQ 289
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-216 |
2.25e-09 |
|
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: 59.87 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndrdwdayrnnRIGFVFQSYNLIPhQSI 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWIMP-GTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVelaltLTGVGHAERRQRArkALEAVGLGEHVDKRPSQ-----------LSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:cd03291 115 KENI-----IFGVSYDEYRYKS--VVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1469307064 170 GALDSTTSVQVMD--LLKDVArDRLVIMVTHNPElAYRYATRIVTLADG 216
Cdd:cd03291 188 GYLDVFTEKEIFEscVCKLMA-NKTRILVTSKME-HLKKADKILILHEG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-206 |
2.38e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDhfdsgdllidgistKDFNDRDWDAyRNNRIGFVFQSYNLIPHQSI 100
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD--------------KEFEGEARPA-PGIKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELaltltGVGH-------------------------AERRQRARKALEAVGLGEhVDKR----------P------ 139
Cdd:PRK11819 88 RENVEE-----GVAEvkaaldrfneiyaayaepdadfdalAAEQGELQEIIDAADAWD-LDSQleiamdalrcPpwdakv 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469307064 140 SQLSGGQMQRVAIARALINDPEIVLADEPTGALDStTSVQVMD-LLKDVARDrlVIMVTHNpelayRY 206
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-ESVAWLEqFLHDYPGT--VVAVTHD-----RY 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-210 |
2.78e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 6 VICKRYVTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIdGISTKdfndrdwdayrnnr 84
Cdd:TIGR03719 322 VIEAENLTKAFgDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 85 IGFVFQSY-NLIPHQSILENVELALTLTGVGHAERRQRARkaleaVGL----GEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:TIGR03719 387 LAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAY-----VGRfnfkGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVImvTHNPELAYRYATRI 210
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVI--SHDRWFLDRIATHI 510
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-221 |
4.69e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.76 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLN-VIGGLDHFDSGDLLIDGistkdfndrdwdayrnnRIGFVFQsYNLI 95
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-----------------SVAYVPQ-VSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 96 PHQSILENVELaltltgvGHAERRQRARKALEAVGLGEHVD-----------KRPSQLSGGQMQRVAIARALINDPEIVL 164
Cdd:PLN03232 691 FNATVRENILF-------GSDFESERYWRAIDVTALQHDLDllpgrdlteigERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 165 ADEPTGALDSTTSVQVMD-LLKDVARDRLVIMVTHN----PELayryaTRIVTLADGKITDD 221
Cdd:PLN03232 764 FDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTNQlhflPLM-----DRIILVSEGMIKEE 820
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-223 |
8.10e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLlidgistkdfndrdwdaYRNNRIGFVFQSYNLIPHQS 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------------DRNGEVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1469307064 180 VMDLLKDV-ARDRLVIMVTHNPELAYRYATRIVTLADGKITDDSD 223
Cdd:PRK13546 182 CLDKIYEFkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
10-221 |
1.10e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.21 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 10 RYVTQSFTQV-ALDSVSLSFRDNEFVAILGPSGSG--KTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDWDAYRNNRIG 86
Cdd:NF000106 17 RGLVKHFGEVkAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 87 FVfQSYnliphqSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:NF000106 97 RR-ESF------SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIVTLADGKITDD 221
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-226 |
1.47e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 2 LDLRVICKRYvtQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayr 81
Cdd:TIGR00957 1285 VEFRNYCLRY--REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD----- 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 82 nnrigFVFQsYNLIPHQSILENVELALTLTGVGHAERrQRARKALEAVGLGEHVDKRPSQL-----------SGGQMQRV 150
Cdd:TIGR00957 1358 -----LRFK-ITIIPQDPVLFSGSLRMNLDPFSQYSD-EEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLV 1430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 151 AIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELAYRYaTRIVTLADGKITDDSDPFD 226
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSN 1505
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-199 |
2.40e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 29 RDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLID-GISTK------DFNDRDWDAYRNNRIGFvfqsynlipHQSIL 101
Cdd:PRK13409 363 YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElKISYKpqyikpDYDGTVEDLLRSITDDL---------GSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 102 eNVELALTLtgvghaerrqrarkaleavGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVM 181
Cdd:PRK13409 434 -KSEIIKPL-------------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180
....*....|....*....|
gi 1469307064 182 DLLKDVA--RDRLVIMVTHN 199
Cdd:PRK13409 494 KAIRRIAeeREATALVVDHD 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-216 |
2.66e-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: 58.38 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGldhfdsgdllidgistkDFNDRDWDAYRNNRIGFVFQSYNLIPhQSI 100
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG-----------------ELEPSEGKIKHSGRISFSPQTSWIMP-GTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVelaltLTGVGHAERRQRArkALEAVGLGEHVDKRPSQ-----------LSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:TIGR01271 504 KDNI-----IFGLSYDEYRYTS--VIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1469307064 170 GALDSTTSVQVMD-LLKDVARDRLVIMVTHNPELAYRyATRIVTLADG 216
Cdd:TIGR01271 577 THLDVVTEKEIFEsCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-200 |
2.70e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 17 TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGG---LDHFDSGDLLIDGistkdfndRDWDAYRNNRIGFVFQSYN 93
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNG--------RPLDSSFQRSIGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPHQSILENVELALTL---TGVGHAERRQRARKALEAVGLGEHVDK----RPSQLSGGQMQRVAIARALINDPE-IVLA 165
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKlLLFL 926
|
170 180 190
....*....|....*....|....*....|....*.
