|
Name |
Accession |
Description |
Interval |
E-value |
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-229 |
1.23e-130 |
|
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: 367.91 E-value: 1.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPpILQVEGYGKHFQLHEQN-KLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmGHELD 79
Cdd:COG4778 1 MTT-LLEVENLSKTFTLHLQGgKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHD-GGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 80 LVLASEHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGER 159
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELAPP 229
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
5-228 |
1.83e-108 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 311.63 E-value: 1.83e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQN-KLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdAMGHELDLVLA 83
Cdd:TIGR02324 1 LLEVEDLSKTFTLHQQGgVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVR-HEGAWVDLAQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 SEHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVN 163
Cdd:TIGR02324 80 SPREVLEVRRKTIGYVSQFLRVIPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELAP 228
Cdd:TIGR02324 160 IARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELVADRVMDVTP 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-226 |
8.85e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.52 E-value: 8.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGYGKHFQLHEQNklIPSSHNVSFTVRAGELTALIGPTGAGKS---SVLKGIYRtylPSAGRILYRDAmghelD 79
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE--VTALRGVSLSIEAGEFVAIVGPSGSGKStllNILGGLDR---PTSGEVLIDGQ-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 80 LVLASEHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGER 159
Cdd:COG1136 72 ISSLSERELARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRL-DHRPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAAR-ADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-226 |
1.11e-49 |
|
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: 161.89 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHelDLVLASE 85
Cdd:cd03255 1 IELKNLSKTY--GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV---DGT--DISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 HQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLA 165
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 166 RGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRlADQVVEL 226
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIEL 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-226 |
1.10e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 156.75 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHelDLVLASEHQILELRRReIGFVTQFLHCLP 107
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV---NGQ--DLSRLKRREIPYLRRR-IGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:COG2884 93 DRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKAL-PHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:COG2884 172 TSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-232 |
2.63e-47 |
|
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: 163.54 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGYGKHFQLHEQNKlIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVL 82
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGG-VRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGK-----DLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 83 ASEHQILELRRReIGFVTQF-LHCL-PRQATLDVVAQPLFALGV-SRDVARQRAAELLSAMKLPERLWSVSPATFSGGER 159
Cdd:COG1123 332 LSRRSLRELRRR-VQMVFQDpYSSLnPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV--------VELAPPP 230
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVavmydgriVEDGPTE 490
|
..
gi 1706422447 231 AV 232
Cdd:COG1123 491 EV 492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-224 |
2.78e-44 |
|
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: 148.42 E-value: 2.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFqlHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELdlvLAS 84
Cdd:cd03257 1 LLEVKNLSVSF--PTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIF---DGKDL---LKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRREIGFVTQ-FLHCL-PRQATLDVVAQPLFALGVSRDVARQRAA--ELLSAMKLPERLWSVSPATFSGGERQ 160
Cdd:cd03257 73 SRRLRKIRRKEIQMVFQdPMSSLnPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
5-226 |
2.02e-43 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 145.96 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQlhEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDLvlAS 84
Cdd:TIGR02211 1 LLKCENLGKRYQ--EGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLF---NGQSLSK--LS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNL 164
Cdd:TIGR02211 74 SNERAKLRNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLaDQVVEL 226
Cdd:TIGR02211 153 ARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRElNTSFLVVTHDLELAKKL-DRVLEM 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-227 |
4.27e-42 |
|
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: 142.96 E-value: 4.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEQNKLIpsSHNVSFTVRAGELTALIGPTGAGKSS---VLKGIYRtylPSAGRILyrdAMGHE 77
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTI--LKGISLEVEAGESVAIVGASGSGKSTllgLLAGLDR---PTSGTVR---LAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 LDLVlaSEHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGvsRDVARQRAAELLSAMKLPERLwSVSPATFSGG 157
Cdd:COG4181 76 LFAL--DEDARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRL-DHYPAQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRlADQVVELA 227
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLR 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-227 |
4.60e-42 |
|
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: 142.86 E-value: 4.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRDamgheLDLvlaSEHQILELRRReIGFVTQFlh 104
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLK---PTSGEVLVDG-----KDI---TKKNLRELRRK-VGLVFQN-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clPRQ----AT-LDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:COG1122 84 --PDDqlfaPTvEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLD 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
28-226 |
3.61e-41 |
|
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: 139.91 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlVLASEHQILELRRReIGFV-----TQF 102
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG--------KDLTKLSLKELRRK-VGLVfqnpdDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRqatlDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:cd03225 89 FGPTVE----EEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 183 SLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-182 |
7.10e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 137.01 E-value: 7.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDlvlaseHQILELRRREIGFVTQFLHCLP 107
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD---GQDLT------DDERKSLRKEIGYVFQDPQLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPE---RLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-227 |
8.89e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.84 E-value: 8.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVE----GYGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgh 76
Cdd:COG1121 2 MMMPAIELEnltvSYGGRPVLE----------DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 77 eldlvlasehQILELRRREIGFVTQFLHcLPRQ--AT-LDVVAQPLFA----LGVSRDVARQRAAELLSAMKLpERLWSV 149
Cdd:COG1121 68 ----------KPPRRARRRIGYVPQRAE-VDWDfpITvRDVVLMGRYGrrglFRRPSRADREAVDEALERVGL-EDLADR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 150 SPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:COG1121 136 PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-235 |
1.75e-40 |
|
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: 139.17 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELdlvlasEHQILELRRREIGFVTQ----FL 103
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD---GRPV------TRRRRKAFRRRVQMVFQdpyaSL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HclPRQATLDVVAQPLFALGvsRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:COG1124 93 H--PRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 184 LDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVEEL 235
Cdd:COG1124 169 LDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
28-224 |
2.18e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDlvlaseHQILELRRReIGFVTQFLHCLP 107
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV---LGEDVA------RDPAEVRRR-IGYVPQEPALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 R---QATLDVVAQplfALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSL 184
Cdd:COG1131 87 DltvRENLRFFAR---LYGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 185 DPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-223 |
1.06e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 136.87 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQlhEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDL 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQ--EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN---GQPMSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQilELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSvSPATFSGGERQ 160
Cdd:PRK11629 76 LSSAAKA--ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANH-RPSELSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
28-228 |
1.63e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlVLASEHQILELRRReIGFVTQflhclp 107
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDG--------KPLSAMPPPEWRRQ-VAYVPQ------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATL------DVVAQPLFALGVSRDvaRQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:COG4619 82 -EPALwggtvrDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 182 SSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAP 228
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-234 |
2.01e-39 |
|
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: 142.35 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLHEqnklIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPSAGRILYRdAMGHELDLVLA 83
Cdd:COG1123 3 PLLEVRDLSVRYPGGD----VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGE-VLLDGRDLLEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 SEHqileLRRREIGFVTQ-FLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRV 162
Cdd:COG1123 77 SEA----LRGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 163 NLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
28-226 |
4.29e-39 |
|
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: 134.68 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHelDLVLASEHQILELRRReIGFVTQFLHCLP 107
Cdd:TIGR02673 19 HDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI---AGE--DVNRLRGRQLPLLRRR-IGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:TIGR02673 93 DRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKA-DAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:TIGR02673 172 LSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIIL 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
28-224 |
1.32e-38 |
|
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: 133.42 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDlvlASEHQILELRRReIGFVTQFLHCLP 107
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID---GLKLT---DDKKNINELRQK-VGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:cd03262 90 HLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDP 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 187 ATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03262 169 ELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-238 |
4.22e-37 |
|
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: 132.48 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHeqNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLP---SAGRILYRDAmghelDLV 81
Cdd:COG0444 1 LLEVRNLKVYFPTR--RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGE-----DLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 82 LASEHQILELRRREIGFVTQ-FLHCL-PRQATLDVVAQPLFA-LGVSRDVARQRAAELLSAMKLP---ERLWSVsPATFS 155
Cdd:COG0444 74 KLSEKELRKIRGREIQMIFQdPMTSLnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRY-PHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 156 GGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLAD--------QVVEL 226
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADrvavmyagRIVEE 232
|
250
....*....|..
gi 1706422447 227 APppaVEELLEE 238
Cdd:COG0444 233 GP---VEELFEN 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
28-219 |
1.11e-36 |
|
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: 129.43 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdaMGHELDLVlasehQILELRRReIGFVTQFLH-CL 106
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRL--FGERRGGE-----DVWELRKR-IGLVSPALQlRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQAT-LDVVAQPLFA-LGVSR---DVARQRAAELLSAM---KLPERLWsvspATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG1119 92 PRDETvLDVVLSGFFDsIGLYReptDEQRERARELLELLglaHLADRPF----GTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAEG-TAMLAIFHH-----PETTRRL 219
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHveeipPGITHVL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
28-224 |
1.56e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.57 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDlvlASEHQILELRRReIGFVTQ----FL 103
Cdd:COG1126 18 KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD---GEDLT---DSKKDINKLRRK-VGMVFQqfnlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HclprqAT-LD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:COG1126 91 H-----LTvLEnVTLAPIKVKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 182 SSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:COG1126 165 SALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
28-239 |
1.63e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.02 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgHELDLVLASEHQILELRRReIGFVTQFLHCLP 107
Cdd:COG3638 20 DDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV-----DGQDVTALRGRALRRLRRR-IGMIFQQFNLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVV------AQPLFA--LGVSRDVARQRAAELLSAMKLPERLWSvsPA-TFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG3638 94 RLSVLTNVlagrlgRTSTWRslLGLFPPEDRERALEALERVGLADKAYQ--RAdQLSGGQQQRVAIARALVQEPKLILAD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 179 EPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVVELA--------PPPAV-EELLEEI 239
Cdd:COG3638 172 EPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRdgrvvfdgPPAELtDAVLREI 242
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
28-239 |
2.60e-36 |
|
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: 128.62 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDlvlasEHQILELRRRE----IGFVTQFL 103
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL--------LD-----GRDLASLSRRElarrIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLPRQATLDVVA------QPLFALGVSRDVAR-QRAAELLSAMKLPERLWSvspaTFSGGERQRVNLARGFIAKPRLLL 176
Cdd:COG1120 85 PAPFGLTVRELVAlgryphLGLFGRPSAEDREAvEEALERTGLEHLADRPVD----ELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELA--------PPPAV--EELLEEI 239
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKdgrivaqgPPEEVltPELLEEV 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-239 |
6.76e-36 |
|
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: 127.30 E-value: 6.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlasehQILELR--RREIGFVTQFLHC 105
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKL--------KGKALRqlRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVA----------QPLFALGVSRDvaRQRAAELLSAMKLPERLWSVSpATFSGGERQRVNLARGFIAKPRLL 175
Cdd:cd03256 90 IERLSVLENVLsgrlgrrstwRSLFGLFPKEE--KQRALAALERVGLLDKAYQRA-DQLSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVVELA--------PPPAV-EELLEEI 239
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKdgrivfdgPPAELtDEVLDEI 240
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
28-226 |
1.30e-35 |
|
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: 124.42 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLvlasehqilELRRREIGFVTQflhclp 107
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL---------ESLRKNIAYVPQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rqatlDVVaqpLFALGVsRDvarqraaELLSamklperlwsvspatfsGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:cd03228 84 -----DPF---LFSGTI-RE-------NILS-----------------GGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTaMLAIFHHPETTRRlADQVVEL 226
Cdd:cd03228 131 TEALILEALRALAKGKT-VIVIAHRLSTIRD-ADRIIVL 167
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
4.62e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 125.59 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEQNKLIpsSHNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRDamghe 77
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTA--LDDVSLTVAAGEFVALVGPSGCGKSTLLRliaGLEK---PTSGEVLVDG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 ldlvlasehQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGG 157
Cdd:COG1116 73 ---------KPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAY-PHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAML--------AIFhhpettrrLADQVVELAP 228
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfvthdvdeAVF--------LADRVVVLSA 214
|
...
gi 1706422447 229 PPA 231
Cdd:COG1116 215 RPG 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-223 |
4.89e-35 |
|
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: 124.62 E-value: 4.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQlhEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDLVLAS 84
Cdd:cd03258 1 MIELKNVSKVFG--DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV---DGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EhqiLELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNL 164
Cdd:cd03258 76 E---LRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAY-PAQLSGGQKQRVGI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV 223
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRV 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
28-224 |
8.23e-35 |
|
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: 123.83 E-value: 8.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYR-----TYLPSAGRILYRDamghelDLVLASEHQILELRRReIGFVtqF 102
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDG------KDIYDLDVDVLELRRR-VGMV--F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQATL-DVVAQPLFALGV-SRDVARQRAAELLSAMKLPERLWSVSPAT-FSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:cd03260 88 QKPNPFPGSIyDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRLHALgLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTAMLAIfHHPETTRRLADQVV 224
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEYTIVIVT-HNMQQAARVADRTA 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-239 |
1.08e-34 |
|
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: 124.20 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlheqnKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLase 85
Cdd:COG4555 2 IEVENLSKKY------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 hqilelrRREIGFVTQFLHCLPRQATLDVVAqpLFAL--GVSRDVARQRAAELLSAMKLPE---RLWSvspaTFSGGERQ 160
Cdd:COG4555 73 -------RRQIGVLPDERGLYDRLTVRENIR--YFAElyGLFDEELKKRIEELIELLGLEEfldRRVG----ELSTGMKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV-----ELAPPPAVEEL 235
Cdd:COG4555 140 KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVilhkgKVVAQGSLDEL 219
|
....
gi 1706422447 236 LEEI 239
Cdd:COG4555 220 REEI 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-224 |
1.64e-34 |
|
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: 123.32 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHF-QLHEQNklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLAS 84
Cdd:cd03219 1 LEVRGLTKRFgGLVALD-------DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE-----DITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQIlelRRREIGFVTQFLHCLPRQATLD---VVAQP-------LFALGVSRDVARQRAAELLSAMKLpERLWSVSPATF 154
Cdd:cd03219 69 PHEI---ARLGIGRTFQIPRLFPELTVLEnvmVAAQArtgsgllLARARREEREARERAEELLERVGL-ADLADRPAGEL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 155 SGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-226 |
1.66e-34 |
|
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: 122.90 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQILELRRReIGFVTQFL 103
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ-----DVSDLRGRAIPYLRRK-IGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:cd03292 88 RLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRAL-PAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 184 LDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-226 |
1.67e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.58 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrDAMGHELDLV-LASEHQILELRRrEIGFVTQFLHCL 106
Cdd:COG4161 19 FDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL---NIAGHQFDFSqKPSEKAIRLLRQ-KVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:COG4161 95 PHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706422447 186 PATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:COG4161 174 PEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
1.82e-34 |
|
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: 123.17 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEG----YGKHfQLHEqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYrda 73
Cdd:COG1127 1 MSEPMIEVRNltksFGDR-VVLD---------GVSLDVPRGEILAIIGGSGSGKSVLLKliiGLLR---PDSGEILV--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 74 MGHelDLVLASEHQILELRRReIGFVTQflhclprQATL-------DVVAQPLFALG-VSRDVARQRAAELLSAMKLP-- 143
Cdd:COG1127 65 DGQ--DITGLSEKELYELRRR-IGMLFQ-------GGALfdsltvfENVAFPLREHTdLSEAEIRELVLEKLELVGLPga 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 144 ERLWsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQ 222
Cdd:COG1127 135 ADKM---PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADR 211
|
....*
gi 1706422447 223 VVELA 227
Cdd:COG1127 212 VAVLA 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
29-224 |
1.94e-34 |
|
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: 122.63 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvlasEHQILELRRREIGFVTQFLHCLPR 108
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----------DVTGVPPERRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03259 87 LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 189 AERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03259 166 REELREELKELqRELGITTIYVTHDQEEALALADRIA 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-227 |
1.94e-34 |
|
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: 122.64 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlvlasehQILELRRREIGFVTQ---FLH 104
Cdd:cd03235 16 EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------------KPLEKERKRIGYVPQrrsIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPrqAT-LDVVAQPLFA----LGVSRDVARQRAAELLSAMKLPErLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:cd03235 82 DFP--ISvRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSE-LADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-231 |
2.25e-34 |
|
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: 122.58 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFQLHEQNKLIpsSHNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRDamgheldlvl 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTA--LEDISLSVEEGEFVALVGPSGCGKSTLLRiiaGLER---PTSGEVLVDG---------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 83 asehQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLP--ERLWsvsPATFSGGERQ 160
Cdd:cd03293 66 ----EPVTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSgfENAY---PHQLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPA 231
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-227 |
3.09e-34 |
|
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: 122.79 E-value: 3.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQnklipSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLAS 84
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ-----ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT-----DITKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRReIGFVTQFLHCLPRQATLDVVAQPLFA--------LGVSRDVARQRAAELLSAMKLPERLWSVSpATFSG 156
Cdd:TIGR02315 71 GKKLRKLRRR-IGMIFQHYNLIERLTVLENVLHGRLGykptwrslLGRFSEEDKERALSALERVGLADKAYQRA-DQLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-224 |
6.32e-34 |
|
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: 120.23 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 10 GYGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELdlvlaSEHQIL 89
Cdd:cd03214 8 GYGGRTVLD----------DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL---DGKDL-----ASLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 90 ELRRReIGFVTQFLhclprqatldvvaqplfalgvsrdvarqraaELLSAMKLPERLWSvspaTFSGGERQRVNLARGFI 169
Cdd:cd03214 70 ELARK-IAYVPQAL-------------------------------ELLGLAHLADRPFN----ELSGGERQRVLLARALA 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 170 AKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVI 169
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
28-226 |
3.08e-33 |
|
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: 117.73 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLvlasehqilELRRREIGFVTQFlhclp 107
Cdd:cd00267 16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL---------EELRRRIGYVPQL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rqatldvvaqplfalgvsrdvarqraaellsamklperlwsvspatfSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:cd00267 82 -----------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd00267 115 SRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
8.54e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 121.74 E-value: 8.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEG----YGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgh 76
Cdd:COG3842 1 MAMPALELENvskrYGDVTALD----------DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 77 eldlvlaseHQILEL--RRREIGFVTQ----FLHclprqatLDV---VAQPLFALGVSRDVARQRAAELLSAMKLP---E 144
Cdd:COG3842 67 ---------RDVTGLppEKRNVGMVFQdyalFPH-------LTVaenVAFGLRMRGVPKAEIRARVAELLELVGLEglaD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 145 RLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQV 223
Cdd:COG3842 131 RY----PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRI 206
|
.
gi 1706422447 224 V 224
Cdd:COG3842 207 A 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-226 |
1.92e-32 |
|
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: 124.18 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrDamGHELdlvlaseHQI-LELRRREIGFVTQflHCL 106
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-D--GIDL-------RQIdPASLRRQIGVVLQ--DVF 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATL-DVVAqpLFALGVSRDVARqRAAELLSA----MKLPERLWS-VSP--ATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG2274 560 LFSGTIrENIT--LGDPDATDEEII-EAARLAGLhdfiEALPMGYDTvVGEggSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAEGTaMLAIFHHPETTrRLADQVVEL 226
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTI-RLADRIIVL 682
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-227 |
2.64e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.97 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 14 HFQLHEQNKLIpssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDlvlasehqilelRR 93
Cdd:cd03226 6 SFSYKKGTEIL---DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE------------RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 94 REIGFVTQflhclprqatlDVVAQpLFALGVSRDVAR---------QRAAELLSAMKLpERLWSVSPATFSGGERQRVNL 164
Cdd:cd03226 71 KSIGYVMQ-----------DVDYQ-LFTDSVREELLLglkeldagnEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
28-227 |
2.87e-32 |
|
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: 117.60 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHelDLVLASEHQILELRRReIGFVTQflhclp 107
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI---DGE--DISGLSEAELYRLRRR-MGMLFQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATL-------DVVAQPLFALGV-SRDVARQRAAELLSAMKLP--ERLWsvsPATFSGGERQRVNLARGFIAKPRLLLL 177
Cdd:cd03261 85 -SGALfdsltvfENVAFPLREHTRlSEEEIREIVLEKLEAVGLRgaEDLY---PAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 178 DEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLY 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-224 |
5.30e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 5.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrDAMGHELDLVLA-SEHQILELRRrEIGFVTQFLHCL 106
Cdd:PRK11124 19 FDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL---NIAGNHFDFSKTpSDKAIRELRR-NVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERL--WsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:PRK11124 95 PHLTVQQnLIEAPCRVLGLSKDQALARAEKLLERLRLKPYAdrF---PLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706422447 184 LDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVV 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-224 |
8.36e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.81 E-value: 8.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrDamGHEL-DLVLASehqileLRRReIGFVTQflhcl 106
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-D--GVDIrDLTLES------LRRQ-IGVVPQ----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 prqatlDVVaqpLF--------ALG---VSRDVARqRAAELLSA----MKLPERLWS-VSP--ATFSGGERQRVNLARGF 168
Cdd:COG1132 422 ------DTF---LFsgtireniRYGrpdATDEEVE-EAAKAAQAhefiEALPDGYDTvVGErgVNLSGGQRQRIAIARAL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 169 IAKPRLLLLDEPTSSLDPATAERVIGLIEGLkAEGTAMLAIFHHPETTRRlADQVV 224
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHRLSTIRN-ADRIL 545
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
28-226 |
1.22e-31 |
|
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: 114.03 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYrdaMGHELdlvlaseHQILELRRREIGFVTQFLh 104
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKiilGLLK---PDSGEIKV---LGKDI-------KKEPEEVKRRIGYLPEEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPRQATldvvaqplfalgvsrdvarqrAAELLSamklperlwsvspatFSGGERQRVNLARGFIAKPRLLLLDEPTSSL 184
Cdd:cd03230 83 SLYENLT---------------------VRENLK---------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 185 DPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-224 |
1.36e-31 |
|
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: 116.78 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgheLDLVLASEhQILELR--RREIGFVTQFlhc 105
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI-------DGRDITAK-KKKKLKdlRKKVGLVFQF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lPRQatldvvaQpLFA-------------LGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLArGFIA-K 171
Cdd:TIGR04521 91 -PEH-------Q-LFEetvykdiafgpknLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIA-GVLAmE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVI 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-225 |
1.87e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 116.18 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLheqnklIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDL 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGP------RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQILELRRREIGFVTQFlhclPRQA-TLDV-----VAQPLFALGVsRDVA--RQRAAELLSAMKLPERLWSVSPA 152
Cdd:PRK11701 76 YALSEAERRRLLRTEWGFVHQH----PRDGlRMQVsaggnIGERLMAVGA-RHYGdiRATAGDWLERVEIDAARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 153 TFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLAD--------QV 223
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHrllvmkqgRV 230
|
..
gi 1706422447 224 VE 225
Cdd:PRK11701 231 VE 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-227 |
4.22e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELdlvlaSEHQILEL-RRREIgfvtqflhcL 106
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL---NGRPL-----AAWSPWELaRRRAV---------L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATL-------DVVAQPLFALGVSRDVARQRAAELLSAMKLP---ERLWSvspaTFSGGERQRVNLAR-------GFI 169
Cdd:COG4559 81 PQHSSLafpftveEVVALGRAPHGSSAAQDRQIVREALALVGLAhlaGRSYQ----TLSGGEQQRVQLARvlaqlwePVD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 170 AKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLH 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
28-220 |
4.95e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVLASEHQIlelrRREIGFVTQFLHCLP 107
Cdd:PRK09493 18 HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD---GLKVNDPKVDERLI----RQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVA-QPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PRK09493 91 HLTALENVMfGPLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190
....*....|....*....|....*....|....
gi 1706422447 187 ATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLA 220
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVA 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-224 |
6.43e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 2 NPPILQVEGYGKHFqlheqnkliPSSH---NVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRdamG 75
Cdd:COG1129 1 AEPLLEMRGISKSF---------GGVKaldGVSLELRPGEVHALLGENGAGKSTLMKilsGVYQ---PDSGEILLD---G 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 76 HELDLvlaseHQILELRRREIGFVTQFLHCLPrqaTLDVvAQPLFaLG--------VSRDVARQRAAELLSAMKLPerlw 147
Cdd:COG1129 66 EPVRF-----RSPRDAQAAGIAIIHQELNLVP---NLSV-AENIF-LGreprrgglIDWRAMRRRARELLARLGLD---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 148 sVSPAT----FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:COG1129 132 -IDPDTpvgdLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
.
gi 1706422447 224 V 224
Cdd:COG1129 211 T 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
29-224 |
9.45e-31 |
|
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: 113.93 E-value: 9.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVlasehqilELRRReIGFVTQFLHCLPR 108
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV--------ELRRK-IGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKL-PERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:cd03295 90 MTVEENIALVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 188 TAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03295 170 TRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIA 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
28-224 |
1.20e-30 |
|
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: 111.51 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlVLASEHQILELRRREIGFVTQFLHCLP 107
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-------DLTDLEDELPPLRRRIGMVFQDFALFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLfalgvsrdvarqraaellsamklperlwsvspatfSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:cd03229 90 HLTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 188 TAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03229 135 TRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVV 172
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-186 |
1.63e-30 |
|
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: 113.89 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHfQLHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLA 83
Cdd:cd03294 18 FKLLAKGKSKE-EILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG-----QDIAAM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 SEHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVN 163
Cdd:cd03294 92 SRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKY-PDELSGGMQQRVG 170
|
170 180
....*....|....*....|...
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDP 186
Cdd:cd03294 171 LARALAVDPDILLMDEAFSALDP 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-224 |
1.73e-30 |
|
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: 112.39 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRaGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldLVLASEHQI-LELRRREIGFVTQFLHCLP 107
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT------VLFDSRKKInLPPQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RqatLDVVAQPLFALGVSRD-VARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:cd03297 89 H---LNVRENLAFGLKRKRNrEDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 187 ATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIV 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-224 |
2.52e-30 |
|
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: 112.82 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 2 NPPILQVEGYGKHFQ-LHeqnklipSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDL 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGgLV-------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-----DI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQI--------------------LE------LRRREIGFVTQFLHcLPRQATldvvaqplfalgvSRDVARQRAA 134
Cdd:COG0411 69 TGLPPHRIarlgiartfqnprlfpeltvLEnvlvaaHARLGRGLLAALLR-LPRARR-------------EEREARERAE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 135 ELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHP 213
Cdd:COG0411 135 ELLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDM 213
|
250
....*....|.
gi 1706422447 214 ETTRRLADQVV 224
Cdd:COG0411 214 DLVMGLADRIV 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-224 |
5.03e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.02 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIyrTYL--PSAGRILYRDamgheLDLVLASEHQILELRRReIGFVTQFLHC 105
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCI--NLLerPTSGSVLVDG-----VDLTALSERELRAARRK-IGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSvSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:COG1135 94 LSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADA-YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 186 PATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:COG1135 173 PETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVA 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-228 |
9.37e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEQNKLIPSSH-----NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamG 75
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTVGVvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFD---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 76 HelDLVLASEHQILELRRReIGFVTQ----FLHclPRQATLDVVAQPLFALGV-SRDVARQRAAELLSAMKLPERLWSVS 150
Cdd:COG4608 80 Q--DITGLSGRELRPLRRR-MQMVFQdpyaSLN--PRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 151 PATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLAD-------- 221
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDrvavmylg 234
|
....*..
gi 1706422447 222 QVVELAP 228
Cdd:COG4608 235 KIVEIAP 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-224 |
1.47e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.28 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFQLHEQNKlipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLvlase 85
Cdd:cd03216 1 LELRGITKRFGGVKALD------GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD---GKEVSF----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 HQILELRRREIGFVTQFlhclprqatldvvaqplfalgvsrdvarqraaellsamklperlwsvspatfSGGERQRVNLA 165
Cdd:cd03216 67 ASPRDARRAGIAMVYQL----------------------------------------------------SVGERQMVEIA 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 166 RGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-224 |
2.48e-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: 109.45 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQILelrRREIGFVTQfLHCLP 107
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR-----DITGLPPHERA---RAGIGYVPE-GRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQAT----LDVVAQPLfalgvSRDVARQRAAELLSAM-KLPERLWSvsPA-TFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:cd03224 88 PELTveenLLLGAYAR-----RRAKRKARLERVYELFpRLKERRKQ--LAgTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 182 SSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAY 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-232 |
3.02e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 110.44 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFQLHEQNKlipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI--------LYRDAMGHe 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLK------GVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinLVRDKDGQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 ldLVLASEHQILELRRReIGFVTQFLHCLPRQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSG 156
Cdd:PRK10619 79 --LKVADKNQLRLLRTR-LTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV--------ELAP 228
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIflhqgkieEEGA 235
|
....
gi 1706422447 229 PPAV 232
Cdd:PRK10619 236 PEQL 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-211 |
6.24e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVLASEHQILelrRREIGFVTQFLHCLPRQ 109
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS---GHDITRLKNREVPFL---RRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATA 189
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNF-PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|..
gi 1706422447 190 ERVIGLIEGLKAEGTAMLAIFH 211
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATH 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
29-224 |
1.38e-28 |
|
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: 107.81 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLasehqiLELRRREIGFVTQFLHCLPR 108
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK-----DITN------LPPEKRDISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03299 86 MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 189 AERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03299 165 KEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVA 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-228 |
1.72e-28 |
|
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: 106.79 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvlaSEHQILELRRREIGFVTQFLHCLP 107
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE----------PIRDAREDYRRRLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQ---ATLDVVAQpLFALGVSRDvarqRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSL 184
Cdd:COG4133 89 ELtvrENLRFWAA-LYGLRADRE----AIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 185 DPATAERVIGLIEGLKAEGTAMLAIFHHPEttRRLADQVVELAP 228
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTTHQPL--ELAAARVLDLGD 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-224 |
2.17e-28 |
|
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: 112.09 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEQNKLIpsSHNVSFTVRAGELTALIGPTGAGKS----SVLKgiyrtYLPSA-----GRILYR 71
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEA--VKGVSFDIAAGETLALVGESGSGKSvtalSILR-----LLPDPaahpsGSILFD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 72 DAmghelDLVLASEHQILELRRREIGFVTQF-------LHCLPRQatldvVAQPLFA-LGVSRDVARQRAAELLSAMKL- 142
Cdd:COG4172 75 GQ-----DLLGLSERELRRIRGNRIAMIFQEpmtslnpLHTIGKQ-----IAEVLRLhRGLSGAAARARALELLERVGIp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 143 -PERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLA 220
Cdd:COG4172 145 dPERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFA 224
|
....
gi 1706422447 221 DQVV 224
Cdd:COG4172 225 DRVA 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
28-234 |
2.46e-28 |
|
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: 112.16 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLvlasehqilELRRREIGFVTQ----Fl 103
Cdd:COG4988 354 DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP---------ASWRRQIAWVPQnpylF- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 hclprQATL-DVVaqpLFALGVSRDVARQRAAELLSAMKLPERLwsvsP-----------ATFSGGERQRVNLARGFIAK 171
Cdd:COG4988 424 -----AGTIrENL---RLGRPDASDEELEAALEAAGLDEFVAAL----PdgldtplgeggRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLkAEGTAMLAIFHHPETTRRlADQVVELAPPPAVEE 234
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQ 552
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
28-185 |
2.63e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.47 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY--RDAMGHeldlvlasehqiLELRRREIGFVTQ---- 101
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngRDLFTN------------LPPRERRVGFVFQhyal 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 FLHclprqatLDV---VAQPLFALGVSRDVARQRAAELLSAMKLPE---RLwsvsPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:COG1118 87 FPH-------MTVaenIAFGLRVRPPSKAEIRARVEELLELVQLEGladRY----PSQLSGGQRQRVALARALAVEPEVL 155
|
170
....*....|
gi 1706422447 176 LLDEPTSSLD 185
Cdd:COG1118 156 LLDEPFGALD 165
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-227 |
6.77e-28 |
|
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: 104.22 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVlASEHQILELRRREIGFVTQflhclpr 108
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR--------LDGA-DISQWDPNELGDHVGYLPQ------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qatldvvaqplfalgvsrDVarqraaELLSAmklperlwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03246 84 ------------------DD------ELFSG--------SIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVELA 227
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLE 169
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-223 |
8.29e-28 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 107.48 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKgIYRTYL-PSAGRilyrdAMGHELDLVlaseHQILELRRReIGFVtqflhclPR 108
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIR-MLTTLLrPTSGT-----ARVAGYDVV----REPRKVRRS-IGIV-------PQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLD---------VVAQPLFalGVSRDVARQRAAELLSAMKLPE---RLwsvsPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:TIGR01188 74 YASVDedltgrenlEMMGRLY--GLPKDEAEERAEELLELFELGEaadRP----VGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRI 194
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-218 |
1.49e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 105.25 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQNKLIPSShnVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDlvlas 84
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTG--VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNL 164
Cdd:PRK10584 79 EEARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHL-PAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRR 218
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAAR 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-223 |
1.93e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.19 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 7 QVEGYGKHFQLHeqNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEH 86
Cdd:PRK11153 3 ELKNISKVFPQG--GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG-----QDLTALSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 87 QiLELRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLAR 166
Cdd:PRK11153 76 E-LRKARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 167 GFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV 223
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRV 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-224 |
1.94e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.22 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlHEQNKLipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghELDLVLASE 85
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVL----HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDI---TIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 HQILELR--RREIGFVTQFLHCLPRQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRV 162
Cdd:PRK11264 75 QQKGLIRqlRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSY-PRRLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 163 NLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-234 |
2.00e-27 |
|
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: 109.51 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKS---SVLKGIyRTYLPSAGRILYRDAM-------------------------GHELDL 80
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSvlmHVLRGM-DQYEPTSGRIIYHVALcekcgyverpskvgepcpvcggtlePEEVDF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQILELRRReIGFVTQFLHCL-PRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSpATFSGGER 159
Cdd:TIGR03269 97 WNLSDKLRRRIRKR-IAIMLQRTFALyGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIA-RDLSGGEK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERV-IGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-226 |
2.84e-27 |
|
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: 104.23 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 21 NKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDlvlasehqILELRRReIGFVT 100
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS--------RKSLRSM-IGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 101 QFLHCLPRqatlDVVAQPLFALGVSRDVARQRAAELLSA----MKLPERLWSV---SPATFSGGERQRVNLARGFIAKPR 173
Cdd:cd03254 84 QDTFLFSG----TIMENIRLGRPNATDEEVIEAAKEAGAhdfiMKLPNGYDTVlgeNGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 174 LLLLDEPTSSLDPATAERVIGLIEGLKaEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVL 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-213 |
3.89e-27 |
|
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: 103.82 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVlasehqilELRRReIGFVTQFL 103
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA--------DLRRN-IGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLprQATL-DVVAqplFALGVSRDVARQRAAELLSAMKLPERlwsvSPATF-----------SGGERQRVNLARGFIAK 171
Cdd:cd03245 88 TLF--YGTLrDNIT---LGAPLADDERILRAAELAGVTDFVNK----HPNGLdlqigergrglSGGQRQAVALARALLND 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTaMLAIFHHP 213
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKT-LIIITHRP 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
29-223 |
6.54e-27 |
|
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: 103.22 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKgIYRTYL-PSAGRILyrdAMGHelDLVLASEhqilELRRReIGFVTQFLHCLP 107
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIK-MLTTLLkPTSGRAT---VAGH--DVVREPR----EVRRR-IGIVFQDLSVDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAqpLFA--LGVSRDVARQRAAELLSAMKLPE---RLWSvspaTFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:cd03265 87 ELTGWENLY--IHArlYGVPGAERRERIDELLDFVGLLEaadRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 183 SLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV 223
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRV 202
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-226 |
6.71e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 104.11 E-value: 6.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 2 NPPILQVEGYGKHFQLHEQNKlipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI--------LYRDA 73
Cdd:COG4598 5 APPALEVRDLHKSFGDLEVLK------GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIrvggeeirLKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 74 MGHeldLVLASEHQILELRRReIGFVTQFLHCLPRQATLD-VVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPA 152
Cdd:COG4598 79 DGE---LVPADRRQLQRIRTR-LGMVFQSFNLWSHMTVLEnVIEAPVHVLGRPKAEAIERAEALLAKVGLADKR-DAYPA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 153 TFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:COG4598 154 HLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFL 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-224 |
8.01e-27 |
|
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: 103.08 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEL-DLVLASehqilelRRREIGFVTQ--FLH 104
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID---GHDVrDYTLAS-------LRRQIGLVSQdvFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 ClprqatlDVVAQPLF--ALGVSRDVARqRAAELLSA----MKLPERLWSV---SPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:cd03251 89 N-------DTVAENIAygRPGATREEVE-EAARAANAhefiMELPEGYDTVigeRGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEGTAmLAIFHHPETTRRlADQVV 224
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTT-FVIAHRLSTIEN-ADRIV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-224 |
9.27e-27 |
|
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: 107.46 E-value: 9.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGYGKHFQLHE-----QNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPSAGRILYrdaMGHE 77
Cdd:COG4172 273 PPLLEARDLKVWFPIKRglfrrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRF---DGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 LDLvlASEHQILELRRReIGFVTQ--FLHCLPRQATLDVVAQPLFALGVSRDVA--RQRAAELLSAMKLPERLWSVSPAT 153
Cdd:COG4172 349 LDG--LSRRALRPLRRR-MQVVFQdpFGSLSPRMTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLDPAARHRYPHE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 154 FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVM 497
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-228 |
1.92e-26 |
|
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: 101.09 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGI--YRTYLPSAGRILYRDAMGHELDLvlasehqilelrRREIGFVTQFLHC 105
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSF------------RKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPrqaTLDVVAQPLFAlgvsrdvarqraAELLSamklperlwsvspatFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03213 94 HP---TLTVRETLMFA------------AKLRG---------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 186 PATAERVIGLIEGLKAEGTAMLAIFHHPETTR-RLADQVVELAP 228
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQPSSEIfELFDKLLLLSQ 187
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-226 |
2.63e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.77 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvlasehqilelrrREIGFVTQFLHcLP 107
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--------------------ARVAYVPQRSE-VP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATL---DVVA----QPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:NF040873 68 DSLPLtvrDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGL-ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-227 |
4.46e-26 |
|
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: 100.91 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLheQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamghELDLVLAS 84
Cdd:cd03266 1 MITADALTKRFRD--VKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------TVDGFDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 eHQILELRRReIGFVTQFLHCLPRQATLDVVAqpLFA--LGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRV 162
Cdd:cd03266 71 -KEPAEARRR-LGFVSDSTGLYDRLTARENLE--YFAglYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 163 NLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLH 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-226 |
4.61e-26 |
|
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: 105.62 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDLVLASEhqilelRRREIGFVTQFLH 104
Cdd:COG4987 349 PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL---GGVDLRDLDEDD------LRRRIAVVPQRPH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLprQATLdvvaqplfalgvsRD---VARQRA--AELLSAMK----------LPERLWSV---SPATFSGGERQRVNLAR 166
Cdd:COG4987 420 LF--DTTL-------------REnlrLARPDAtdEELWAALErvglgdwlaaLPDGLDTWlgeGGRRLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 167 GFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLkAEGTAMLAIFHHPeTTRRLADQVVEL 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRL-AGLERMDRILVL 542
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
28-226 |
4.68e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 100.38 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASEhqileLRRREIGFVTQFLHCLP 107
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASK-----FRREKLGYLFQNFALIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:TIGR03608 90 NETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKL-KQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPK 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:TIGR03608 169 NRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-224 |
5.43e-26 |
|
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: 101.21 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVE----GYGKhfqlheqnklIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghel 78
Cdd:COG0410 1 MPMLEVEnlhaGYGG----------IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 79 DLVLASEHQILelrRREIGFVTQFLHCLPRQaTldvVAQPLfALGVSRDVARQRAAELLSAM-----KLPERLWSVSpAT 153
Cdd:COG0410 66 DITGLPPHRIA---RLGIGYVPEGRRIFPSL-T---VEENL-LLGAYARRDRAEVRADLERVyelfpRLKERRRQRA-GT 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 154 FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:COG0410 137 LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAY 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-227 |
9.41e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.00 E-value: 9.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELdlvlaSEHQILEL-RRREIgfvtqflhcL 106
Cdd:PRK13548 19 DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL---NGRPL-----ADWSPAELaRRRAV---------L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATL-------DVVAQPLFALGVSRDVARQRAAELLSAM---KLPERLWsvspATFSGGERQRVNLAR------GFIA 170
Cdd:PRK13548 82 PQHSSLsfpftveEVVAMGRAPHGLSRAEDDALVAAALAQVdlaHLAGRDY----PQLSGGEQQRVQLARvlaqlwEPDG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 171 KPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLH 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-226 |
4.05e-25 |
|
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: 102.75 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQilelRRREIGFVTQFLHCLPr 108
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV-----PLADADADS----WRDQIAWVPQHPFLFA- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qATldVVAQPLFALGVSRDVARQRAAELLSAMK----LPERLWSV---SPATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:TIGR02857 410 -GT--IAENIRLARPDASDAEIREALERAGLDEfvaaLPQGLDTPigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 182 SSLDPATAERVIGLIEGLkAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:TIGR02857 487 AHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-185 |
5.67e-25 |
|
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: 98.57 E-value: 5.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFQLheqnklIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY--RDAMGHELdlvla 83
Cdd:cd03296 3 IEVRNVSKRFGD------FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggEDATDVPV----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 sehqilelRRREIGFVTQFLHCLPRQATLDVVAqplFALGV-------SRDVARQRAAELLSAMKLpERLWSVSPATFSG 156
Cdd:cd03296 72 --------QERNVGFVFQHYALFRHMTVFDNVA---FGLRVkprserpPEAEIRAKVHELLKLVQL-DWLADRYPAQLSG 139
|
170 180
....*....|....*....|....*....