gi 1469307064 166 DEPTGALDSTTSVQVMDLLKDVARDRLVIMVT-HNP 200
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQP 962
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
934-1084 |
2.72e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 934 YTDYMGIIMGSVTDIVNTISLVLIAFVSISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAET----FI 1009
Cdd:PRK10535 503 FTWNMDSVLKTAEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTREIGIRMAVGARASDVLQQFLIEAvlvcLV 582
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 1010 EGLIAGVFAIVVVVAVSLPVNAWALAAKQVPNLMSLpvqdalvliAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:PRK10535 583 GGALGITLSLLIAFTLQLFLPGWEIGFSPLALLSAF---------LCSTVTGILFGWLPARNAARLDPVDALARE 648
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-219 |
3.93e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 15 SFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFVFQ---- 90
Cdd:PRK10982 258 SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNANEAINHGFALVTEerrs 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 ----SYNLIPHQSILENVELALTLTGVGHAERRQRARK-ALEAVGLgehvdKRPSQ------LSGGQMQRVAIARALIND 159
Cdd:PRK10982 335 tgiyAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQwVIDSMRV-----KTPGHrtqigsLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 160 PEIVLADEPTGALDSTTSVQVMDLLKDVA-RDRLVIMVTHN-PELaYRYATRIVTLADGKIT 219
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEmPEL-LGITDRILVMSNGLVA 470
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-198 |
5.28e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfnDRDWDAYRnNRIGFVFQSYNLIPH 97
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENV--ELALTLTGVGHAErrqrarkALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDST 175
Cdd:PRK13540 89 LTLRENClyDIHFSPGAVGITE-------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....
gi 1469307064 176 TSVQVMDLLKD-VARDRLVIMVTH 198
Cdd:PRK13540 162 SLLTIITKIQEhRAKGGAVLLTSH 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-173 |
7.29e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 7.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 5 RVICKRYVTQSFTQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGlDHFD--SGDLLIdgistkdFNDRD------ 76
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgySNDLTL-------FGRRRgsgeti 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 77 WDAYRNnrIGFVFQSYNLIPHQSI-LENVELALTLTGVG---HAERRQR--ARKALEAVGLGEHVDKRPSQ-LSGGQMQR 149
Cdd:PRK10938 332 WDIKKH--IGYVSSSLHLDYRVSTsVRNVILSGFFDSIGiyqAVSDRQQklAQQWLDILGIDKRTADAPFHsLSWGQQRL 409
|
170 180
....*....|....*....|....