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALD 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
30-226 |
5.98e-25 |
|
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: 100.57 E-value: 5.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamgHELDLVLASEHQ--ILELRRREIGFVTQflhclp 107
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEI-------VLNGRTLFDSRKgiFLPPEKRRIGYVFQ------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATL---DVVAQPL-----FALGVSRDVARQRAAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:TIGR02142 83 -EARLfphLSVRGNLrygmkRARPSERRISFERVIELLGIGHLLGRL----PGRLSGGEKQRVAIGRALLSSPRLLLMDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVEL 226
Cdd:TIGR02142 158 PLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-224 |
1.90e-24 |
|
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: 97.89 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 14 HFQLHEQNKliPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdAMGHELdlvlASEHQILELRR 93
Cdd:TIGR04520 7 SFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVT---VDGLDT----LDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 94 ReIGFV-----TQFLhclprqATL--DVVAqplFAL---GVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVN 163
Cdd:TIGR04520 78 K-VGMVfqnpdNQFV------GATveDDVA---FGLenlGVPREEMRKRVDEALKLVGMEDFR-DREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 164 LArGFIA-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTrRLADQVV 224
Cdd:TIGR04520 147 IA-GVLAmRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEA-VLADRVI 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
31-236 |
2.06e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.75 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 31 SFTVRAGELTALIGPTGAGKSSVLKGI--YRTylPSAGRILYRDAmghelDLVLASEHQilelrrREIGFVTQ----FLH 104
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIagFLP--PDSGRILWNGQ-----DLTALPPAE------RPVSMLFQennlFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clprqatLDVvAQPLfALGVS-----RDVARQRAAELLSAMKLPE---RLwsvsPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:COG3840 86 -------LTV-AQNI-GLGLRpglklTAEQRAQVEQALERVGLAGlldRL----PGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV-----ELAPPPAVEELL 236
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLlvadgRIAADGPTAALL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
29-226 |
2.65e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.95 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGriLYRDAmGHelDLVLASEHQILELRRREIGFVTQFLHCLPR 108
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG--TYRVA-GQ--DVATLDADALAQLRREHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:PRK10535 101 LTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEI 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-234 |
2.74e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.18 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQN---KLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLV 81
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR---GQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 82 LASEHQILelrRREIGFVtqFLHCL----PRQATLDVVAQPLFALgVSRDVARQ--RAAELLSAMKLPERLWSVSPATFS 155
Cdd:TIGR02769 79 DRKQRRAF---RRDVQLV--FQDSPsavnPRMTVRQIIGEPLRHL-TSLDESEQkaRIAELLDMVGLRSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 156 GGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
30-211 |
3.46e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 95.18 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLvlaSEHQILELRRReIGFVTQFlhclPRQ 109
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLID---GEPLDY---SRKGLLERRQR-VGLVFQD----PDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATL------DVVAQPLfALGVSRDVARQR---AAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:TIGR01166 80 QLFaadvdqDVAFGPL-NLGLSEAEVERRvreALTAVGASGLRERP----THCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFH 211
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
4.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 18 HEQNKLIPSS----HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI--LYRDAMGHE---------LDLVL 82
Cdd:PRK13651 10 KIFNKKLPTElkalDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKktkekekvlEKLVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 83 ASEH-----QILELRRReIGFVTQFLHCLPRQATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLPERLWSVSPATFS 155
Cdd:PRK13651 90 QKTRfkkikKIKEIRRR-VGVVFQFAEYQLFEQTIekDIIFGPV-SMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1706422447 156 GGERQRVNLArGFIA-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFH 211
Cdd:PRK13651 168 GGQKRRVALA-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
29-224 |
6.06e-24 |
|
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: 95.26 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEldlVLASEHQIlelrRREIGFVTQFLHCLPR 108
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN---GYS---IRTDRKAA----RQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAqpLFAL--GVSRDVARQRAAELLSAMKLPE-RLWSVSpaTFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03263 90 LTVREHLR--FYARlkGLPKSEIKEEVELLLRVLGLTDkANKRAR--TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 186 PATAERVIGLIEGLKAEGTAMLAIfHHPETTRRLADQVV 224
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTT-HSMDEAEALCDRIA 203
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-227 |
6.69e-24 |
|
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: 94.87 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 31 SFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgHELDlvlaseHQILELRRREIGFVTQ----FLHcl 106
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI-----NGVD------VTAAPPADRPVSMLFQennlFAH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 prqatLDVVAQplFALGVS-----RDVARQRAAELLSAMKLPERLWSVsPATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:cd03298 85 -----LTVEQN--VGLGLSpglklTAEDRQAIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 182 SSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-224 |
8.23e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.72 E-value: 8.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRdamGHELDlvlaSEHqilelrRREIGFvtqflh 104
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRiilGILA---PDSGEVLWD---GEPLD----PED------RRRIGY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 cLPRQ----ATLDVVAQPLF--AL-GVSRDVARQRAAELLSAMKLPERlWSVSPATFSGGERQRVNLARGFIAKPRLLLL 177
Cdd:COG4152 76 -LPEErglyPKMKVGEQLVYlaRLkGLSKAEAKRRADEWLERLGLGDR-ANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 178 DEPTSSLDPATAERVIGLIEGLKAEGTAMlaIF--HHPETTRRLADQVV 224
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKGTTV--IFssHQMELVEELCDRIV 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-212 |
1.10e-23 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 93.53 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 14 HFQLHEQNKLIpsSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQilELRR 93
Cdd:cd03247 7 SFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT--------LDGVPVSDLE--KALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 94 REIGFVTQFLHclprqatldvvaqpLFALGVSRDVARQraaellsamklperlwsvspatFSGGERQRVNLARGFIAKPR 173
Cdd:cd03247 75 SLISVLNQRPY--------------LFDTTLRNNLGRR----------------------FSGGERQRLALARILLQDAP 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 174 LLLLDEPTSSLDPATAERVIGLIEGLkAEGTAMLAIFHH 212
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHH 156
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-238 |
1.18e-23 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 94.91 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDlvlasehqiLELRRREIGFVTQflhclpr 108
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---------LRWLRSQIGLVSQ------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qatldvvaQP-LFALGVSRDVA----------RQRAAELLSA----MKLPERLWSV---SPATFSGGERQRVNLARGFIA 170
Cdd:cd03249 85 --------EPvLFDGTIAENIRygkpdatdeeVEEAAKKANIhdfiMSLPDGYDTLvgeRGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 171 KPRLLLLDEPTSSLDPATAERVIGLIEGLkAEGTAMLAIFHHPETTRRlADQVVELAPPPAVE-----ELLEE 238
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEqgthdELMAQ 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-224 |
1.91e-23 |
|
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: 96.71 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRDamghelDLVLASEHQI-LELRRREIGFVTQ--- 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRaiaGLER---PDSGRIRLGG------EVLQDSARGIfLPPHRRRIGYVFQear 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 -FLHclprqatLDVVAQPLFalGVSRDVARQRAAELLSAMKLP--ERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG4148 88 lFPH-------LSVRGNLLY--GRKRAPRAERRISFDEVVELLgiGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVV 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-223 |
2.77e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEG----YGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTY--LPSA---GRILYR-- 71
Cdd:COG1117 9 EPKIEVRNlnvyYGDKQALK----------DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 72 DAMGHELDLVlasehqilELRRReIGFVTQ----F-------------LHCLPRQATLD-VVAQPLfalgvsrdvarqRA 133
Cdd:COG1117 79 DIYDPDVDVV--------ELRRR-VGMVFQkpnpFpksiydnvayglrLHGIKSKSELDeIVEESL------------RK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 134 AELLSAMKlpERLWSvSPATFSGGERQRVNLARGfIA-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTaMLAIFHH 212
Cdd:COG1117 138 AALWDEVK--DRLKK-SALGLSGGQQQRLCIARA-LAvEPEVLLMDEPTSALDPISTAKIEELILELKKDYT-IVIVTHN 212
|
250
....*....|.
gi 1706422447 213 PETTRRLADQV 223
Cdd:COG1117 213 MQQAARVSDYT 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
30-226 |
3.86e-23 |
|
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: 93.11 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlvlaseHQILELRRREIGFVTQFLHCLPRQ 109
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-------------KPLDIAARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATLDVVAqpLFA--LGVSRDVARQRAAELLSAMKLPERlWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:cd03269 86 KVIDQLV--YLAqlKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
29-226 |
5.40e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrDAMGHELDLVLASEHqiLELRRREIGFVTQFLHCLPR 108
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI---TIAGYHITPETGNKN--LKKLRKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PRK13641 100 ENTVlkDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 187 ATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-187 |
7.13e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.14 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRDamghelDLVLAsehqiLELRRREIGFVTQ--- 101
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRmiaGLED---PTSGEILIGG------RDVTD-----LPPKDRNIAMVFQsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 -FLHclprqatLDV---VAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLL 177
Cdd:COG3839 86 lYPH-------MTVyenIAFPLKLRKVPKAEIDRRVREAAELLGLEDLL-DRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170
....*....|
gi 1706422447 178 DEPTSSLDPA 187
Cdd:COG3839 158 DEPLSNLDAK 167
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
28-230 |
8.25e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDlvlaseHQILELRRREIGFVTQFLHCLP 107
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT--------LD------GVPVTGPGADRGVVFQKDALLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPE----RLWSVSpatfsGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:COG4525 90 WLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADfarrRIWQLS-----GGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 184 LDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPP 230
Cdd:COG4525 165 LDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVMSPGP 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-234 |
1.00e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPSAGRILYRDAMGHELdlvlaSEHQILELRRR-EIGFVTQFLHCLP 107
Cdd:PRK15134 304 NISFTLRPGETLGLVGESGSGKSTTGLALLR-LINSQGEIWFDGQPLHNL-----NRRQLLPVRHRiQVVFQDPNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQplfALGVSRDV--ARQRAAELLSAMK---LPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:PRK15134 378 RLNVLQIIEE---GLRVHQPTlsAAQREQQVIAVMEevgLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 183 SLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQ 507
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-224 |
1.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMgheldlVLASEHQILELR--RREIGFVTQFLHCL 106
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYA------IPANLKKIKEVKrlRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLArGFIAKP-RLLLLDEPTSS 183
Cdd:PRK13645 103 LFQETIekDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALA-GIIAMDgNTLVLDEPTGG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 184 LDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-234 |
1.09e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.55 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVlasehqILELRRREIGFVTQfLHCLP 107
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVD---GHDLALA------DPAWLRRQVGVVLQ-ENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVArqrAAELLSA----MKLPERLWSV---SPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:cd03252 89 NRSIRDNIALADPGMSMERVIE---AAKLAGAhdfiSELPEGYDTIvgeQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 181 TSSLDpATAERVIglIEGLKA--EGTAMLAIFHHPETTRRlADQVVELAPPPAVEE 234
Cdd:cd03252 166 TSALD-YESEHAI--MRNMHDicAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-211 |
1.48e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYgkHFQLHEQNKliPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamghELDL 80
Cdd:PRK13635 1 MKEEIIRVEHI--SFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------TVGG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQILELRRReIGFV-----TQFLhclprQATL-DVVAqplFAL---GVSRDVARQRAAELLSAMKLPERLwSVSP 151
Cdd:PRK13635 69 MVLSEETVWDVRRQ-VGMVfqnpdNQFV-----GATVqDDVA---FGLeniGVPREEMVERVDQALRQVGMEDFL-NREP 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 152 ATFSGGERQRVNLArGFIA-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTA-MLAIFH 211
Cdd:PRK13635 139 HRLSGGQKQRVAIA-GVLAlQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITH 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
1.55e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 20 QNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRD-AMGHELDLVLASEHQIL-------EL 91
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiYIGDKKNNHELITNPYSkkiknfkEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 92 RRReIGFVTQFLHCLPRQATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLArGFI 169
Cdd:PRK13631 115 RRR-VSMVFQFPEYQLFKDTIekDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIA-GIL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 170 A-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK13631 192 AiQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-234 |
1.80e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLHEQNKLIPSS---HNVSFTVRAGELTALIGPTGAGKSSV---LKGIYRtylPSAGRILYRDAMGHE 77
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQHQtvlNNVSLSLKSGETVALLGRSGCGKSTLarlLVGLES---PSQGNVSWRGEPLAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 LDlvlASEHQILelrRREIGFVTQ--FLHCLPRQATLDVVAQPLFALGVSRDVARQ-RAAELLSAMKLPERLWSVSPATF 154
Cdd:PRK10419 79 LN---RAQRKAF---RRDIQMVFQdsISAVNPRKTVREIIREPLRHLLSLDKAERLaRASEMLRAVDLDDSVLDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 155 SGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVE 233
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
.
gi 1706422447 234 E 234
Cdd:PRK10419 233 T 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-193 |
2.20e-22 |
|
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: 91.52 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 14 HFQLHEQNKLIpssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVlasehQILELRR 93
Cdd:cd03253 7 TFAYDPGRPVL---KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID---GQDIREV-----TLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 94 ReIGFVTQflhclprqatlDVVaqpLF-----------ALGVSRD--VARQRAAELL-SAMKLPE-----------RLws 148
Cdd:cd03253 76 A-IGVVPQ-----------DTV---LFndtigynirygRPDATDEevIEAAKAAQIHdKIMRFPDgydtivgerglKL-- 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 149 vspatfSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATaERVI 193
Cdd:cd03253 139 ------SGGEKQRVAIARAILKNPPILLLDEATSALDTHT-EREI 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-223 |
2.95e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdAMGhelDLVLASEHQILELR--RREIGFVTQFLHC- 105
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV----TVG---DIVVSSTSKQKEIKpvRKKVGVVFQFPESq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:PRK13643 97 LFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 186 PATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYV 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
28-224 |
4.03e-22 |
|
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: 90.39 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY--RDAMGheldlvlasehqiLELRRREIGFVTQFLHC 105
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIggRDVTD-------------LPPKDRDIAMVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVAQPLFALGVSRDVARQR---AAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:cd03301 84 YPHMTVYDNIAFGLKLRKVPKDEIDERvreVAELLQIEHLLDRK----PKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 183 SLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIA 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-224 |
5.81e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.55 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFqlheqnkliPSSH---NVSFTVRAGELTALIGPTGAGKS---SVLKGIYRtylPSAGRILYRdam 74
Cdd:COG3845 1 MMPPALELRGITKRF---------GGVVandDVSLTVRPGEIHALLGENGAGKStlmKILYGLYQ---PDSGEILID--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 75 GHELDLvlASEHQILELRrreIGFVTQFLHCLPrqaTLDVV------AQPLFALGVSRDVARQRAAELLSAMKLPerlws 148
Cdd:COG3845 66 GKPVRI--RSPRDAIALG---IGMVHQHFMLVP---NLTVAenivlgLEPTKGGRLDRKAARARIRELSERYGLD----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 149 VSP----ATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:COG3845 133 VDPdakvEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVT 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
28-229 |
5.90e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.85 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTyLPSA----GRILYRdamGHELDLvlasehqiLELRRREIGFVTQ-- 101
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGT-LSPAfsasGEVLLN---GRRLTA--------LPAEQRRIGILFQdd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 --FLHclprqatLDVVAQPLFAL--GVSRDVARQRAAELLSAMKLP---ERlwsvSPATFSGGERQRVNLARGFIAKPRL 174
Cdd:COG4136 86 llFPH-------LSVGENLAFALppTIGRAQRRARVEQALEEAGLAgfaDR----DPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 175 LLLDEPTSSLDPATAERVIGLI-EGLKAEGTAMLAIFHHPEtTRRLADQVVELAPP 229
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEE-DAPAAGRVLDLGNW 209
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-232 |
6.49e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.95 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQ----LHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGH 76
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrgLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQ---GQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 77 EldlVLASEHQILELRRREIGFVTQ--FLHCLPRQATLDVVAQPL-FALGVSRDVARQRAAELLSAMKLPERLWSVSPAT 153
Cdd:PRK11308 78 D---LLKADPEAQKLLRQKIQIVFQnpYGSLNPRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLRPEHYDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 154 FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV--------V 224
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVmvmylgrcV 234
|
....*...
gi 1706422447 225 ELAPPPAV 232
Cdd:PRK11308 235 EKGTKEQI 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
28-185 |
6.70e-22 |
|
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: 90.37 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLvlasehqilelRRREIGFVTQFLHCLP 107
Cdd:cd03300 17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-----------HKRPVNTVFQNYALFP 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-234 |
7.76e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLHEQ--NKLIPSSH---NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEL 78
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGllNRVTREVHaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN---GQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 79 DLVLASEHQILelrRREIGFVTQ--FLHCLPRQATLDVVAQPLFALGVSR-DVARQRAAELLSAMKL-PERLWSVsPATF 154
Cdd:PRK10261 389 DTLSPGKLQAL---RRDIQFIFQdpYASLDPRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLlPEHAWRY-PHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 155 SGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLAD--------QVVE 225
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHrvavmylgQIVE 544
|
....*....
gi 1706422447 226 LAPPPAVEE 234
Cdd:PRK10261 545 IGPRRAVFE 553
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-224 |
9.39e-22 |
|
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: 93.35 E-value: 9.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrDamGHEL-DLVLASehqileLRRReIGFVTQflhcl 106
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-D--GQDIrDVTQAS------LRAA-IGIVPQ----- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 prqatlDVVaqpLF-----------ALGVSRDVARQ--RAAELLS-AMKLPERLwsvspAT--------FSGGERQRVNL 164
Cdd:COG5265 440 ------DTV---LFndtiayniaygRPDASEEEVEAaaRAAQIHDfIESLPDGY-----DTrvgerglkLSGGEKQRVAI 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATaERVIglIEGLK--AEGTAMLAIFHhpettrRL-----ADQVV 224
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRT-ERAI--QAALRevARGRTTLVIAH------RLstivdADEIL 563
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-222 |
9.46e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEG----YGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRT--YLPS---AGRILYR 71
Cdd:PRK14239 1 MTEPILQVSDlsvyYNKKKALN----------SVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 72 damGHEldlVLASEHQILELRRrEIGFVTQFLHCLPRQATLDVVaqplFALGVS--RDVARQRAA---ELLSAM---KLP 143
Cdd:PRK14239 71 ---GHN---IYSPRTDTVDLRK-EIGMVFQQPNPFPMSIYENVV----YGLRLKgiKDKQVLDEAvekSLKGASiwdEVK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 144 ERLWSvSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTaMLAIFHHPETTRRLADQ 222
Cdd:PRK14239 140 DRLHD-SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDR 216
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-186 |
1.04e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 92.09 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQILELRRREIGFVTQ-F-Lhc 105
Cdd:COG4175 44 NDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGE-----DITKLSKKELRELRRKKMSMVFQhFaL-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVAQPLFALGVSRDVARQRAAELLS-------AMKLPERLwsvspatfSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG4175 117 LPHRTVLENVAFGLEIQGVPKAERRERAREALElvglagwEDSYPDEL--------SGGMQQRVGLARALATDPDILLMD 188
|
....*...
gi 1706422447 179 EPTSSLDP 186
Cdd:COG4175 189 EAFSALDP 196
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-230 |
1.45e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgheldlvlasEHQILELRRREIGFVTQFLH 104
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL--------------DGKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPE----RLWSVSpatfsGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGaekrYIWQLS-----GGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPP 230
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGP 206
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-224 |
1.55e-21 |
|
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: 92.86 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEL-DLVLASehqilelRRREIGFVTQF 102
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD---GHDLaDYTLAS-------LRRQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPrqatlDVVAQPLfALGVSRDVAR---QRAAELLSAM----KLPERLWS---VSPATFSGGERQRVNLARGFIAKP 172
Cdd:TIGR02203 415 VVLFN-----DTIANNI-AYGRTEQADRaeiERALAAAYAQdfvdKLPLGLDTpigENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 173 RLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMlaIFHHPETTRRLADQVV 224
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTL--VIAHRLSTIEKADRIV 538
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-228 |
2.59e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFqlhEQNKLIpssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdAMGHELdlvla 83
Cdd:COG0488 314 KVLELEGLSKSY---GDKTLL---DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----KLGETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 sehqilelrrrEIGFVTQFLHCLPRQAT-LDVVAQplfalgVSRDVARQRAAELLSAMKL-PERLWS-VSpaTFSGGERQ 160
Cdd:COG0488 379 -----------KIGYFDQHQEELDPDKTvLDELRD------GAPGGTEQEVRGYLGRFLFsGDDAFKpVG--VLSGGEKA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERvigLIEGLKA-EGTAMLaIFHHPETTRRLADQVVELAP 228
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEA---LEEALDDfPGTVLL-VSHDRYFLDRVATRILEFED 504
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
29-224 |
3.73e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYR------------DAMGHE--LDLVLASEHQILELRRR 94
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkglrigylpqepPLDDDLtvLDTVLDGDAELRALEAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 95 EIGFVTQFLHCLPRQATLDVVAQPLFALGVSRdvARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRL 174
Cdd:COG0488 96 LEELEAKLAEPDEDLERLAELQEEFEALGGWE--AEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1706422447 175 LLLDEPTSSLDpatAERVIGLIEGLKAEGTAMLAIFHhpetTRRLADQVV 224
Cdd:COG0488 174 LLLDEPTNHLD---LESIEWLEEFLKNYPGTVLVVSH----DRYFLDRVA 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
29-227 |
4.06e-21 |
|
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: 87.63 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGeLTALIGPTGAGKSSVLKGIYRTYLPSAGRILY--RDAMGheldlvlasehQILELRRReIGFVTQFLHCL 106
Cdd:cd03264 18 GVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLK-----------QPQKLRRR-IGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:cd03264 85 PNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706422447 187 ATAERVIGLIEGLKAEGTAMLAIfHHPETTRRLADQVVELA 227
Cdd:cd03264 164 EERIRFRNLLSELGEDRIVILST-HIVEDVESLCNQVAVLN 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-223 |
1.01e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEHQILELRRREIGFVTQFLHC-LP 107
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD-----TLITSTSKNKDIKQIRKKVGLVFQFPESqLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFV 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-213 |
2.06e-20 |
|
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: 86.17 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGI-------YRTYlpsaGRILYRdamGHELdlvlaSEHQIlelrRREIGFVTQ 101
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAIsgrveggGTTS----GQILFN---GQPR-----KPDQF----QKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 ---FLHCLPRQATLDVVAQplFALGV-SRDVARQRAAE--LLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:cd03234 89 ddiLLPGLTVRETLTYTAI--LRLPRkSSDAIRKKRVEdvLLRDLAL-TRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQP 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-226 |
2.44e-20 |
|
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: 85.99 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVlasEHQILelrRREIGFVTQFLHCLPR 108
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD---GKPISQY---EHKYL---HSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATlDVVAQPLFALGVSRDVARQRAAELLS-AMKLPERLWS---VSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSL 184
Cdd:cd03248 103 SLQ-DNIAYGLQSCSFECVKEAAQKAHAHSfISELASGYDTevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 185 DPATAERVIGLIEGlKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:cd03248 182 DAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVL 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-238 |
2.66e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAGriLYRDAMGHeldLVLASEHQILelrrreigFVTQFLHcLP 107
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AG--LWPYGSGR---IARPAGARVL--------FLPQRPY-LP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATL-DVVAQPlfalGVSRDVARQRAAELLSAMKLP---ERL-----WSvspATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:COG4178 439 -LGTLrEALLYP----ATAEAFSDAELREALEAVGLGhlaERLdeeadWD---QVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 179 EPTSSLDPATAERVIGLiegLKAE--GTAMLAIFHHPeTTRRLADQVVELAPPPAVEELLEE 238
Cdd:COG4178 511 EATSALDEENEAALYQL---LREElpGTTVISVGHRS-TLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-233 |
3.07e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLK------GIYRTYLPSAGRILYRDAMGHELDLVLAsehqilelrRREIGFVTQF 102
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKvlnrliEIYDSKIKVDGKVLYFGKDIFQIDAIKL---------RKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQATLDVVAQPLFALGVS--RDVaRQRAAELLSAMKLPERLWSV--SPAT-FSGGERQRVNLARGFIAKPRLLLL 177
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKekREI-KKIVEECLRKVGLWKEVYDRlnSPASqLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 178 DEPTSSLDPATAERVIGLIEGLKAEgTAMLAIFHHPETTRRLADQVVELAPPPAVE 233
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-224 |
5.76e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.23 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdAMGhelDLVLASEHQILELR--RREIGFVTQFL-HC 105
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV----TIG---ERVITAGKKNKKLKplRKKVGIVFQFPeHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATL-DVVAQPLfALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLArGFIA-KPRLLLLDEPTSS 183
Cdd:PRK13634 98 LFEETVEkDICFGPM-NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIA-GVLAmEPEVLVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 184 LDPATAERVIGLIEGLKAEG--TAMLaIFHHPETTRRLADQVV 224
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKglTTVL-VTHSMEDAARYADQIV 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-228 |
6.04e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 2 NPPILQVEGYGkhFQLHEQNKLipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLV 81
Cdd:PRK10247 4 NSPLLQLQNVG--YLAGDAKIL----NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGE-----DIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 82 LASEhqilELRRREIGFVTQflhcLPRQATLDVVAQPLFALGVSRD-VARQRAAELLSAMKLPERLWSVSPATFSGGERQ 160
Cdd:PRK10247 73 TLKP----EIYRQQVSYCAQ----TPTLFGDTVYDNLIFPWQIRNQqPDPAIFLDDLERFALPDTILTKNIAELSGGEKQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRlADQVVELAP 228
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEINH-ADKVITLQP 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-233 |
6.10e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 6.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLHEQN-------KLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGH 76
Cdd:PRK15079 7 VLLEVADLKVHFDIKDGKqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW---LGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 77 elDLVLASEHQILElRRREIGFVTQF-LHCL-PRQATLDVVAQPL--FALGVSRDVARQRAAELLSAMKLPERLWSVSPA 152
Cdd:PRK15079 84 --DLLGMKDDEWRA-VRSDIQMIFQDpLASLnPRMTIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 153 TFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPA 231
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHA 240
|
..
gi 1706422447 232 VE 233
Cdd:PRK15079 241 VE 242
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-213 |
7.34e-20 |
|
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: 87.88 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYrDamGHELDLvlasehqileLRRREIGfvtQFLH 104
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARllvGVWP---PTAGSVRL-D--GADLSQ----------WDREELG---RHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPrQatlDVVaqpLFALGVSRDVAR---------QRAAELLSA----MKLPE----RLwSVSPATFSGGERQRVNLARG 167
Cdd:COG4618 410 YLP-Q---DVE---LFDGTIAENIARfgdadpekvVAAAKLAGVhemiLRLPDgydtRI-GEGGARLSGGQRQRIGLARA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 168 FIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP 527
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
7.86e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.04 E-value: 7.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFqlheqNKLIpSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDL 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF-----GGLL-AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR---GQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VlaSEHQILELrrreiGFVTQFLHC-LPRQATLD---VVAQ----------PLFALGVSRDVARQ---RAAELLSAMKLP 143
Cdd:PRK11300 72 L--PGHQIARM-----GVVRTFQHVrLFREMTVIenlLVAQhqqlktglfsGLLKTPAFRRAESEaldRAATWLERVGLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 144 ErLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFH 211
Cdd:PRK11300 145 E-HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-215 |
9.78e-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: 84.08 E-value: 9.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamghelDLVLASEHQILELRRReIGFVTQflh 104
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI--------DGVDISKIGLHDLRSR-ISIIPQ--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clprqatlDVVaqpLFA---------LGVSRDVARQRAAELlSAMK-----LPERLWSV---SPATFSGGERQRVNLARG 167
Cdd:cd03244 86 --------DPV---LFSgtirsnldpFGEYSDEELWQALER-VGLKefvesLPGGLDTVveeGGENLSVGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 168 FIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTaMLAIFHHPET 215
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT-VLTIAHRLDT 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-223 |
1.14e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGYGKHFQLHEQNKlipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVL 82
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLK------GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 83 AseHQIlelrrrEIGFVTQFLHCLPRQATLDVVaqpLFALGVSRDvARQRAAELLSAMKLPERLwSVSPATFSGGERQRV 162
Cdd:PRK15439 83 A--HQL------GIYLVPQEPLLFPNLSVKENI---LFGLPKRQA-SMQKMKQLLAALGCQLDL-DSSAGSLEVADRQIV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 163 NLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-239 |
1.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.10 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldLVLASEHQILELRRREIGFVTQFL-HCLP 107
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-------VDITDKKVKLSDIRKKVGLVFQYPeYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLP-ERLWSVSPATFSGGERQRVNLArGFIA-KPRLLLLDEPTSSLD 185
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIA-GVVAmEPKILILDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706422447 186 PATAERVIGLIEGLKAEgTAMLAIF--HHPETTRRLADQV-------VELAPPPAV----EELLEEI 239
Cdd:PRK13637 177 PKGRDEILNKIKELHKE-YNMTIILvsHSMEDVAKLADRIivmnkgkCELQGTPREvfkeVETLESI 242
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-185 |
1.48e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.91 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVLAsehqilelRRREIGFVTQFlHCLP 107
Cdd:PRK10851 19 NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH---GTDVSRLHA--------RDRKVGFVFQH-YALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQAT-LDVVAqplFALGV-------SRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:PRK10851 87 RHMTvFDNIA---FGLTVlprrerpNAAAIKAKVTQLLEMVQL-AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
....*.
gi 1706422447 180 PTSSLD 185
Cdd:PRK10851 163 PFGALD 168
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
31-227 |
1.50e-19 |
|
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: 83.37 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 31 SFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvlasEHQILELRRREIGFVTQ----FLHCL 106
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ-----------SHTGLAPYQRPVSMLFQennlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQaTLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:TIGR01277 87 VRQ-NIGLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRL----PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 187 ATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELA 227
Cdd:TIGR01277 162 LLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-221 |
1.99e-19 |
|
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: 83.75 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEHQilelR-RREIGFvtqflhcL 106
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-----QDITKLPMHK----RaRLGIGY-------L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLD---VVAQPLFA----LGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:cd03218 81 PQEASIFrklTVEENILAvleiRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLAD 221
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITD 201
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-213 |
2.49e-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: 86.25 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamghELDLVlasehqilELRRREIGFVTQFLHCLPR 108
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV--------RLDGA--------DLKQWDRETFGKHIGYLPQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLdvvaqplFALGVSRDVARQR----------AAELLSAMKLPERL-----WSVSP--ATFSGGERQRVNLARGFIAK 171
Cdd:TIGR01842 400 DVEL-------FPGTVAENIARFGenadpekiieAAKLAGVHELILRLpdgydTVIGPggATLSGGQRQRIALARALYGD 472
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRP 514
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
29-213 |
2.91e-19 |
|
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: 85.88 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQILELRRReIGFVTQFLHclpr 108
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT--------LDGVPVSSLDQDEVRRR-VSVCAQDAH---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qatldvvaqpLFA------LGVSR-DVARQRAAELLSAMKL-------PERLWSV---SPATFSGGERQRVNLARGFIAK 171
Cdd:TIGR02868 420 ----------LFDttvrenLRLARpDATDEELWAALERVGLadwlralPDGLDTVlgeGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 172 PRLLLLDEPTSSLDPATAERvigLIEGLKA--EGTAMLAIFHHP 213
Cdd:TIGR02868 490 APILLLDEPTEHLDAETADE---LLEDLLAalSGRTVVLITHHL 530
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-224 |
6.59e-19 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 82.21 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 32 FTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIL--------YRDAMG-----HEL--DLVLASEHQILELRRREI 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKvagaspgkGWRHIGyvpqrHEFawDFPISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 97 GFVTQflhclPRQATLDVVAQPLFALGVSrDVARQRAAELlsamklperlwsvspatfSGGERQRVNLARGFIAKPRLLL 176
Cdd:TIGR03771 81 GWLRR-----PCVADFAAVRDALRRVGLT-ELADRPVGEL------------------SGGQRQRVLVARALATRPSVLL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:TIGR03771 137 LDEPFTGLDMPTQELLTELFIELAGAGTAILMTTHDLAQAMATCDRVV 184
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-227 |
8.17e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASehqilelrrREIGFVtqflhclPRQ 109
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---------RRVASV-------PQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATL--DVVAQPLFALG----VSR--------DVARQRAAELLSAMKLPERlwsvSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:PRK09536 86 TSLsfEFDVRQVVEMGrtphRSRfdtwtetdRAAVERAMERTGVAQFADR----PVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-216 |
8.20e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHqilELRRREIGFvtqflhcLPR 108
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE-----DISLLPLH---ARARRGIGY-------LPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QAT----LDVVAQPLFALGVSRDVARQ----RAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK10895 86 EASifrrLSVYDNLMAVLQIRDDLSAEqredRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETT 216
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRET 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
1.01e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEQNKLIPSshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPS------AGRILYrdam 74
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVN--DVSLQIEAGETLALVGESGSGKSVTALSILR-LLPSppvvypSGDIRF---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 75 gHELDLVLASEHQILELRRREIGFVTQF-------LHCLPRQATlDVVAqplFALGVSRDVARqraAELLSAM------K 141
Cdd:PRK15134 74 -HGESLLHASEQTLRGVRGNKIAMIFQEpmvslnpLHTLEKQLY-EVLS---LHRGMRREAAR---GEILNCLdrvgirQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 142 LPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLA 220
Cdd:PRK15134 146 AAKRL-TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLA 224
|
250
....*....|....
gi 1706422447 221 DQVVELAPPPAVEE 234
Cdd:PRK15134 225 DRVAVMQNGRCVEQ 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-223 |
1.12e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.81 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 16 QLHEQNKLIPsshnVSFTVRAGELTALIGPTGAGKSSVLKGIYRTyLPSAGRILYrdaMGHELdlvlaSEHQILELRRRE 95
Cdd:COG4138 5 DVAVAGRLGP----ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILL---NGRPL-----SDWSAAELARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 96 IgfvtqflhCLPRQATldvvaqPLFALGV------------SRDVARQRAAELLSAMKLPERL-WSVSpaTFSGGERQRV 162
Cdd:COG4138 72 A--------YLSQQQS------PPFAMPVfqylalhqpagaSSEAVEQLLAQLAEALGLEDKLsRPLT--QLSGGEWQRV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 163 NLARGFI-------AKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:COG4138 136 RLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRV 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-223 |
1.21e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgHELDLVLASEHQILElrrREIGFVTQFLHCLPR 108
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI-----DGQEMRFASTTAALA---AGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QAtldvVAQPLFaLG--------VSRDVARQRAAELLSAMKLperlwSVSPAT----FSGGERQRVNLARGFIAKPRLLL 176
Cdd:PRK11288 94 MT----VAENLY-LGqlphkggiVNRRLLNYEAREQLEHLGV-----DIDPDTplkyLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAI 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-239 |
1.21e-18 |
|
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: 84.08 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLHEQNkLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdaMGHELdlVLA 83
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRG-VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR--VGDEW--VDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 SEHQILELRR--REIGFVTQFLHCLPRQATLDVVAQPLfALGVSRDVARQRAAELLSAM----KLPERLWSVSPATFSGG 157
Cdd:TIGR03269 353 TKPGPDGRGRakRYIGILHQEYDLYPHRTVLDNLTEAI-GLELPDELARMKAVITLKMVgfdeEKAEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV--------VELAP 228
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAalmrdgkiVKIGD 511
|
250
....*....|.
gi 1706422447 229 PpavEELLEEI 239
Cdd:TIGR03269 512 P---EEIVEEL 519
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-234 |
1.53e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGrilYRdamgHELDLVLASE-----HQILELRRReIGFVTQFLH 104
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---YR----YSGDVLLGGRsifnyRDVLEFRRR-VGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPRQATLDVVA----QPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK14271 112 PFPMSIMDNVLAgvraHKLVPRKEFRGVAQARLTEVGLWDAVKDRL-SDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 181 TSSLDPATAERVIGLIEGLkAEGTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-224 |
1.68e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.86 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrDAMGHElDLVLASehqilelRRREIGFVTQflh 104
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGTDIR-TVTRAS-------LRRNIAVVFQ--- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clprqatldvvAQPLFA------LGVSR----DVARQRAAELLSAMKLPERlwsvSPATF-----------SGGERQRVN 163
Cdd:PRK13657 417 -----------DAGLFNrsiednIRVGRpdatDEEMRAAAERAQAHDFIER----KPDGYdtvvgergrqlSGGERQRLA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMlaIFHHPETTRRLADQVV 224
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTF--IIAHRLSTVRNADRIL 540
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-223 |
2.04e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFqlheqnKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDL 80
Cdd:PRK09700 1 MATPYISMAGIGKSF------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASE------HQ----ILELRRREIGFVTqflhclpRQATLDVVAQPLfalgVSRDVARQRAAELLSAMKLPERLwSVS 150
Cdd:PRK09700 75 KLAAQlgigiiYQelsvIDELTVLENLYIG-------RHLTKKVCGVNI----IDWREMRVRAAMMLLRVGLKVDL-DEK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 151 PATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK09700 143 VANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-226 |
2.09e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.62 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASE--HQILelrRREIGFVTQflhcL 106
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL--------LDGVPLVQydHHYL---HRQVALVGQ----E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLDVVAQPLFALGVSRDVARQRAAELLSA----MKLPERLWSVSPAT---FSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVGEKgsqLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 180 PTSSLDpATAERVIGliEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:TIGR00958 644 ATSALD-AECEQLLQ--ESRSRASRTVLLIAHRLSTVER-ADQILVL 686
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
29-221 |
3.17e-18 |
|
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: 80.40 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEHqilELRRREIGFvtqflhcLPR 108
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDG-----QDITHLPMH---ERARLGIGY-------LPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLD---VVAQPLFAL-----GVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:TIGR04406 84 EASIFrklTVEENIMAVleirkDLDRAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLAD 221
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICD 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
3.42e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFqlheqnKLIPSSHNVSFTVRAGELTALIGPTGAGKSS---VLKGIYR--TYlpsAGRILYRdamG 75
Cdd:PRK13549 1 MMEYLLEMKNITKTF------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVYPhgTY---EGEIIFE---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 76 HELdlvlaSEHQILELRRREIGFVTQFLhCLPRQATldvVAQPLFaLG--------VSRDVARQRAAELLSAMKLperlw 147
Cdd:PRK13549 69 EEL-----QASNIRDTERAGIAIIHQEL-ALVKELS---VLENIF-LGneitpggiMDYDAMYLRAQKLLAQLKL----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 148 SVSPAT----FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK13549 134 DINPATpvgnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-192 |
7.90e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFQLheqnklIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdaMGHELDLVLA 83
Cdd:PRK11607 18 PLLEIRNLTKSFDG------QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-----MLDGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 SEHQilelrrREIGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPErLWSVSPATFSGGERQRVN 163
Cdd:PRK11607 87 PPYQ------RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVA 159
|
170 180
....*....|....*....|....*....