gi 1469307064 150 VAIARALINDPEIVLADEPTGALD 173
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-221 |
7.59e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 33 FVAILGPSGSGKTTMLN-VIGGLDHFDSGDLLIDGistkdfndrdwdayrnnRIGFVFQsYNLIPHQSILENVELALTLt 111
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-----------------TVAYVPQ-VSWIFNATVRDNILFGSPF- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 112 gvgHAERRQRA------RKALEAVGLGEHVD--KRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMD- 182
Cdd:PLN03130 706 ---DPERYERAidvtalQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDk 782
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1469307064 183 LLKDVARDRLVIMVTHnpELAY-RYATRIVTLADGKITDD 221
Cdd:PLN03130 783 CIKDELRGKTRVLVTN--QLHFlSQVDRIILVHEGMIKEE 820
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-173 |
7.96e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistKDFNDRD-WDAYRNnriGFVFQSYN-----L 94
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSpQDGLAN---GIVYISEDrkrdgL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 95 IPHQSILENvelaLTLTGVGHAERRQ-RARKALEAVGLGEHVD----KRPSQ------LSGGQMQRVAIARALINDPEIV 163
Cdd:PRK10762 342 VLGMSVKEN----MSLTALRYFSRAGgSLKHADEQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 1469307064 164 LADEPTGALD 173
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-176 |
1.10e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdaYRNNrIGFVFQS--------- 91
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKV-LGIIPQApvlfsgtvr 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIP---HQ--SILENVELAltltgvgHAERRQRaRKALeavGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLAD 166
Cdd:PLN03130 1331 FNLDPfneHNdaDLWESLERA-------HLKDVIR-RNSL---GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170
....*....|
gi 1469307064 167 EPTGALDSTT 176
Cdd:PLN03130 1400 EATAAVDVRT 1409
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-201 |
1.27e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDsGDLLIDGISTKDFNDRDWDayrnnrigfvfQSYNLIPHQSI 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWR-----------KAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTLTgvGHAE-RRQRARKALEAVGLGEHVDKRPSQ-----------LSGGQMQRVAIARALINDPEIVLADEP 168
Cdd:TIGR01271 1303 IFSGTFRKNLD--PYEQwSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190
....*....|....*....|....*....|...
gi 1469307064 169 TGALDSTTSVQVMDLLKDVARDRLVIMVTHNPE 201
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-221 |
1.52e-07 |
|
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: 55.22 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVI-GGLDHFDSGDLLIDGistKDFNDRDWDAYRNNRIGFVFQS---YNLIP 96
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFING---KPVDIRNPAQAIRAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 97 HQSILENVELAL-----TLTGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:TIGR02633 353 ILGVGKNITLSVlksfcFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDRLVIMVThNPELA--YRYATRIVTLADGKITDD 221
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVV-SSELAevLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-221 |
2.02e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 22 DSVSLSFRDNEFVAILGPSGSGKTTMLNVI-GGLDHFDSGDLLIDGISTKDFNDRDwdAYRNNrIGFVFQS---YNLIPH 97
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQG-IAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVelalTLTGVGHAERRQRARKALEAVGLGEHVD----KRPS------QLSGGQMQRVAIARALINDPEIVLADE 167
Cdd:PRK13549 356 MGVGKNI----TLAALDRFTGGSRIDDAAELKTILESIQrlkvKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 168 PTGALDSTTSVQVMDLLKDVARDRL-VIMVTHN-PELaYRYATRIVTLADGKITDD 221
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVaIIVISSElPEV-LGLSDRVLVMHEGKLKGD 486
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-224 |
2.11e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdayrnnrigfVFQSYNLIPHQSI 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-----------LRRVLSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 101 LENVELALTL--------TGVGHAERRQRARKALE--AVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTG 170
Cdd:PLN03232 1321 LFSGTVRFNIdpfsehndADLWEALERAHIKDVIDrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 171 ALDSTTSVQVMDLLKDVARDRLVIMVTHnpelayRYAT-----RIVTLADGKITDDSDP 224
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAH------RLNTiidcdKILVLSSGQVLEYDSP 1453
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-202 |
3.55e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.72 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFD--SGDLLIDGistKDFNDRDWDAYRNNRIGFVFQSYNLIPHQ 98
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKG---ESILDLEPEERAHLGIFLAFQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALtltgvgHAERRQRARKALEAVGLGEH-------VDKRPSQL--------SGGQMQRVAIARALINDPEIV 163
Cdd:CHL00131 100 SNADFLRLAY------NSKRKFQGLPELDPLEFLEIineklklVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1469307064 164 LADEPTGALDsttsvqvMDLLKDVA--------RDRLVIMVTHNPEL 202
Cdd:CHL00131 174 ILDETDSGLD-------IDALKIIAeginklmtSENSIILITHYQRL 213
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-202 |
5.14e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDH--FDSGDLLIDGISTKDfndrdwDAYRnnRI-GFVFQSYNLIPH 97
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQ------ETFA--RIsGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVELALTL---TGVGHAERRQRARKALEAVGLGEHVDK---RP--SQLSGGQMQRVAIARALINDPEIVLADEPT 169
Cdd:PLN03140 968 VTVRESLIYSAFLrlpKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190
....*....|....*....|....*....|....