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDPATAERV 192
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRM 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-221 |
9.79e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 11 YGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRT--YLPSA---GRILYRdamGHELdlvLASE 85
Cdd:PRK14243 20 YGSFLAVK----------NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFH---GKNL---YAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 HQILELRRReIGFVTQFLHCLPRqATLDVVAQPLFALGVSRD----VARQ-RAAELLSAMKlpERLwSVSPATFSGGERQ 160
Cdd:PRK14243 84 VDPVEVRRR-IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDmdelVERSlRQAALWDEVK--DKL-KQSGLSLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLaIFHHPETTRRLAD 221
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIII-VTHNMQQAARVSD 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-224 |
1.06e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 78.34 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGI--YRTYLPSAGRILYRDamgheldlvlaseHQILELRRREIgfvtqflhc 105
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKG-------------EDITDLPPEER--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lprqatldvvaqplFALGVSrdVARQRAAELlSAMKLPERLWSVSpATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03217 75 --------------ARLGIF--LAFQYPPEI-PGVKNADFLRYVN-EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 186 pATAERVIG-LIEGLKAEGTAMLAIFHHpettRRLADQVV 224
Cdd:cd03217 137 -IDALRLVAeVINKLREEGKSVLIITHY----QRLLDYIK 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-224 |
1.12e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 78.41 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlHEQNKLipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheldlVLASE 85
Cdd:cd03268 1 LKTNDLTKTY--GKKRVL----DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----------FDGKS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 HQILELRRREIGFVTQ----FLHCLPRQAtldvvaqpLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQR 161
Cdd:cd03268 64 YQKNIEALRRIGALIEapgfYPNLTAREN--------LRLLARLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 162 VNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-224 |
1.16e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlHEQNKLipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlase 85
Cdd:PRK11247 13 LLLNAVSKRY--GERTVL----NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 86 hqilelrRREIGFVTQFLHCLPRQATLDVVAqplfaLGVSRDvARQRAAELLSAMKLPERL--WsvsPATFSGGERQRVN 163
Cdd:PRK11247 80 -------REDTRLMFQDARLLPWKKVIDNVG-----LGLKGQ-WRDAALQALAAVGLADRAneW---PAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVL 205
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-215 |
1.77e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.08 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 37 GELTALIGPTGAGKSSVLKGIyrtylpsAGRILYRDAMGHeldlVLASEHQILELRRREIGFVTQ----FLHCLPRQaTL 112
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGT----ILANNRKPTKQILKRTGFVTQddilYPHLTVRE-TL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 113 DVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPATF----SGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:PLN03211 162 VFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180
....*....|....*....|....*..
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFHHPET 215
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
28-227 |
1.77e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRD-AMGHELDLVLAsehqilelrrREIGFVTQfLHCL 106
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkPISMLSSRQLA----------RRLALLPQ-HHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRqatlDVVAQPLFALGVS-----------RDVAR-QRAAELLSAMKLPERLWSvspaTFSGGERQRVNLARGFIAKPRL 174
Cdd:PRK11231 88 PE----GITVRELVAYGRSpwlslwgrlsaEDNARvNQAMEQTRINHLADRRLT----DLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 175 LLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLA 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-185 |
2.26e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQIlelRRREIGFVTQFLHCLPR 108
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF--------IDGEDVTHRSI---QQRDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAEllsAMKLperlwsVSPATF--------SGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQRVKE---ALEL------VDLAGFedryvdqiSGGQQQRVALARALILKPKVLLFDEP 163
|
....*
gi 1706422447 181 TSSLD 185
Cdd:PRK11432 164 LSNLD 168
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-226 |
2.47e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.69 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlaSEHQILELRRReIGFV----- 99
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITL-----TAKTVWDIREK-VGIVfqnpd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 TQFLhclprQATL-DVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSvSPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:PRK13640 95 NQFV-----GATVgDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDS-EPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTrRLADQVVEL 226
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVL 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-224 |
3.20e-17 |
|
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: 77.76 E-value: 3.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 18 HEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRIlyrDAMGheldlVLASEHQILELRRr 94
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKilsGLLQ---PTSGEV---RVAG-----LVPWKRRKKFLRR- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 95 eIGFV----TQFLHCLPRQATLDVVAQplfALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIA 170
Cdd:cd03267 96 -IGVVfgqkTQLWWDLPVIDSFYLLAA---IYDLPPARFKKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 171 KPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVL 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
23-211 |
3.33e-17 |
|
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: 77.07 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 23 LIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamghELDLVLASEHQILELRRReigfvtqf 102
Cdd:cd03369 20 LPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI--------EIDGIDISTIPLEDLRSS-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQATldvvaqpLFALGVSRDV---ARQRAAELLSAMKLPErlwsvSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:cd03369 84 LTIIPQDPT-------LFSGTIRSNLdpfDEYSDEEIYGALRVSE-----GGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTaMLAIFH 211
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNST-ILTIAH 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-223 |
3.59e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.83 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSS---VLKGIYR--TYlpsAGRILYRDAMGHELDLVlASEHqilelrrREIGFVTQFL 103
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTlmkVLSGVYPhgSY---EGEILFDGEVCRFKDIR-DSEA-------LGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLPrqatLDVVAQPLFaLG--------VSRDVARQRAAELLSAMKLPErlwsvSPATFSG----GERQRVNLARGFIAK 171
Cdd:NF040905 88 ALIP----YLSIAENIF-LGnerakrgvIDWNETNRRARELLAKVGLDE-----SPDTLVTdigvGKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
42-185 |
4.89e-17 |
|
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: 78.69 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 42 LIGPTGAGKSSVLKGIYRTYLPSAGRILyrdaMGHElDLVLASEHqilelrRREIGFVTQFLHCLPRQATLDVVAQPLFA 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM----LDGE-DVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKM 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 122 LGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-223 |
4.99e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.31 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 16 QLHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEHQILELRRRE 95
Cdd:PRK10070 33 QILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG-----VDIAKISDAELREVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 96 IGFVTQFLHCLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEGT-AMLAIFHHPETTRRLADQV 223
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRI 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-226 |
5.49e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 77.75 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQlheQNKLIpssHNVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAGRILYRDAMGHELDLV--- 81
Cdd:PRK09984 4 IIRVEKLAKTFN---QHQAL---HAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELLgrt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 82 ------LASEhqiLELRRREIGFVTQFLHCLPRQATLDVV------AQPLFALGVS--RDVARQRAAELLSAMKLP---- 143
Cdd:PRK09984 71 vqregrLARD---IRKSRANTGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSwfTREQKQRALQALTRVGMVhfah 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 144 ERLwsvspATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLADQ 222
Cdd:PRK09984 148 QRV-----STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCER 222
|
....
gi 1706422447 223 VVEL 226
Cdd:PRK09984 223 IVAL 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-203 |
8.24e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSV---LKGIYRtylPSAGRILYRdamGHELDLvlaSEHQILELRRReIGFVTQ---- 101
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLflhFNGILK---PTSGEVLIK---GEPIKY---DKKSLLEVRKT-VGIVFQnpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 --FLhclPRQATlDVVAQPLfALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLArGFIA-KPRLLLLD 178
Cdd:PRK13639 90 qlFA---PTVEE-DVAFGPL-NLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIA-GILAmKPEIIVLD 162
|
170 180
....*....|....*....|....*
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAEG 203
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEG 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-226 |
8.73e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamgheLDLVLASEHQileLRRREIGFVTQFLHcLPRQ 109
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV-------LGVPVPARAR---LARARIGVVPQFDN-LDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATldvVAQPLFALG-VSRDVARQRAAELLSAMKLP--ERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PRK13536 129 FT---VRENLLVFGrYFGMSTREIEAVIPSLLEFArlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 187 ATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-212 |
1.08e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQilelRRREIGFVTQFlhclP 107
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-----DVTKLPEYK----RAKYIGRVFQD----P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQAT---LdVVAQPL-----------FALGVSRDVaRQRAAELLSAMK--LPERLwSVSPATFSGGERQRVNLARGFIAK 171
Cdd:COG1101 90 MMGTapsM-TIEENLalayrrgkrrgLRRGLTKKR-RELFRELLATLGlgLENRL-DTKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLKAEG--TAMLaIFHH 212
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLM-VTHN 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-227 |
1.09e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKS---SVLKGIYRTYLPSAGRILYRdamGHELDLVlasehqilELRRREiGFVTQ--- 101
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTtlmNALAFRSPKGVKGSGSVLLN---GMPIDAK--------EMRAIS-AYVQQddl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 FLHCLPRQATLDVVAQplFALG--VSRDVARQRAAELLSAMKL----------PERLWSVSpatfsGGERQRVNLARGFI 169
Cdd:TIGR00955 110 FIPTLTVREHLMFQAH--LRMPrrVTKKEKRERVDEVLQALGLrkcantrigvPGRVKGLS-----GGERKRLAFASELL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 170 AKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETT-RRLADQVVELA 227
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSElFELFDKIILMA 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-211 |
1.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 18 HEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdAMGHELdlvlaSEHQILELRRReIG 97
Cdd:PRK13650 14 YKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQII---IDGDLL-----TEENVWDIRHK-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 98 FV-----TQFLhclprQATL-DVVAQPLFALGVSRDVARQR---AAELLSAMKLPERlwsvSPATFSGGERQRVNLArGF 168
Cdd:PRK13650 85 MVfqnpdNQFV-----GATVeDDVAFGLENKGIPHEEMKERvneALELVGMQDFKER----EPARLSGGQKQRVAIA-GA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 169 IA-KPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFH 211
Cdd:PRK13650 155 VAmRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
28-226 |
1.63e-16 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 78.01 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY-----RDAMGHELDLVLASEHQILELRRREIGfvtQF 102
Cdd:TIGR01192 352 FDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIdgidiNTVTRESLRKSIATVFQDAGLFNRSIR---EN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQATLDVVAQPLFALGVSrDVARQRAAELLSAMKlpERlwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:TIGR01192 429 IRLGREGATDEEVYEAAKAAAAH-DFILKRSNGYDTLVG--ER-----GNRLSGGERQRLAIARAILKNAPILVLDEATS 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 183 SLDPATAERVIGLIEGLKAEGTAMlaIFHHPETTRRLADQVVEL 226
Cdd:TIGR01192 501 ALDVETEARVKNAIDALRKNRTTF--IIAHRLSTVRNADLVLFL 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
28-226 |
1.63e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 75.20 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsagrilyrdaMGhELDLVLASehqiLELRRReIGFVTQ--FLhc 105
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSAL----------------LG-ELEKLSGS----VSVPGS-IAYVSQepWI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lpRQATL-DVVaqpLFalGVSRDVARQ----RAAELLSAMK-LP--------ERlwsvsPATFSGGERQRVNLARGFIAK 171
Cdd:cd03250 78 --QNGTIrENI---LF--GKPFDEERYekviKACALEPDLEiLPdgdlteigEK-----GINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIG-LIEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVL 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-203 |
1.67e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSV---LKGIYRtylPSAGRILYRDamgheLDLVLASEHQilelR-RREIGFVTQ-- 101
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTTfymIVGLVK---PDSGRIFLDG-----EDITHLPMHK----RaRLGIGYLPQea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 --FlhclpRQATldvVAQPLFA----LGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:COG1137 88 siF-----RKLT---VEDNILAvlelRKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180
....*....|....*....|....*...
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEG 203
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
29-229 |
1.75e-16 |
|
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: 74.11 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLK---GIYRTYlpsAGRILYrdamgheldlvlasehqileLRRREIGFVTQflhc 105
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRalaGLWPWG---SGRIGM--------------------PEGEDLLFLPQ---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lprqatldvvaQPLFALGVSRDvarqraaellsAMKLPerlWSvspATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03223 72 -----------RPYLPLGTLRE-----------QLIYP---WD---DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 186 PATAERVIGLiegLKAEGTAMLAIFHHPeTTRRLADQVVELAPP 229
Cdd:cd03223 124 EESEDRLYQL---LKELGITVISVGHRP-SLWKFHDRVLDLDGE 163
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-226 |
2.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.94 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvLASEHQILELRRrEIGFVTQFlhclPR 108
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ--------AITDDNFEKLRK-HIGIVFQN----PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALG-----VSRDVARQRAAELLSAMKLPERLWSvSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:PRK13648 94 NQFVGSIVKYDVAFGlenhaVPYDEMHRRVSEALKQVDMLERADY-EPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 184 LDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVM 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-225 |
2.23e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.75 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 20 QNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEL-DLVLASehqilelRRREIGF 98
Cdd:PRK11176 352 PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLD---GHDLrDYTLAS-------LRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 99 VTQFLHCLPrqatlDVVAQPLfALGVSRDVARQ---RAAELLSAM----KLPERLWSV---SPATFSGGERQRVNLARGF 168
Cdd:PRK11176 422 VSQNVHLFN-----DTIANNI-AYARTEQYSREqieEAARMAYAMdfinKMDNGLDTVigeNGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 169 IAKPRLLLLDEPTSSLDPATaERVI-GLIEGLKAEGTAmLAIFHHPETTRRlADQ--VVE 225
Cdd:PRK11176 496 LRDSPILILDEATSALDTES-ERAIqAALDELQKNRTS-LVIAHRLSTIEK-ADEilVVE 552
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-223 |
2.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.65 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 11 YGKHFQLHEQNKLIPssHNVSFtvrageltALIGPTGAGKSSVLKGIYR-------TYLPSAGRILYRDAMGHELDLVLA 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIP--QNGVF--------ALMGPSGCGKSTLLRTFNRllelneeARVEGEVRLFGRNIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 84 sehqilelrRREIGFVTQFLHCLPRQATLDVVA--QPLFALGVSRDVARQRAAELLSAMKLPE----RLwSVSPATFSGG 157
Cdd:PRK14267 84 ---------RREVGMVFQYPNPFPHLTIYDNVAigVKLNGLVKSKKELDERVEWALKKAALWDevkdRL-NDYPSNLSGG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLaIFHHPETTRRLADQV 223
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL-VTHSPAQAARVSDYV 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-226 |
2.94e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.59 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlVLASEHQilELRRREIGFVTQFLHCLP 107
Cdd:PRK10575 28 HPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQ-------PLESWSS--KAFARKVAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLF----ALGVSRDVARQRAAE---LLSAMKLPERLWSvspaTFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK10575 99 GMTVRELVAIGRYpwhgALGRFGAADREKVEEaisLVGLKPLAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVAL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-234 |
4.41e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYR--TYLPSA---GRILYRDAMGHELDLVlasehqilELRRReIGFVTQFLH 104
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVI--------ELRRR-VQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPRQATLDVVA--QPLFALGVSRDVARQRAAELLSAMKLPE----RLwSVSPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:PRK14247 93 PIPNLSIFENVAlgLKLNRLVKSKKELQERVRWALEKAQLWDevkdRL-DAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAEGTAMLaIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVL-VTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-185 |
5.01e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFqlhEQNKLIPsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDL 80
Cdd:PRK09452 10 SLSPLVELRGISKSF---DGKEVIS---NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD---GQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLAsehqilelRRREIGFVTQFLHCLPRQATLDVVAqplFAL---GVSRDVARQRAAELLSAMKLpERLWSVSPATFSGG 157
Cdd:PRK09452 81 VPA--------ENRHVNTVFQSYALFPHMTVFENVA---FGLrmqKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-224 |
5.33e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 19 EQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlYRDAMGHELdlvlasEHQILELRRREiGF 98
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDTSD------EENLWDIRNKA-GM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 99 VTQFlhclPRQ---ATL---DVVAQPLfALGVSRDVARQRAAELLSAMKLPErLWSVSPATFSGGERQRVNLArGFIA-K 171
Cdd:PRK13633 90 VFQN----PDNqivATIveeDVAFGPE-NLGIPPEEIRERVDESLKKVGMYE-YRRHAPHLLSGGQKQRVAIA-GILAmR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRlADQVV 224
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRII 215
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-211 |
5.79e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 32 FTVRAGELTALIGPTGAGKSSV---LKGIyrtyLPSAGRIlYRDAMGHELDLVLASEHQILELRRREIGFVTQFlhclPR 108
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSQTafaLMGL----LAANGRI-GGSATFNGREILNLPEKELNKLRAEQISMIFQD----PM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QAT---LDVVAQPLFAL----GVSRDVARQRAAELLSAMKLPE---RLwSVSPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:PRK09473 108 TSLnpyMRVGEQLMEVLmlhkGMSKAEAFEESVRMLDAVKMPEarkRM-KMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190
....*....|....*....|....*....|....
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFH 211
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREfNTAIIMITH 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-222 |
5.88e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELdlvlaSEHQILELRRREIGFVTQFL 103
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD---GKDI-----TDWQTAKIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLPRQATLDVVAQPLFAlgVSRDVARQRAAELLSAM-KLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELFpRLHERR-IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1706422447 183 SLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQ 222
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-234 |
8.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 8.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheLDLVLASEHQILELRRREIGFVTQFlhclP 107
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD-----ITITHKTKDKYIRPVRKRIGMVFQF----P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 R-QATLDVVAQP-LFA---LGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:PRK13646 95 EsQLFEDTVEREiIFGpknFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 183 SLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELAPPPAVEE 234
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQ 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
31-224 |
1.08e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.46 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 31 SFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgheldlvlasEHQILELRRREIGFVTQ----FLHCL 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----------DHTTTPPSRRPVSMLFQennlFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQaTLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PRK10771 88 VAQ-NIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARL----PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 187 ATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK10771 163 ALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSL 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-207 |
1.31e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.35 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQN---------------KLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAG 66
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltGILV---PTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 67 RILyrdAMGHEldlvlASEHQIlELRRReIGFV----TQFLHCLPRQATLDvvaqpLFAL--GVSRDVARQRAAELLSAM 140
Cdd:COG4586 78 EVR---VLGYV-----PFKRRK-EFARR-IGVVfgqrSQLWWDLPAIDSFR-----LLKAiyRIPDAEYKKRLDELVELL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 141 KLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAML 207
Cdd:COG4586 143 DL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTIL 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-209 |
1.81e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGY--GKHFqlheqnklipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIL----------Y 70
Cdd:COG1129 254 EVVLEVEGLsvGGVV------------RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 71 RDAMGHelDLVLASEHqilelRRREiGFVTQF-------LhclprqATLDVVAQPLFalgVSRDVARQRAAELLSAMKL- 142
Cdd:COG1129 322 RDAIRA--GIAYVPED-----RKGE-GLVLDLsirenitL------ASLDRLSRGGL---LDRRRERALAEEYIKRLRIk 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 143 ---PERLwsVSpaTFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:COG1129 385 tpsPEQP--VG--NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI 450
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
1.83e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQlheqNKLIpsSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamghelDL 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYG----DKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG------EP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 VLASEHQIlelrRREIGFVTQFLHCLPR---QATLDVVAQplfALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGG 157
Cdd:PRK13537 71 VPSRARHA----RQRVGVVPQFDNLDPDftvRENLLVFGR---YFGLSAAAARALVPPLLEFAKLENKA-DAKVGELSGG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-226 |
2.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrDAMGHELdlvlaSEHQILELRRReIGFVTQFLHCLPRQ 109
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---KVMGREV-----NAENEKWVRSK-VGLVFQDPDDQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:PRK13647 95 STVwdDVAFGPV-NMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK13647 173 GQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVL 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
29-213 |
3.50e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmGHELDLVLASEHQI-------LELRRRE-IGFVT 100
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-DIDDPDVAEACHYLghrnamkPALTVAEnLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 101 QFLhclpRQATLDVVAQpLFALGVSrDVARQRAAELlsamklperlwsvspatfSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK13539 99 AFL----GGEELDIAAA-LEAVGLA-PLAHLPFGYL------------------SAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-217 |
3.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYR-TYLPSAGRILYRdamgheldlVLASEHQILELR------RREIGFVTQF 102
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmNELESEVRVEGR---------VEFFNQNIYERRvnlnrlRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPrQATLDVVAQPLFALGVSRDVARQRAAEllSAMKLPErLWS-------VSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:PRK14258 97 PNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVE--SALKDAD-LWDeikhkihKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHH--PETTR 217
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHnlHQVSR 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-224 |
4.34e-15 |
|
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: 70.92 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 2 NPPILQVEGYGKHFQLHeqnklipsshNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLV 81
Cdd:cd03215 1 GEPVLEVRGLSVKGAVR----------DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK-----PVT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 82 LASEHqilELRRREIGFVTqflhclprqatldvvaqplfalgvsRDvaRQRAAeLLSAMKLPERLwsVSPATFSGGERQR 161
Cdd:cd03215 66 RRSPR---DAIRAGIAYVP-------------------------ED--RKREG-LVLDLSVAENI--ALSSLLSGGNQQK 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 162 VNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-223 |
4.36e-15 |
|
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: 73.71 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYR--TYlpsAGRILYRdamGHELdlvlaSEHQILELRRREIGFVTQF 102
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKilsGVYPhgTW---DGEIYWS---GSPL-----KASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQAtldvVAQPLFaLG---------VSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPR 173
Cdd:TIGR02633 87 LTLVPELS----VAENIF-LGneitlpggrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1706422447 174 LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-214 |
8.35e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYL--PSAGRIlyrdamgheldlvlasehqilELRRREIGFVTQFLHCL 106
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV---------------------DVPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLDVvaqplfalgvsrdvarqrAAELLSAMKLPER-LWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:COG2401 107 GRKGDFKD------------------AVELLNAVGLSDAvLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|
gi 1706422447 186 PATAERV-IGLIEGLKAEGTAMLAIFHHPE 214
Cdd:COG2401 169 RQTAKRVaRNLQKLARRAGITLVVATHHYD 198
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-223 |
8.73e-15 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 70.89 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFQlhEQNKLipssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHEL---DLvl 82
Cdd:TIGR03740 1 LETKNLSKRFG--KQTAV----NNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFD---GHPWtrkDL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 83 asehqilelrrREIGFVTQ---FLHCLPRQATLDVVAQplfALGVSRdvarQRAAELLSAMKLpERLWSVSPATFSGGER 159
Cdd:TIGR03740 70 -----------HKIGSLIEsppLYENLTARENLKVHTT---LLGLPD----SRIDEVLNIVDL-TNTGKKKAKQFSLGMK 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:TIGR03740 131 QRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHI 194
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-226 |
1.01e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 27 SHNVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAGrilyrdamgheLDLVLASEHQILELR-------RREIGFV 99
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMI-------AG-----------LEDITSGDLFIGEKRmndvppaERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 TQFLHCLPRqatLDVVAQPLFAL---GVSRDVARQR---AAELLSAMKLPERlwsvSPATFSGGERQRVNLARGFIAKPR 173
Cdd:PRK11000 81 FQSYALYPH---LSVAENMSFGLklaGAKKEEINQRvnqVAEVLQLAHLLDR----KPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 174 LLLLDEPTSSLDPATaeRVIGLIEGLKAE---GTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK11000 154 VFLLDEPLSNLDAAL--RVQMRIEISRLHkrlGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-213 |
1.46e-14 |
|
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: 69.83 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASEhqilelrrreigfvtqfLHCLPRQ 109
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG-----------------LLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ATLDVVAQPLFALG-VSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03231 82 PGIKTTLSVLENLRfWHADHSDEQVEEALARVGL-NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-233 |
1.61e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFqlHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAG-----RILYRDAMGHELD 79
Cdd:PRK10261 12 VLAVENLNIAF--MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdKMLLRRRSRQVIE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 80 LVLASEHQILELRRREIGFVTQ--FLHCLPRQATLDVVAQPL-FALGVSRDVARQRAAELLSAMKLPER--LWSVSPATF 154
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQepMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQVRIPEAqtILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 155 SGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEgTAMLAIF--HHPETTRRLADQVVELAPPPAV 232
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKE-MSMGVIFitHDMGVVAEIADRVLVMYQGEAV 248
|
.
gi 1706422447 233 E 233
Cdd:PRK10261 249 E 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-223 |
1.83e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlheqnKLIPSSHNVSFTVRAGELTALIGPTGAgksSVLKGIYRTYL--PSAGRILYR----DAMGHELD 79
Cdd:NF000106 14 VEVRGLVKHF------GEVKAVDGVDLDVREGTVLGVLGP*GA---A**RGALPAHV*gPDAGRRPWRf*twCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 80 LVLAsEHQILELRRREIGFVTQFLHCLPRqatldvvaqplfALGVSRDVARQRAAELLSAMKLPERLWSVSpATFSGGER 159
Cdd:NF000106 85 RTIG-*HRPVR*GRRESFSGRENLYMIGR------------*LDLSRKDARARADELLERFSLTEAAGRAA-AKYSGGMR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:NF000106 151 RRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHEL 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
16-223 |
3.33e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 16 QLHEQNKLIPsshnVSFTVRAGELTALIGPTGAGKSSVLKGIYRTyLPSAGRILYrdaMGHELDLVLASEhqiLELRRre 95
Cdd:PRK03695 5 DVAVSTRLGP----LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQF---AGQPLEAWSAAE---LARHR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 96 iGFVTQ-----FLhcLPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPErlwSVSpaTFSGGERQRVNLARGFI- 169
Cdd:PRK03695 72 -AYLSQqqtppFA--MPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGR---SVN--QLSGGEWQRVRLAAVVLq 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 170 ----AKP--RLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK03695 144 vwpdINPagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRV 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
28-223 |
5.36e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLP----SAGRILyrdamgheLDLVLASEHQileLRRREIGFVTQFl 103
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVL--------LDGKPVAPCA---LRGRKIATIMQN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 hclPRQATLDV------VAQPLFALGVSRDVARQRAAelLSAMKL--PERLWSVSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:PRK10418 88 ---PRSAFNPLhtmhthARETCLALGKPADDATLTAA--LEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 176 LLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQV 223
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDV 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
28-213 |
5.57e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.94 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSS---VLKGIYRtYLPSAGRILYRDamgheldlvlaseHQILEL----RRRE---IG 97
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDG-------------EDILELspdeRARAgifLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 98 F----------VTQFLHclprqATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERlwSVSpATFSGGERQRVNLARG 167
Cdd:COG0396 83 FqypveipgvsVSNFLR-----TALNARRGEELSAREFLKLLKEKMKELGLDEDFLDR--YVN-EGFSGGEKKRNEILQM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 168 FIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-224 |
5.94e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.25 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSV---LKGIYRtylPSAGRILYRDamgheldlVLASEHQILELRRREIGFV-- 99
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLR---PQKGKVLVSG--------IDTGDFSKLQGIRKLVGIVfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 ---TQFLHclpRQATLDVVAQPLfALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:PRK13644 85 npeTQFVG---RTVEEDLAFGPE-NLCLPPIEIRKRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVV 224
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRII 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-211 |
9.12e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMgheldlvlasehqilelrrrEIGFVTQFLHClp 107
Cdd:PRK09544 21 SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL--------------------RIGYVPQKLYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATLDVVAQPLFAL--GVSRD-----VARQRAAELLSA--MKLperlwsvspatfSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:PRK09544 79 -DTTLPLTVNRFLRLrpGTKKEdilpaLKRVQAGHLIDApmQKL------------SGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFH 211
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSH 179
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-227 |
1.25e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmgHELDLVlasehqILELRRREIGFVTQ------- 101
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDI------NLKWWRSKIGVVSQdpllfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 -----FLHCLPRQATLDVVAQPLFALGVS-------RDVARQRAA-------------ELLSAMK--------------- 141
Cdd:PTZ00265 475 siknnIKYSLYSLKDLEALSNYYNEDGNDsqenknkRNSCRAKCAgdlndmsnttdsnELIEMRKnyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 142 ----------LPER---LWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLA 208
Cdd:PTZ00265 555 kvlihdfvsaLPDKyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250
....*....|....*....
gi 1706422447 209 IFHHPETTRRLADQVVELA 227
Cdd:PTZ00265 635 IIAHRLSTIRYANTIFVLS 653
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-231 |
1.87e-13 |
|
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: 67.49 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELD------LVLASEHQILELR--RREIGF-V 99
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE---GKQITepgpdrMVVFQNYSLLPWLtvRENIALaV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 TQFLHCLPRQATLDVVAQPLFALGVsrdvarQRAAEllsamKLPERLwsvspatfSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:TIGR01184 80 DRVLPDLSKSERRAIVEEHIALVGL------TEAAD-----KRPGQL--------SGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 180 PTSSLDPATAERVI-GLIEGLKAEGTAMLAIFHHPETTRRLADQVVELAPPPA 231
Cdd:TIGR01184 141 PFGALDALTRGNLQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-227 |
2.95e-13 |
|
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: 66.13 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRTYLPSAGRILYRdamGHELDlvlasehQILELRRREIGFVTQ--- 101
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKalaNRTEGNVSVEGDIHYN---GIPYK-------EFAEKYPGEIIYVSEedv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 FLHCLPRQATLDvvaqplFALgvsrdvaRQRAAELLSAmklperlwsvspatFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:cd03233 94 HFPTLTVRETLD------FAL-------RCKGNEFVRG--------------ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 182 SSLDPATAERVIGLIEGL--KAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:cd03233 147 RGLDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLY 194
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-193 |
3.66e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSS---VLKGiyrtYLPSAGRILYRdamGHEL-DLVLASehqilelRRREIGFVTQFLH 104
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSllnALLG----FLPYQGSLKIN---GIELrELDPES-------WRKHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 cLPRQATLDVVAqplfaLG--------VSRDVARQRAAELLSamKLPERLWSV---SPATFSGGERQRVNLARGFIAKPR 173
Cdd:PRK11174 434 -LPHGTLRDNVL-----LGnpdasdeqLQQALENAWVSEFLP--LLPQGLDTPigdQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180
....*....|....*....|
gi 1706422447 174 LLLLDEPTSSLDPATAERVI 193
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVM 525
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-213 |
4.41e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLkgiyrtylpsagRIL-YRDAMGHELDLVLASEHQILELRRREIGFVTQF-LHc 105
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLL------------DVLaGRKTAGVITGEILINGRPLDKNFQRSTGYVEQQdVH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lprQATLDVvaqplfalgvsrdvarqRAAELLSAmKLpeRLWSVSpatfsggERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:cd03232 91 ---SPNLTV-----------------REALRFSA-LL--RGLSVE-------QRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*...
gi 1706422447 186 PATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQP 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-226 |
1.47e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAgeLTALIGPTGAGKSSV---LKGIYRtylPSAGRILYRdamGHELDLvlaSEHQILELRRrEIGFVTQFlhc 105
Cdd:PRK13638 21 NLDFSLSP--VTGLVGANGCGKSTLfmnLSGLLR---PQKGAVLWQ---GKPLDY---SKRGLLALRQ-QVATVFQD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lPRQATL--DV---VAQPLFALGVSRDVARQRAAELLSAMKlPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK13638 86 -PEQQIFytDIdsdIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-212 |
1.66e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 15 FQLHEQnkliPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDLVLASEHQilelrrr 94
Cdd:PRK13540 9 FDYHDQ----PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF---ERQSIKKDLCTYQK------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 95 EIGFVTqflHCLPRQATLDVVAQPLFALGVSRdvARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRL 174
Cdd:PRK13540 75 QLCFVG---HRSGINPYLTLRENCLYDIHFSP--GAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 175 LLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHH 212
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
29-226 |
1.69e-12 |
|
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: 62.85 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMgheldlvlasehqilelrrrEIGFVTQFlhclpr 108
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV--------------------KIGYFEQL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qatldvvaqplfalgvsrdvarqraaellsamklperlwsvspatfSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03221 72 ----------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 189 AERvigLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03221 106 IEA---LEEALKEYPGTVILVSHDRYFLDQVATKIIEL 140
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
29-223 |
2.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELdlvlaSEHQILELRRReIGFVTQFLHCLPR 108
Cdd:PRK13652 22 NINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR---GEPI-----TKENIREVRKF-VGLVFQNPDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATL--DVVAQPLfALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PRK13652 93 SPTVeqDIAFGPI-NLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 187 ATAERVIGLIEGLkAEGTAMLAIF--HHPETTRRLADQV 223
Cdd:PRK13652 171 QGVKELIDFLNDL-PETYGMTVIFstHQLDLVPEMADYI 208
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-193 |
2.05e-12 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 66.30 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVlaSEHQIlelrRREIGFVTQflhclp 107
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN---GFSLKDI--DRHTL----RQFINYLPQ------ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rqatldvvaQP-LFA--------LGVSRDVARQraaELLSAMKLPE--------------RLwSVSPATFSGGERQRVNL 164
Cdd:TIGR01193 556 ---------EPyIFSgsilenllLGAKENVSQD---EIWAACEIAEikddienmplgyqtEL-SEEGSSISGGQKQRIAL 622
|
170 180
....*....|....*....|....*....
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPATAERVI 193
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIV 651
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
10-239 |
3.75e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.24 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 10 GYGKHFQLHEQNKLIPSSHnvsftvrageLTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQIL 89
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGH----------FTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW--------LDGEHIQHYASK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 90 ELRRReIGFVTQFLHCLPRQATLDVVA------QPLFALGVSRDvarqrAAELLSAMKLP--ERLWSVSPATFSGGERQR 161
Cdd:PRK10253 78 EVARR-IGLLAQNATTPGDITVQELVArgryphQPLFTRWRKED-----EEAVTKAMQATgiTHLADQSVDTLSGGQRQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 162 VNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVEL---------APPPA 231
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALregkivaqgAPKEI 231
|
....*....
gi 1706422447 232 VE-ELLEEI 239
Cdd:PRK10253 232 VTaELIERI 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-226 |
4.77e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.51 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 40 TALIGPTGAGKSS---VLKGIYRtylPSAGRILYRDamghelDLVLASEHQI-LELRRREIGFVTQ----FLHclprqat 111
Cdd:PRK11144 27 TAIFGRSGAGKTSlinAISGLTR---PQKGRIVLNG------RVLFDAEKGIcLPPEKRRIGYVFQdarlFPH------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 112 LDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwsvsPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAER 191
Cdd:PRK11144 91 YKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRY----PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1706422447 192 VIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK11144 167 LLPYLERLAREiNIPILYVSHSLDEILRLADRVVVL 202
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
29-238 |
6.31e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIY----RTYLPSAGRILYRDamgheLDLVLASEHQILELRRREIGFVTQF-L 103
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICgitkDNWHVTADRFRWNG-----IDLLKLSPRERRKIIGREIAMIFQEpS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 HCLPRQATLDvvAQPLFALGVS--------RDVAR-QRAAELLS--AMKLPERLWSVSPATFSGGERQRVNLARGFIAKP 172
Cdd:COG4170 100 SCLDPSAKIG--DQLIEAIPSWtfkgkwwqRFKWRkKRAIELLHrvGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 173 RLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLAD--------QVVELAPppaVEELLEE 238
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADtitvlycgQTVESGP---TEQILKS 249
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-211 |
7.88e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlaSEHQIlelrRREIGFVTQFLHCLp 107
Cdd:PRK11160 357 KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY-----SEAAL----RQAISVVSQRVHLF- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rQATLD---VVAQPLFALGVSRDVARQRAAELLSAMKLPERLW-SVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:PRK11160 427 -SATLRdnlLLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWlGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180
....*....|....*....|....*...
gi 1706422447 184 LDPATAERVIGLIEGLkAEGTAMLAIFH 211
Cdd:PRK11160 506 LDAETERQILELLAEH-AQNKTVLMITH 532
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-192 |
1.01e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 62.95 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 14 HFQLHeqnkLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlvlasehqilelrr 93
Cdd:cd03291 44 NLCLV----GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 94 rEIGFVTQFLHCLPRQATLDVVAqplfalGVSRDVARQR----AAELLSAM-KLPERLWSV---SPATFSGGERQRVNLA 165
Cdd:cd03291 99 -RISFSSQFSWIMPGTIKENIIF------GVSYDEYRYKsvvkACQLEEDItKFPEKDNTVlgeGGITLSGGQRARISLA 171
|
170 180
....*....|....*....|....*..
gi 1706422447 166 RGFIAKPRLLLLDEPTSSLDPATAERV 192
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-226 |
1.03e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdaMGHELDLvlASEHQILElrrREIGFVTQFLHCLPR 108
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF---QGKEIDF--KSSKEALE---NGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVV---AQPLFALGVSRDVARQRAAELLSAMKLperlwSVSP----ATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:PRK10982 88 RSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDI-----DIDPrakvATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 182 SSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITIL 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-200 |
1.04e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 18 HEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamghELDLVLASEHQILELRRReIG 97
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV--------KIDGELLTAENVWNLRRK-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 98 FVTQFLHCLPRQATL-DVVAQPLFALGVSRDVARQRAAELLSAMKLPErLWSVSPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:PRK13642 85 MVFQNPDNQFVGATVeDDVAFGMENQGIPREEMIKRVDEALLAVNMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180
....*....|....*....|....
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLK 200
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIK 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
28-227 |
1.06e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKgIYRTYLPSAGRILYRDAMGhelDLVLASE--HQILELRrreigfvtqfLHC 105
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLK-ALAGDLTGGGAPRGARVTG---DVTLNGEplAAIDAPR----------LAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LprQATLDVVAQPLFALGV---------------------SRDVArQRAAELLSAMKLPERlwsvSPATFSGGERQRVNL 164
Cdd:PRK13547 84 L--RAVLPQAAQPAFAFSAreivllgrypharragalthrDGEIA-WQALALAGATALVGR----DVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 165 AR---------GFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK13547 157 ARvlaqlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLA 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-224 |
1.08e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.94 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLvlaSEHQILELRRrEIGFVTQFL-HCLPR 108
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD---GKPIDY---SRKGLMKLRE-SVGMVFQDPdNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP-A 187
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPmG 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 188 TAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVF 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
28-226 |
1.38e-11 |
|
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: 61.78 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASEhqiLELRRRE-IGFVtqflhcl 106
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFN---PELTGREnIYLN------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 prqATLdvvaqplfaLGVSRDVARQRA------AELLSAMKLPERlwsvspaTFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:cd03220 109 ---GRL---------LGLSRKEIDEKIdeiiefSELGDFIDLPVK-------TYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 181 TSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-224 |
1.45e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASEhqilelRRREIgFVTQFLHCLPR 108
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ------RIRMI-FQDPSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPL-FALGVSRDVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:PRK15112 104 QRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 188 TAERVIGLIEGLKAE-GTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK15112 184 MRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVL 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-214 |
1.53e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYlpsagrilyrdAMGHELDLVL-----ASEHQILELRRReIGFVTQF 102
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-----------PQGYSNDLTLfgrrrGSGETIWDIKKH-IGYVSSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHCLPRQAT--LDVVAQPLF-ALGVSRDVA-RQR--AAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:PRK10938 345 LHLDYRVSTsvRNVILSGFFdSIGIYQAVSdRQQklAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190
....*....|....*....|....*....|....*....