gi 1469307064 170 GALDSTTSVQVMDLLKD-VARDRLVIMVTHNPEL 202
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSI 1081
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-203 |
6.87e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 25 SLSFRDNEFVAILGPSGSGKTTMLNVIGgldhfdsgdlLIDGISTKDFNDRdwdayrnnrigfvfqSYNLIPHQSILENV 104
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG----------LALGGAQSATRRR---------------SGVKAGCIVAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 105 ELALTLTgvghaerrqrarkaleavglgehvdkrpsQLSGGQMQRVAIARALIN-----DPEIVLaDEPTGALDSTTSVQ 179
Cdd:cd03227 70 ELIFTRL-----------------------------QLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQA 119
|
170 180
....*....|....*....|....*
gi 1469307064 180 VMDLLKD-VARDRLVIMVTHNPELA 203
Cdd:cd03227 120 LAEAILEhLVKGAQVIVITHLPELA 144
|
|
| YbbP |
COG3127 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease ... |
954-1084 |
3.24e-06 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442361 [Multi-domain] Cd Length: 830 Bit Score: 51.34 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 954 LVLIAFvsISLVVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAETFIEGLIagvfaivvvvaVS------- 1026
Cdd:COG3127 256 LLLVAL--LALLLAGVAVANAARRYVARRLDTIALLRCLGASRRQIFRIYLLQLLLLGLL-----------GSllglllg 322
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469307064 1027 --LPVNAWALAAKQVPNLMSLPV--QDALVLIAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:COG3127 323 alLQALLAALLADLLPVPLEPALspLPLLLGLLVGLLVLLLFALPPLLRLRRVPPLRVLRRD 384
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-216 |
3.35e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.47 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGgldhFDSGDLLIDGISTKdfndrdwdaYRNNRIGFVFQSYNLIphqs 99
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL----YASGKARLISFLPK---------FSRNKLIFIDQLQFLI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ilenvelaltltgvghaerrqrarkaleAVGLGEHVDKRP-SQLSGGQMQRVAIARALINDPE--IVLADEPTGALDSTT 176
Cdd:cd03238 73 ----------------------------DVGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 177 SVQVMDLLKD-VARDRLVIMVTHNPELAyRYATRIVTLADG 216
Cdd:cd03238 125 INQLLEVIKGlIDLGNTVILIEHNLDVL-SSADWIIDFGPG 164
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-219 |
6.66e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.17 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKT-TMLNVIG---GldHFDSGDLLIDG--ISTKDFNDrdwdAYRNNrIGFVFQ---S 91
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyG--RNISGTVFKDGkeVDVSTVSD----AIDAG-LAYVTEdrkG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 92 YNLIPHQSILENVELAlTLTGV-------GHAERR--QRARKAL--EAVGLGEHVDKrpsqLSGGQMQRVAIARALINDP 160
Cdd:NF040905 349 YGLNLIDDIKRNITLA-NLGKVsrrgvidENEEIKvaEEYRKKMniKTPSVFQKVGN----LSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 161 EIVLADEPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHN-PELaYRYATRIVTLADGKIT 219
Cdd:NF040905 424 DVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSElPEL-LGMCDRIYVMNEGRIT 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-220 |
7.70e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 12 VTQSF-TQVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGldhfdsgDLLIDGISTKdfndrdWDayRNNRIGFVFQ 90
Cdd:PRK15064 325 LTKGFdNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-------ELEPDSGTVK------WS--ENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 91 SynlipHQSILENvelALTL-------TGVGHAErrQRARKALeavGL----GEHVDKRPSQLSGGQMQRVAIARALIND 159
Cdd:PRK15064 390 D-----HAYDFEN---DLTLfdwmsqwRQEGDDE--QAVRGTL---GRllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469307064 160 PEIVLADEPTGALDsTTSVQVMDLLKDVARDRLvIMVTHNPELAYRYATRIVTLADGKITD 220
Cdd:PRK15064 457 PNVLVMDEPTNHMD-MESIESLNMALEKYEGTL-IFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-218 |
7.87e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGdllidgistkdfndRDWDAyrnnrigfvfQSYNLIPH 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--------------RVWAE----------RSIAYVPQ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILENVelalTLTG---VGHAERRQRARKA-----LEA------VGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIV 163
Cdd:PTZ00243 729 QAWIMNA----TVRGnilFFDEEDAARLADAvrvsqLEAdlaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1469307064 164 LADEPTGALDSTTSVQVM-DLLKDVARDRLVIMVTHNPELAYRyATRIVTLADGKI 218
Cdd:PTZ00243 805 LLDDPLSALDAHVGERVVeECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-221 |
9.83e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 24 VSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTKDFNDRDwdAYRNnriGFVF-----QSYNLIPHQ 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD--AIRA---GIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELA---------LTLTGVGHAERRQRARKALEAvglgehvdKRPS------QLSGGQMQRVAIARALINDPEIV 163