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEG-TAMLAIFHHPE 214
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSHHAE 463
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-226 |
1.56e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 21 NKLIPSSHNVSFTV--------RAGELTALIGPTGAGKSSVLKGI----YRTYLPSAGRILYRdamGHeldlvlaSEHQI 88
Cdd:TIGR00956 63 RKLKKFRDTKTFDIlkpmdgliKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYD---GI-------TPEEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 89 LELRRREIGFVTQ----FLHcLPRQATLDVVAQ----PLFALGVSRDVARQRAAEL-LSAMKLPERLWSVSPATF----S 155
Cdd:TIGR00956 133 KKHYRGDVVYNAEtdvhFPH-LTVGETLDFAARcktpQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrgvS 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 156 GGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAervIGLIEGLKA-----EGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATA---LEFIRALKTsanilDTTPLVAIYQCSQDAYELFDKVIVL 284
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
29-227 |
1.59e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 62.32 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSS---VLKGIYRtylPSAGRIlyrdamghELDLVLASEHQILELRRReIGFV-----T 100
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTiskILTGLLK---PQSGEI--------KIDGITISKENLKEIRKK-IGIIfqnpdN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 101 QFLhclprQATL-DVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDE 179
Cdd:PRK13632 95 QFI-----GATVeDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAIASVLALNPEIIIFDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1706422447 180 PTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELA 227
Cdd:PRK13632 169 STSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFS 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-220 |
2.46e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILYRdamGHELDLVLASEHQILELrrreIGfvtqflH 104
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRilaGLAR---PDAGEVLWQ---GEPIRRQRDEYHQDLLY----LG------H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clprQATLDVVAQPL----FALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEP 180
Cdd:PRK13538 82 ----QPGIKTELTALenlrFYQRLHGPGDDEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1706422447 181 TSSLDPATAERVIGLIEG-LKAEGTAMLA----IFHHPETTRRLA 220
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVILTthqdLPVASDKVRKLR 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-226 |
2.98e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYrdamghELDLVLASEHQilELRRREIGFVtqflhclpr 108
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY------EQDLIVARLQQ--DPPRNVEGTV--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 qatLDVVAQPLFALG--------VSRDVARQRAAELLSAM-KLPERL-----W-------------SVSPAT----FSGG 157
Cdd:PRK11147 84 ---YDFVAEGIEEQAeylkryhdISHLVETDPSEKNLNELaKLQEQLdhhnlWqlenrinevlaqlGLDPDAalssLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATaervIGLIEG-LKAEGTAMLAIFHHPETTRRLADQVVEL 226
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWLEGfLKTFQGSIIFISHDRSFIRNMATRIVDL 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-213 |
3.81e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAGRIlyrdAMGH-ELDLVLASEHQILELRRREIGFVTQF-LHcL 106
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTLLNVL-------AERV----TTGViTGGDRLVNGRPLDSSFQRSIGYVQQQdLH-L 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PrQATLDVVAQPLFALGVSRDVAR-------QRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLL-LD 178
Cdd:TIGR00956 849 P-TSTVRESLRFSAYLRQPKSVSKsekmeyvEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*
gi 1706422447 179 EPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQP 962
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-213 |
3.97e-11 |
|
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: 60.45 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlasehqilelrRREIGFVTQFLHCLPR 108
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ--------------RDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:TIGR01189 84 LKPELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-226 |
4.16e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.87 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 3 PPILQVEGYGKHFQLHEQNK------LIPSS----------HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAG 66
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSrslkelLLRRRrtrreefwalKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 67 RILYRdamGHeldlvLASehqILELRrreIGFVTQ-------FLHCLprqatldvvaqplfALGVSRDVARQRA------ 133
Cdd:COG1134 82 RVEVN---GR-----VSA---LLELG---AGFHPEltgreniYLNGR--------------LLGLSRKEIDEKFdeivef 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 134 AELLSAMKLPERlwsvspaTFSGGERQRVNLArgfIA---KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIF 210
Cdd:COG1134 134 AELGDFIDQPVK-------TYSSGMRARLAFA---VAtavDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVS 203
|
250
....*....|....*.
gi 1706422447 211 HHPETTRRLADQVVEL 226
Cdd:COG1134 204 HSMGAVRRLCDRAIWL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-223 |
6.28e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELdlvlaSEHQILElrRREIGFVTqflhcLP- 107
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLN---GKEI-----NALSTAQ--RLARGLVY-----LPe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 -RQAT---LD----------VVAQPLFALGVSRDVA---RQRAAellSAMKLPERLWSVSpaTFSGGERQRVNLARGFIA 170
Cdd:PRK15439 346 dRQSSglyLDaplawnvcalTHNRRGFWIKPARENAvleRYRRA---LNIKFNHAEQAAR--TLSGGNQQKVLIAKCLEA 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 171 KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQV 223
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-225 |
7.53e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKS-SVLKGIYRTYLPsaGRILYRDAMGHELDLVLASEHQILELRRREIGFVTQflhclP 107
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQ-----D 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLD----VVAQPLFALGV----SRDVARQRAAELLSAMKLPE---RLwSVSPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:PRK11022 98 PMTSLNpcytVGFQIMEAIKVhqggNKKTRRQRAIDLLNQVGIPDpasRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 177 LDEPTSSLDPATAERVIG-LIEGLKAEGTAMLAIFHH----PETTRRL----ADQVVE 225
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIElLLELQQKENMALVLITHDlalvAEAAHKIivmyAGQVVE 234
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
30-236 |
7.77e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGI----YRTYLPSAGRILYRDamgheLDLVLASEHQilelRRREIGFVTQFLHC 105
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDD-----IDLLRLSPRE----RRKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPrQATLDvvaqPlfalgvSRDVARQ-----------------------RAAELLS--AMKLPERLWSVSPATFSGGERQ 160
Cdd:PRK15093 97 EP-QSCLD----P------SERVGRQlmqnipgwtykgrwwqrfgwrkrRAIELLHrvGIKDHKDAMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGL-KAEGTAMLAIFHHPETTRRLAD--------QVVELAPPpa 231
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADkinvlycgQTVETAPS-- 243
|
....*
gi 1706422447 232 vEELL 236
Cdd:PRK15093 244 -KELV 247
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
29-230 |
1.92e-10 |
|
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: 58.10 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSS-VLKGIYrtylpSAGRILYRDamghelDLVLASEHQILelrrreigFVTQFlhclp 107
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTlVNEGLY-----ASGKARLIS------FLPKFSRNKLI--------FIDQL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rqatldvvaQPLFALGvsrdvarqraaelLSAMKLPERLwsvspATFSGGERQRVNLARgFIA---KPRLLLLDEPTSSL 184
Cdd:cd03238 69 ---------QFLIDVG-------------LGYLTLGQKL-----STLSGGELQRVKLAS-ELFsepPGTLFILDEPSTGL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1706422447 185 DPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVELAPPP 230
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-188 |
2.36e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.73 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELdlvlasehQILELRRReIGFVTQ--F 102
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL--------QLDSWRSR-LAVVSQtpF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 LHClprqatlDVVAQPLfALGvsRDVARQ----RAAELLSA----MKLP--------ERlwsvsPATFSGGERQRVNLAR 166
Cdd:PRK10789 400 LFS-------DTVANNI-ALG--RPDATQqeieHVARLASVhddiLRLPqgydtevgER-----GVMLSGGQKQRISIAR 464
|
170 180
....*....|....*....|..
gi 1706422447 167 GFIAKPRLLLLDEPTSSLDPAT 188
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRT 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-192 |
2.84e-10 |
|
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: 59.92 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDamgheldlvlasehqilelrrrEIGFVTQFLH 104
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------------RISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLPRQATLDVVaqplfaLGVSRDVARQRAaeLLSAMKLPERLwSVSP-----------ATFSGGERQRVNLARGFIAKPR 173
Cdd:TIGR01271 498 IMPGTIKDNII------FGLSYDEYRYTS--VIKACQLEEDI-ALFPekdktvlgeggITLSGGQRARISLARAVYKDAD 568
|
170
....*....|....*....
gi 1706422447 174 LLLLDEPTSSLDPATAERV 192
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTEKEI 587
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-224 |
3.88e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHfqlHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYlPSA--GRILYRdamGHELDL-- 80
Cdd:TIGR02633 257 ILEARNLTCW---DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFIN---GKPVDIrn 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 81 -VLASEHQIL---ELRRREiGFVTQFlhCLPRQATLDVVaQPLFALGVSRDVARQRAaeLLSAMKlPERLWSVSP----A 152
Cdd:TIGR02633 330 pAQAIRAGIAmvpEDRKRH-GIVPIL--GVGKNITLSVL-KSFCFKMRIDAAAELQI--IGSAIQ-RLKVKTASPflpiG 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 153 TFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-203 |
4.73e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.86 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDLVLASEH------QILELRRREiGF 98
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD---GHEVVTRSPQDGlangivYISEDRKRD-GL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 99 VTQflhcLPRQATLDVVAQPLFA-LGVSRDVARQRAAE----LLSAMKLPERLWSVspATFSGGERQRVNLARGFIAKPR 173
Cdd:PRK10762 342 VLG----MSVKENMSLTALRYFSrAGGSLKHADEQQAVsdfiRLFNIKTPSMEQAI--GLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190
....*....|....*....|....*....|
gi 1706422447 174 LLLLDEPTSSLDPATAERVIGLIEGLKAEG 203
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEG 445
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-185 |
7.73e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAGrilyrdamgheLDLVLASEHQI-------LELRRREIGFVT 100
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMV-------AG-----------LERITSGEIWIggrvvneLEPADRDIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 101 QFLHCLPRQATLDVVAQPLFALGVSRDVARQR---AAELLSAMKLPERlwsvSPATFSGGERQRVNLARGFIAKPRLLLL 177
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERvaeAARILELEPLLDR----KPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
....*...
gi 1706422447 178 DEPTSSLD 185
Cdd:PRK11650 159 DEPLSNLD 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-207 |
7.98e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdAMGHELdlvlasehqilelrrrEIGFVTQFLHCL-P 107
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKL----------------EVAYFDQHRAELdP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVA---QPLFALGVSRDVARQRAAELLSamklPERlwSVSPA-TFSGGERQRVNLARGFIAKPRLLLLDEPTSS 183
Cdd:PRK11147 397 EKTVMDNLAegkQEVMVNGRPRHVLGYLQDFLFH----PKR--AMTPVkALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180
....*....|....*....|....*.
gi 1706422447 184 LDPATAErvigLIEGLKAE--GTAML 207
Cdd:PRK11147 471 LDVETLE----LLEELLDSyqGTVLL 492
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
28-187 |
1.17e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.02 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY-----RDAMGHELDLVLA----SEHQILELRRRE-IG 97
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdgldvATTPSRELAKRLAilrqENHINSRLTVRElVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 98 FvTQFLHCLPR--QATLDVVAQPLFALGVSrDVARQRAAELlsamklperlwsvspatfSGGERQRVnlargFIA----- 170
Cdd:COG4604 98 F-GRFPYSKGRltAEDREIIDEAIAYLDLE-DLADRYLDEL------------------SGGQRQRA-----FIAmvlaq 152
|
170
....*....|....*..
gi 1706422447 171 KPRLLLLDEPTSSLDPA 187
Cdd:COG4604 153 DTDYVLLDEPLNNLDMK 169
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
29-214 |
1.38e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.70 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAmghelDLVLASEHQILELRRReIGFVTQFLHCLPR 108
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE-----NIPAMSRSRLYTVRKR-MSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQPLfalgvsRDVARQRAAELLSA--MKLP----ERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:PRK11831 99 MNVFDNVAYPL------REHTQLPAPLLHSTvmMKLEavglRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190
....*....|....*....|....*....|....
gi 1706422447 183 SLDPATAERVIGLIEGL-KAEGTAMLAIFHH-PE 214
Cdd:PRK11831 173 GQDPITMGVLVKLISELnSALGVTCVVVSHDvPE 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
127-211 |
1.50e-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: 57.64 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 127 DVARQ--RAAEllsAMKLPERLWSVspATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDpatAERVIGLIEGLKAEGT 204
Cdd:TIGR03719 138 DLDSQleIAMD---ALRCPPWDADV--TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG 209
|
....*..
gi 1706422447 205 AMLAIFH 211
Cdd:TIGR03719 210 TVVAVTH 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-199 |
2.17e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.18 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlYRDAmghELDLVLASEHQI--LELRRREIGFVtqfLHCL 106
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSA---KVRMAVFSQHHVdgLDLSSNPLLYM---MRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRQATLDVVAQpLFALGVSRDVARQraaellsamklperlwsvSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDP 186
Cdd:PLN03073 600 PGVPEQKLRAH-LGSFGVTGNLALQ------------------PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
170
....*....|...
gi 1706422447 187 ATAErviGLIEGL 199
Cdd:PLN03073 661 DAVE---ALIQGL 670
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-236 |
2.68e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 23 LIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQILELRRreigfvtqf 102
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM--------IDDCDVAKFGLTDLRR--------- 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 lhclprqaTLDVVAQ-PLFALGVSR----DVARQRAAELLSAMKLP--ERLWSVSP-----------ATFSGGERQRVNL 164
Cdd:PLN03232 1311 --------VLSIIPQsPVLFSGTVRfnidPFSEHNDADLWEALERAhiKDVIDRNPfgldaevseggENFSVGQRQLLSL 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 165 ARGFIAKPRLLLLDEPTSSLDPataeRVIGLIEGLKAE---GTAMLAIFHHPETT----RRL---ADQVVELAPPpavEE 234
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDV----RTDSLIQRTIREefkSCTMLVIAHRLNTIidcdKILvlsSGQVLEYDSP---QE 1455
|
..
gi 1706422447 235 LL 236
Cdd:PLN03232 1456 LL 1457
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-236 |
2.88e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 23 LIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLASEHQILELRRReIGFVTQ- 101
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL--------IDGCDISKFGLMDLRKV-LGIIPQa 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 102 ----------------------FLHCLPRQATLDVVAQPlfALGVSRDVArqRAAEllsamklperlwsvspaTFSGGER 159
Cdd:PLN03130 1322 pvlfsgtvrfnldpfnehndadLWESLERAHLKDVIRRN--SLGLDAEVS--EAGE-----------------NFSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 160 QRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLI-EGLKAegTAMLAIFHHPETT----RRL---ADQVVELAPPpa 231
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIrEEFKS--CTMLIIAHRLNTIidcdRILvldAGRVVEFDTP-- 1456
|
....*
gi 1706422447 232 vEELL 236
Cdd:PLN03130 1457 -ENLL 1460
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-187 |
3.19e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIyrTYL--PSAGRilyrdAM--GHELDlvlASEhqiLELRRReIGFVTQ-F- 102
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKML--TGLlpASEGE-----AWlfGQPVD---AGD---IATRRR-VGYMSQaFs 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 103 ------------LHclprqatldvvAQpLFalGVSRDVARQRAAELLS-------AMKLPERLwsvspatfSGGERQRVN 163
Cdd:NF033858 350 lygeltvrqnleLH-----------AR-LF--HLPAAEIAARVAEMLErfdladvADALPDSL--------PLGIRQRLS 407
|
170 180
....*....|....*....|....
gi 1706422447 164 LARGFIAKPRLLLLDEPTSSLDPA 187
Cdd:NF033858 408 LAVAVIHKPELLILDEPTSGVDPV 431
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-211 |
3.49e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVEGYGKHFqlheqnkliP---SSHNVSFTVRAGELTALIGPTGAGKSS---VLKGIYRTylpSAGRILYrdaMGHE 77
Cdd:PRK10762 3 ALLQLKGIDKAF---------PgvkALSGAALNVYPGRVMALVGENGAGKSTmmkVLTGIYTR---DAGSILY---LGKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 78 LDLVLASEHQilelrRREIGFVTQFLHCLPrQATldvVAQPLFaLG---VSR------DVARQRAAELLSAMKL---PER 145
Cdd:PRK10762 68 VTFNGPKSSQ-----EAGIGIIHQELNLIP-QLT---IAENIF-LGrefVNRfgridwKKMYAEADKLLARLNLrfsSDK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422447 146 LWSvspaTFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFH 211
Cdd:PRK10762 138 LVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-224 |
4.27e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEgygkhfQLHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGI--YRTYLPSAGRILYRDAMGHEL 78
Cdd:CHL00131 3 KNKPILEIK------NLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 79 D--------LVLASEHQIlelrrrEIGFVT--QFLHCL---PRQATLDVVAQPLFALGVSRdvarqraaELLSAMKLPER 145
Cdd:CHL00131 77 EpeerahlgIFLAFQYPI------EIPGVSnaDFLRLAynsKRKFQGLPELDPLEFLEIIN--------EKLKLVGMDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 146 LWS--VSPAtFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDpATAERVIGL-IEGLKAEGTAMLAIFHHPettrRLADQ 222
Cdd:CHL00131 143 FLSrnVNEG-FSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKIIAEgINKLMTSENSIILITHYQ----RLLDY 216
|
..
gi 1706422447 223 VV 224
Cdd:CHL00131 217 IK 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-224 |
4.77e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRtylpsagriLYRDAMGhELDLVLASEHQilELRRREIGFVTQFLHCLP 107
Cdd:PRK15056 24 RDASFTVPGGSIAALVGVNGSGKSTLFKALMG---------FVRLASG-KISILGQPTRQ--ALQKNLVAYVPQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATL--DVVAQPLFA----LGVSRDVARQRAAELLSAMKLPErLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPT 181
Cdd:PRK15056 92 SFPVLveDVVMMGRYGhmgwLRRAKKRDRQIVTAALARVDMVE-FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 182 SSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:PRK15056 171 TGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-234 |
4.79e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlYRDamGHELDLVlasEHQILelrRREIGFVTQflhclp 107
Cdd:PRK10790 358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-RLD--GRPLSSL---SHSVL---RQGVAMVQQ------ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 rqatlD--VVAQPLFA---LGvsRDVARQRAAELLSAMKLPERLWSVSPA----------TFSGGERQRVNLARGFIAKP 172
Cdd:PRK10790 423 -----DpvVLADTFLAnvtLG--RDISEEQVWQALETVQLAELARSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 173 RLLLLDEPTSSLDPATaERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVELAPPPAVEE 234
Cdd:PRK10790 496 QILILDEATANIDSGT-EQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-209 |
5.51e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKS---SVLKGIYRtylPSAGRILYRDAmghelDLVLASehqILELRRREIGFVtqflh 104
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSelaEALAGLRP---PASGSIRLDGE-----DITGLS---PRERRRLGVAYI----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clP--RQAT-------------LDVVAQPLFALG--VSRDVARQRAAELLSAMKlperlwsVSPA-------TFSGGERQ 160
Cdd:COG3845 339 --PedRLGRglvpdmsvaenliLGRYRRPPFSRGgfLDRKAIRAFAEELIEEFD-------VRTPgpdtparSLSGGNQQ 409
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
132-211 |
5.68e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 132 RAAEllsAMKLPERLWSVSpaTFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDpatAERVIGLIEGLKA-EGTaMLAIF 210
Cdd:PRK11819 147 IAMD---ALRCPPWDAKVT--KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDyPGT-VVAVT 217
|
.