Cdd:PRK11288 347 SVADNINISarrhhlragCLINNRWEAENADRFIRSLNI--------KTPSreqlimNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 164 LADEPTGALDSTTSVQVMDLLKDVA-RDRLVIMVTHN-PELaYRYATRIVTLADGKITDD 221
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDlPEV-LGVADRIVVMREGRIAGE 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-174 |
2.86e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 28 FRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfndrdwdAYRNNRIgfvfqsynliphqsilenvela 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP---------VYKPQYI---------------------- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469307064 108 ltltgvghaerrqrarkaleavglgehvdkrpsQLSGGQMQRVAIARALINDPEIVLADEPTGALDS 174
Cdd:cd03222 71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| FtsX |
COG2177 |
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning]; |
887-1067 |
3.45e-05 |
|
Cell division protein FtsX [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 441780 [Multi-domain] Cd Length: 292 Bit Score: 47.13 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 887 LGYADEADPISVKIFPRDFE--AKERVLDHIDAYNKQVKAaghdEQAISYTDYMGIIMGSVTDIVNTISLVLIAFVSISL 964
Cdd:COG2177 103 LGESDLLELLDENPLPASIEvkLKPEDPEDLEALAAALEA----LPGVAEVDYDREWVERLFALLNLLRLVGLVLAALLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 965 VVSSIMIGIITYISVLERKKEIGILRAIGASKRNVANVFNAETFIEGLI------AGVFAIVVVVAVSLpvnAWALAAKQ 1038
Cdd:COG2177 179 LAAVLLIGNTIRLAIYSRREEIEIMKLVGATDGFIRRPFLLEGALLGLLggllalLLLALLYLLLVSAL---ADGLAFLS 255
|
170 180
....*....|....*....|....*....
gi 1469307064 1039 VPNLMSLPVQDALVLIAVSVLLTVVAGLL 1067
Cdd:COG2177 256 LLSLGGLLLLLLLLLLLLGALLGALGSRL 284
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-182 |
5.00e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 20 ALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGISTkdfndrdwdayrnnrigFVFQSYNLIPHQS 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAA-----------------LIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 100 ILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQ 179
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
...
gi 1469307064 180 VMD 182
Cdd:PRK13545 182 CLD 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-225 |
5.06e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 34 VAILGPSGSGKTTMLNVIGGLDHFDSGDLlidgistkdfndrdwdaYRNNRIGFVFQSYNLIPHQSILENVELALTLTGV 113
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 114 GHAERRQRARkaLEAVGLGEHVDKRPS-QLSGGQMQRVAIARALINDPEIVLADEPTGALDsttsvqvMDLLKDVARDRL 192
Cdd:PLN03073 601 GVPEQKLRAH--LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-------LDAVEALIQGLV 671
|
170 180 190
....*....|....*....|....*....|....*...
gi 1469307064 193 -----VIMVTHNPELAYRYATRIVTLADGKITddsdPF 225
Cdd:PLN03073 672 lfqggVLMVSHDEHLISGSVDELWVVSEGKVT----PF 705
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-202 |
1.02e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 46.28 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 18 QVALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDgistkdfndrdwdayRNNRIGFVFQ----SYN 93
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFYVPQrpymTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 94 LIPHQSILENVELALTLTGVGHAERRQrarkALEAVGLgEHVDKRP----------SQLSGGQMQRVAIARALINDPEIV 163
Cdd:TIGR00954 530 TLRDQIIYPDSSEDMKRRGLSDKDLEQ----ILDNVQL-THILEREggwsavqdwmDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 164 LADEPTGALdsttSVQVMDLLKDVARDRLV--IMVTHNPEL 202
Cdd:TIGR00954 605 ILDECTSAV----SVDVEGYMYRLCREFGItlFSVSHRKSL 641
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
19-219 |
1.60e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 44.28 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 19 VALDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLidgistkdfndrdwdAYRNNRIGFVFQSYnLIPHQ 98
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI---------------GLRGDALPLGANSF-ILPGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALTLTGVGHAERRQRARKALEavgLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSV 178
Cdd:PRK15177 65 TGEENARMMASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 179 QVMDLLKDVARDRLVIMVTHNPELAYRYATRIVTLADGKIT 219
Cdd:PRK15177 142 RMQAALACQLQQKGLIVLTHNPRLIKEHCHAFGVLLHGKIT 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-226 |
2.43e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 137 KRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLkdVARDRLVIMVTHNPELAYRYATRIVTLADG 216
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
90
....*....|...
gi 1469307064 217 KITD---DSDPFD 226
Cdd:PLN03073 418 KLVTykgDYDTFE 430
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-202 |
6.78e-04 |
|
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: 42.21 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 22 DSVSLSFRDnEFVAILGPSGSGKTTmlnviggldhfdsgdlLIDGISTKDFndrdWDAYRNNRIGFVFQSynLIPHQSIL 101
Cdd:cd03240 14 ERSEIEFFS-PLTLIVGQNGAGKTT----------------IIEALKYALT----GELPPNSKGGAHDPK--LIREGEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 102 ENVELALTLTGvGHAERRQRARKALEAVG----------LGEHVDkrpsQLSGGQ------MQRVAIARALINDPEIVLA 165
Cdd:cd03240 71 AQVKLAFENAN-GKKYTITRSLAILENVIfchqgesnwpLLDMRG----RCSGGEkvlaslIIRLALAETFGSNCGILAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1469307064 166 DEPTGALDSTTS----VQVMDLLKdVARDRLVIMVTHNPEL 202
Cdd:cd03240 146 DEPTTNLDEENIeeslAEIIEERK-SQKNFQLIVITHDEEL 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-226 |
7.90e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDL-LIDGIstkdfndrdwdayrnnRIGFVFQsynlipHQ- 98
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI----------------KLGYFAQ------HQl 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SILENVELALT-LTGVGHAERRQRARKALEAVGL-GEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTT 176
Cdd:PRK10636 386 EFLRADESPLQhLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1469307064 177 SVQVMDLLKDVarDRLVIMVTHNPELAYRYATRIVTLADGKItddsDPFD 226
Cdd:PRK10636 466 RQALTEALIDF--EGALVVVSHDRHLLRSTTDDLYLVHDGKV----EPFD 509
|
|
| PRK10814 |
PRK10814 |
lipoprotein-releasing ABC transporter permease subunit LolC; |
962-1084 |
1.07e-03 |
|
lipoprotein-releasing ABC transporter permease subunit LolC;
Pssm-ID: 182753 [Multi-domain] Cd Length: 399 Bit Score: 42.77 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 962 ISLVVSSIMIGIITYIS--VLERKKEIGILRAIGASKRNVANVFNAETFIEGLIAGVfaivvvvavsLPVNAWALAAKQV 1039
Cdd:PRK10814 271 LSLIVAVAAFNIITSLGllVMEKQGEVAILQTQGLTRRQIMMVFMVQGASAGIIGAL----------LGALLGALLASQL 340
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 1040 PNLM----------SLPVQ-DAL--VLIAVS-VLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:PRK10814 341 NNLMpiigvlldgaALPVAiEPLqvIVIALVaMAIALLSTLYPSWRAAATQPAEALRYE 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-203 |
1.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469307064 137 KRPSQLSGG-QMQ-----RVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVIMVTHNPELA 203
Cdd:COG4717 554 RPVEELSRGtREQlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELV 626
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
26-211 |
1.72e-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: 41.10 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 26 LSFRD---NEFVAILGPSGSGKTTMlnviggldhFDSGDLLIDGISTKDFNDRDWDAYRNN-----RIGFVFQSYNLIpH 97
Cdd:cd03279 20 IDFTGldnNGLFLICGPTGAGKSTI---------LDAITYALYGKTPRYGRQENLRSVFAPgedtaEVSFTFQLGGKK-Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 98 QSILEnvelaltltgvGHAERRQRARKALEAVGLGEHVDKRP-SQLSGGQMQRVAIARAL------INDPEIVLA----D 166
Cdd:cd03279 90 RVERS-----------RGLDYDQFTRIVLLPQGEFDRFLARPvSTLSGGETFLASLSLALalsevlQNRGGARLEalfiD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1469307064 167 EPTGALDSTTSVQVMDLLKDVARD-RLVIMVTHNPELAYRYATRIV 211
Cdd:cd03279 159 EGFGTLDPEALEAVATALELIRTEnRMVGVISHVEELKERIPQRLE 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-219 |
1.75e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 115 HAERRQRARKALEAVGLGEHVDKRPSQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRLVI 194
Cdd:PRK10938 109 EVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
90 100 110
....*....|....*....|....*....|
gi 1469307064 195 MVTHN-----PElayrYATRIVTLADGKIT 219
Cdd:PRK10938 189 VLVLNrfdeiPD----FVQFAGVLADCTLA 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-181 |
2.64e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHFDSGDLLIDGistkdfndRDWDAY--RNNRigfvfQSYNLIPHQ 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG--------REIGAYglRELR-----RQFSMIPQD 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 SIL------ENVELALTLTGvghAErrqrARKALEAVGLGEHV-------DKR----PSQLSGGQMQRVAIARALIN-DP 160
Cdd:PTZ00243 1393 PVLfdgtvrQNVDPFLEASS---AE----VWAALELVGLRERVasesegiDSRvlegGSNYSVGQRQLMCMARALLKkGS 1465
|
170 180
....*....|....*....|....*
gi 1469307064 161 EIVLADEPTG----ALDSTTSVQVM 181
Cdd:PTZ00243 1466 GFILMDEATAnidpALDRQIQATVM 1490
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-203 |
2.65e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNeFVAILGPSGSGKTTMLNVIggldhfdsgDLLIDG-----ISTKDFNDRDWDAYRNNRIGFVFQSY--- 92
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEAL---------RLLLGPsssrkFDEEDFYLGDDPDLPEIEIELTFGSLlsr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 93 --NLIPHQSILENVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRP----------------------------SQL 142
Cdd:COG3593 84 llRLLLKEEDKEELEEALEELNEELKEALKALNELLSEYLKELLDGLDLelelsldeledllkslslriedgkelplDRL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 143 SGGQMQRVAIA--RALI-----NDPEIVLADEPTGALDSTTSVQVMDLLKDVARDRL-VIMVTHNPELA 203
Cdd:COG3593 164 GSGFQRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTHSPHLL 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-223 |
3.13e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 21 LDSVSLSFRDNEFVAILGPSGSGKTTMLNVIGGLDHF--DSGDLLIDGistKDFNDRDWDAYRNNRIGFVFQSYNLIPhq 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKG---KDLLELSPEDRAGEGIFMAFQYPVEIP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 99 sileNVELALTLTGVGHAERRQRARKALEAVGLGEHVDKRPSQL---------------SGGQMQRVAIARALINDPEIV 163
Cdd:PRK09580 92 ----GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469307064 164 LADEPTGALDsttsvqvMDLLKDVA------RD--RLVIMVTHNPE-LAYRYATRIVTLADGKITDDSD 223
Cdd:PRK09580 168 ILDESDSGLD-------IDALKIVAdgvnslRDgkRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSGD 229
|
|
| ADOP |
TIGR03434 |
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ... |
1033-1084 |
4.24e-03 |
|
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.
Pssm-ID: 274576 [Multi-domain] Cd Length: 803 Bit Score: 41.34 E-value: 4.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1469307064 1033 ALAAKQVPNLMSLPVqDALVL---IAVSVLLTVVAGLLPARSASKKDPVEALRSE 1084
Cdd:TIGR03434 349 ALLPASLPRLLEISL-DGRVLlfaLALSLLTGLLFGLAPALQATRSDLAEALKEG 402
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
130-202 |
8.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 130 GLGEHVDkrpsQLSGGQMQ------RVAIARALINDPEIVLADEPTGALDSTTSVQVMDL----LKDVARDRLVIMVTHN 199
Cdd:PRK01156 794 GMVEGID----SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDIPQVIMISHH 869
|
...
gi 1469307064 200 PEL 202
Cdd:PRK01156 870 REL 872
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
121-198 |
8.54e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469307064 121 RARKALEAVGLGEHVDKRP-SQLSGGQMQRVAIARALINDPEIVLADEPTGALDSTTsvqvMDLLKDV--ARDRLVIMVT 197
Cdd:PRK15064 134 RAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVlnERNSTMIIIS 209
|
.
gi 1469307064 198 H 198
Cdd:PRK15064 210 H 210
|
|
| |