gi 1706422447 211 H 211
Cdd:PRK11819 218 H 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
29-188 |
6.21e-09 |
|
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: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPSAGRIlyrdamghELDLVlaSEHQI-LELRRREIGFVTQ--FLHC 105
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEI--------QIDGV--SWNSVtLQTWRKAFGVIPQkvFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDVVAQplfalgvSRDVARQRAAE---LLSAM-KLPERLWSV---SPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:TIGR01271 1306 GTFRKNLDPYEQ-------WSDEEIWKVAEevgLKSVIeQFPDKLDFVlvdGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170
....*....|
gi 1706422447 179 EPTSSLDPAT 188
Cdd:TIGR01271 1379 EPSAHLDPVT 1388
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-209 |
8.73e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHfqlHEQNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYlP--SAGRILY----------RD 72
Cdd:PRK13549 259 ILEVRNLTAW---DPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIdgkpvkirnpQQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 73 AMGHELDLVLasehqilELRRREiGFVTQFlhCLPRQATLDVVAQplFALGVSRDvarqRAAELLSAMKLPERLwSV--- 149
Cdd:PRK13549 335 AIAQGIAMVP-------EDRKRD-GIVPVM--GVGKNITLAALDR--FTGGSRID----DAAELKTILESIQRL-KVkta 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1706422447 150 SP----ATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK13549 398 SPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-224 |
1.15e-08 |
|
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: 53.43 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 1 MNPPILQVEGYGKHFQLHEqnklipsshnVSFT-VRAGELTALIGPTGAGKSSVLKGIyrTYlpsagrILY----RDAMG 75
Cdd:cd03279 1 MKPLKLELKNFGPFREEQV----------IDFTgLDNNGLFLICGPTGAGKSTILDAI--TY------ALYgktpRYGRQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 76 HELDLVLASEHQILElrrreIGFVTQFlhclpRQATLDVVAQPlfalGVSRDVARQraaellsAMKLPE----RLWSVSP 151
Cdd:cd03279 63 ENLRSVFAPGEDTAE-----VSFTFQL-----GGKKYRVERSR----GLDYDQFTR-------IVLLPQgefdRFLARPV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 152 ATFSGGERQRVNLA-----------RGFiAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLA 220
Cdd:cd03279 122 STLSGGETFLASLSlalalsevlqnRGG-ARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIP 200
|
....
gi 1706422447 221 DQVV 224
Cdd:cd03279 201 QRLE 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-229 |
1.44e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTY-LPSAGRILYR----DAMGHELDLVLASEHQILELRRREIGF 98
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHIVFKnehtNDMTNEQDYQGDEEQNVGMKNVNEFSL 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 99 VTQFLHCLPR-------QATLD-----------------VVAQP--LFALGV-------SRDVARQ---RAAELLSAMKL 142
Cdd:PTZ00265 1261 TKEGGSGEDStvfknsgKILLDgvdicdynlkdlrnlfsIVSQEpmLFNMSIyenikfgKEDATREdvkRACKFAAIDEF 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 143 PERL-----WSVSP--ATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATA---ERVIGLIEGlKAEGTaMLAIFHH 212
Cdd:PTZ00265 1341 IESLpnkydTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKTIVDIKD-KADKT-IITIAHR 1418
|
250
....*....|....*..
gi 1706422447 213 PETTRRlADQVVELAPP 229
Cdd:PTZ00265 1419 IASIKR-SDKIVVFNNP 1434
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-213 |
1.85e-08 |
|
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: 54.37 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 22 KLIPSshnVSFTVRAGELTALIGPTGAGKSS---VLKGIY-----RTYLPSAGRILY---RDAM--GHELDLVLASEhQI 88
Cdd:TIGR00954 466 VLIES---LSFEVPSGNNLLICGPNGCGKSSlfrILGELWpvyggRLTKPAKGKLFYvpqRPYMtlGTLRDQIIYPD-SS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 89 LELRRREIG--------FVTQFLHCLPRQATLDVVAQplfalgvsrdvarqraaellsamklperlWSvspATFSGGERQ 160
Cdd:TIGR00954 542 EDMKRRGLSdkdleqilDNVQLTHILEREGGWSAVQD-----------------------------WM---DVLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 161 RVNLARGFIAKPRLLLLDEPTSSLDPATAERvigLIEGLKAEGTAMLAIFHHP 213
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGY---MYRLCREFGITLFSVSHRK 639
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
150-233 |
2.50e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 150 SPATFSGGERQRVNLARGFIAKPR--LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVELA 227
Cdd:cd03270 134 SAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI-RAADHVIDIG 212
|
....*.
gi 1706422447 228 PPPAVE 233
Cdd:cd03270 213 PGAGVH 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
127-185 |
3.77e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.77e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 127 DVARQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:PLN03073 318 YTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-219 |
5.63e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.09 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 15 FQLHEQNKLIPSSHN-----VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGrilyrDAM--GHELDLVLASEHQ 87
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpavdrLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG-----DATvaGKSILTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 88 ILE-----------LRRREIGFVTQFLHCLPRQATLDVVAQPLFALGVSrdvarqraaelLSAMKLPerlwsvspATFSG 156
Cdd:TIGR01257 2013 NMGycpqfdaiddlLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS-----------LYADRLA--------GTYSG 2073
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRL 219
Cdd:TIGR01257 2074 GNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEAL 2136
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
130-211 |
7.21e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 130 RQRAAELLSAMKLPERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDpatAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK10636 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILI 202
|
..
gi 1706422447 210 FH 211
Cdd:PRK10636 203 SH 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
28-227 |
1.22e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 28 HNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRilyrdamgheldlVLASehqilelrrREIGFVtqflhclP 107
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-------------VWAE---------RSIAYV-------P 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATL---DVVAQPLFalgvsrdVARQRAAELLSAMK---LPERLWSVSPA----------TFSGGERQRVNLARGFIAK 171
Cdd:PTZ00243 728 QQAWImnaTVRGNILF-------FDEEDAARLADAVRvsqLEADLAQLGGGleteigekgvNLSGGQKARVSLARAVYAN 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVI-GLIEGLKAEGTAMLAIfhHPETTRRLADQVVELA 227
Cdd:PTZ00243 801 RDVYLLDDPLSALDAHVGERVVeECFLGALAGKTRVLAT--HQVHVVPRADYVVALG 855
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-200 |
1.38e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.39 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 39 LTALIGPTGAGKSSVLKGI-------YRTYLPSAGRILYRDAMGHELDLVLASEHQILELRRREiGFVTQFLHCLPRQ-- 109
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIryalygkARSRSKLRSDLINVGSEEASVELEFEHGGKRYRIERRQ-GEFAEFLEAKPSErk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 110 ---------ATLDVVAQPLFALgvsRDVARQRAAELLSAMKLPERLWSV-----SPATFSGGERQRVNLARGFiakprLL 175
Cdd:COG0419 104 ealkrllglEIYEELKERLKEL---EEALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLL-----SL 175
|
170 180
....*....|....*....|....*
gi 1706422447 176 LLDepTSSLDPATAERVIGLIEGLK 200
Cdd:COG0419 176 ILD--FGSLDEERLERLLDALEELA 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-227 |
1.56e-07 |
|
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: 51.94 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY--RDaMGHELDLVLAS-----EHQILelrrreig 97
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKD-IETNLDAVRQSlgmcpQHNIL-------- 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 98 fvtqFLHclprqatLDVVAQPLFAL---GVSRDVARQRAAELLSAMKLPERLwSVSPATFSGGERQRVNLARGFIAKPRL 174
Cdd:TIGR01257 1015 ----FHH-------LTVAEHILFYAqlkGRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1706422447 175 LLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIfHHPETTRRLADQVVELA 227
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMST-HHMDEADLLGDRIAIIS 1134
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
150-228 |
3.14e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 150 SPATFSGGERQRVNLAR----GFIAKprLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVE 225
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATqigsGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI-RAADYVID 561
|
...
gi 1706422447 226 LAP 228
Cdd:TIGR00630 562 IGP 564
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
29-188 |
3.39e-07 |
|
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: 49.85 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRtYLPSAGRIlyrdamghELDLVlaSEHQI-LELRRREIGFVTQ--FLHC 105
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDI--------QIDGV--SWNSVpLQKWRKAFGVIPQkvFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 LPRQATLDvvaqplfALGVSRDVARQRAAE---LLSAM-KLPERLWSV---SPATFSGGERQRVNLARGFIAKPRLLLLD 178
Cdd:cd03289 91 GTFRKNLD-------PYGKWSDEEIWKVAEevgLKSVIeQFPGQLDFVlvdGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170
....*....|
gi 1706422447 179 EPTSSLDPAT 188
Cdd:cd03289 164 EPSAHLDPIT 173
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-228 |
5.63e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 143 PERlwsvSPATFSGGERQRVNLARGFIAKPR--LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIfHHPETTRRLA 220
Cdd:PRK00635 470 PER----ALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLV-EHDEQMISLA 544
|
....*...
gi 1706422447 221 DQVVELAP 228
Cdd:PRK00635 545 DRIIDIGP 552
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-232 |
9.52e-07 |
|
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: 49.17 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKgiyrtylpsagrilyrdAMGHELDLVLASEHQilelrRREIGFVtqflh 104
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLS-----------------ALLAEMDKVEGHVHM-----KGSVAYV----- 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clPRQATLD---VVAQPLFALGVSRDVARQ--RAAELLSAMK-LP---ERLWSVSPATFSGGERQRVNLARGFIAKPRLL 175
Cdd:TIGR00957 705 --PQQAWIQndsLRENILFGKALNEKYYQQvlEACALLPDLEiLPsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1706422447 176 LLDEPTSSLDPATA----ERVIGlIEGLKAEGTAML---AIFHHPETTR--RLAD-QVVELAPPPAV 232
Cdd:TIGR00957 783 LFDDPLSAVDAHVGkhifEHVIG-PEGVLKNKTRILvthGISYLPQVDViiVMSGgKISEMGSYQEL 848
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-215 |
1.29e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.79 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheldlvlasehqILELRRREIGfvtqfLHCLPR 108
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII------------------IDGLNIAKIG-----LHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLdVVAQPLFALGVSR---DVARQRAAE------LLSAMK-----LPERL---WSVSPATFSGGERQRVNLARGFIAK 171
Cdd:TIGR00957 1361 KITI-IPQDPVLFSGSLRmnlDPFSQYSDEevwwalELAHLKtfvsaLPDKLdheCAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEgLKAEGTAMLAIFHHPET 215
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIR-TQFEDCTVLTIAHRLNT 1482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-211 |
1.55e-06 |
|
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: 47.75 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 33 TVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHELDLVLASEHQIL--ELRRREIGFVT--QFLHCLPR 108
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYftKLLEGDVKVIVkpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 109 QATLDVVAQplfalgVSRDVARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03236 102 AVKGKVGEL------LKKKDERGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180
....*....|....*....|...
gi 1706422447 189 AERVIGLIEGLKAEGTAMLAIFH 211
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEH 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-209 |
1.83e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILY----------RDAMGHelDLVLASEHqilelrRREIGFV 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdgkpidirspRDAIRA--GIMLCPED------RKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 tqflHCLPRQATLDVVAQPLFAL-------GVSRDVARQRAAELlsAMKLPERLWSVspATFSGGERQRVNLARGFIAKP 172
Cdd:PRK11288 344 ----PVHSVADNINISARRHHLRagclinnRWEAENADRFIRSL--NIKTPSREQLI--MNLSGGNQQKAILGRWLSEDM 415
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 173 RLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV 452
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
153-228 |
1.85e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.61 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 153 TFSGGERQRVNLARgFIAKPR----LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVELAP 228
Cdd:cd03271 169 TLSGGEAQRIKLAK-ELSKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI-KCADWIIDLGP 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
151-228 |
2.46e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 151 PATF-SGGERQRVNLARGFIAK---PRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQVVEL 226
Cdd:TIGR00630 826 PATTlSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDL 904
|
..
gi 1706422447 227 AP 228
Cdd:TIGR00630 905 GP 906
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-209 |
2.64e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.86 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI-LYRDAMG--HELDLVLASEHQILElRRREIGFVTQFlhc 105
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrLNGKDISprSPLDAVKKGMAYITE-SRRDNGFFPNF--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 106 lprqatldVVAQPLF------------ALGVSRDVARQRAAELLSAmKLPERLWSVSP--ATFSGGERQRVNLARGFIAK 171
Cdd:PRK09700 357 --------SIAQNMAisrslkdggykgAMGLFHEVDEQRTAENQRE-LLALKCHSVNQniTELSGGNQQKVLISKWLCCC 427
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 172 PRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-188 |
2.66e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMgheldlvlasehqilelrrrEIGFVTQFLHCL-P 107
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV--------------------KLAYVDQSRDALdP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQATLDVVAQPLfalgvsrDVARqraaelLSAMKLPERLWsVSPATF------------SGGERQRVNLARGFIAKPRLL 175
Cdd:TIGR03719 400 NKTVWEEISGGL-------DIIK------LGKREIPSRAY-VGRFNFkgsdqqkkvgqlSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|...
gi 1706422447 176 LLDEPTSSLDPAT 188
Cdd:TIGR03719 466 LLDEPTNDLDVET 478
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-206 |
3.28e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIyrtylpsAG-RILYRDAMgHELDLVLASEHQilelrRREIGfvtqflhclP 107
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGaRKIQQGRV-EVLGGDMADARH-----RRAVC---------P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 108 RQA------------TLDVV------AQpLFalGVSRDVARQRAAELLSAMKL---PERlwsvsPA-TFSGGERQRVNLA 165
Cdd:NF033858 77 RIAympqglgknlypTLSVFenldffGR-LF--GQDAAERRRRIDELLRATGLapfADR-----PAgKLSGGMKQKLGLC 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1706422447 166 RGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAM 206
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGM 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-228 |
3.90e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 3.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 153 TFSGGERQRVNLARGFIA---KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVELAP 228
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELGP 886
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
155-185 |
5.66e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 5.66e-06
10 20 30
....*....|....*....|....*....|.
gi 1706422447 155 SGGERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-228 |
5.94e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 6 LQVEGYGKHFqlhEQNKLIpssHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRD-------AMGHEL 78
Cdd:PRK15064 320 LEVENLTKGF---DNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEnanigyyAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 79 DlvLASEHQILElrrreigFVTQFlhclpRQATLD--VVAQPLFALGVSRDVARQRAAELlsamklperlwsvspatfSG 156
Cdd:PRK15064 394 D--FENDLTLFD-------WMSQW-----RQEGDDeqAVRGTLGRLLFSQDDIKKSVKVL------------------SG 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLDpataervIGLIEGL-----KAEGTamlAIF--HHPETTRRLADQVVELAP 228
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MESIESLnmaleKYEGT---LIFvsHDREFVSSLATRIIEITP 510
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-209 |
1.10e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGYGKHFQLHEQNKLIpssHNVSFTVRAGELTALIGPTGAGKS----SVLKGIYRTYLpsAGRIL----------Y 70
Cdd:NF040905 257 VFEVKNWTVYHPLHPERKVV---DDVSLNVRRGEIVGIAGLMGAGRTelamSVFGRSYGRNI--SGTVFkdgkevdvstV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 71 RDAMGH----------ELDLVLasehqiLELRRREIGFvtqflhclprqATLDVVAQplfaLGVSRDVARQRAAE-LLSA 139
Cdd:NF040905 332 SDAIDAglayvtedrkGYGLNL------IDDIKRNITL-----------ANLGKVSR----RGVIDENEEIKVAEeYRKK 390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 140 MKLpeRLWSVSPAT--FSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:NF040905 391 MNI--KTPSVFQKVgnLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-232 |
1.18e-05 |
|
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: 45.09 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 33 TVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdamGHELDLVlASEHQILELRRReiGFVTQFLHclprQATL 112
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------EIELDTV-SYKPQYIKADYE--GTVRDLLS----SITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 113 DVVAQPLFAlgvsrdvarqraAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT---A 189
Cdd:cd03237 88 DFYTHPYFK------------TEIAKPLQI-EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1706422447 190 ERVIGLIeGLKAEGTAMLaIFHHPETTRRLADQVVELAPPPAV 232
Cdd:cd03237 155 SKVIRRF-AENNEKTAFV-VEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-211 |
1.38e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.63 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 24 IPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRDAMGHEldlvlASEHQILELRRREIGFVTQfl 103
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESE-----PSFEATRSRNRYSVAYAAQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 104 hclpRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVSPAT--------FSGGERQRVNLARGFIAKPRLL 175
Cdd:cd03290 87 ----KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerginLSGGQRQRICVARALYQNTNIV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1706422447 176 LLDEPTSSLDPATAERVI--GLIEGLKAEGTAMLAIFH 211
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTH 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-185 |
1.38e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 4 PILQVE----GYGKHFQLHE-QNKLIPSShnvsftvRAGeltaLIGPTGAGKSSVLKGIYRTYLPSAGRIlyrdAMGHEL 78
Cdd:PRK10636 311 PLLKMEkvsaGYGDRIILDSiKLNLVPGS-------RIG----LLGRNGAGKSTLIKLLAGELAPVSGEI----GLAKGI 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 79 DLVLASEHQILELRRREIGFvtQFLHCLPRQATLDVVAQPLFALGVSRDvarqraaellsamklperlwSVSPAT--FSG 156
Cdd:PRK10636 376 KLGYFAQHQLEFLRADESPL--QHLARLAPQELEQKLRDYLGGFGFQGD--------------------KVTEETrrFSG 433
|
170 180
....*....|....*....|....*....
gi 1706422447 157 GERQRVNLARGFIAKPRLLLLDEPTSSLD 185
Cdd:PRK10636 434 GEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
10-188 |
3.74e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 43.74 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 10 GYGKHFQLHE-----QNKLIPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILyrdamgheLDLVLAS 84
Cdd:cd03288 15 GLGGEIKIHDlcvryENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIV--------IDGIDIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRReigfvtqflhclprqatLDVVAQ-PL-------FALGVSRDVARQRAAELLSAMKLPERLWSVSPA---- 152
Cdd:cd03288 87 KLPLHTLRSR-----------------LSIILQdPIlfsgsirFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGldav 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1706422447 153 ------TFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPAT 188
Cdd:cd03288 150 vteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
151-228 |
6.37e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 151 PA-TFSGGERQRVNLARgFIAKPR----LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVE 225
Cdd:COG0178 823 PAtTLSGGEAQRVKLAS-ELSKRStgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVI-KTADWIID 900
|
...
gi 1706422447 226 LAP 228
Cdd:COG0178 901 LGP 903
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-209 |
6.48e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 5 ILQVEGygkhfqLHEQNKliPSSHNVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRILYRdamGHELDlvlas 84
Cdd:PRK10982 250 ILEVRN------LTSLRQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLH---GKKIN----- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 85 EHQILELRRREIGFVTQflhclPRQAT-----LDVVAQPLFA--------LGVSRDVARQRAAE-LLSAMKLPERLWSVS 150
Cdd:PRK10982 314 NHNANEAINHGFALVTE-----ERRSTgiyayLDIGFNSLISnirnyknkVGLLDNSRMKSDTQwVIDSMRVKTPGHRTQ 388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422447 151 PATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-211 |
1.25e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI----------LYRDAMGHE----LDLVLASEHQILELR-- 92
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpnerlgkLRQDQFAFEeftvLDTVIMGHTELWEVKqe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 93 RREIgfvtqflHCLP--------RQATLDVVaqplFAL--GVSrdvARQRAAELLSAMKLPERLW-----SVSPatfsgG 157
Cdd:PRK15064 99 RDRI-------YALPemseedgmKVADLEVK----FAEmdGYT---AEARAGELLLGVGIPEEQHyglmsEVAP-----G 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 158 ERQRVNLARGFIAKPRLLLLDEPTSSLDPATaervIGLIEG-LKAEGTAMLAIFH 211
Cdd:PRK15064 160 WKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDvLNERNSTMIIISH 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-224 |
1.60e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.46 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 33 TVRAGELTALIGPTGAGKSSVLK----------GIYRTYlPSAGRIL--YRdamGHELdlvlaseHQILE-LRRREIGFV 99
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKilsgelkpnlGDYDEE-PSWDEVLkrFR---GTEL-------QDYFKkLANGEIKVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 100 --TQFLHCLPRQATldvvaqplfalGVSRDV-----ARQRAAELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKP 172
Cdd:COG1245 164 hkPQYVDLIPKVFK-----------GTVRELlekvdERGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1706422447 173 RLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVV 224
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVH 283
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
16-228 |
2.82e-04 |
|
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: 40.04 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 16 QLHEQN-KLIPSSHNVSFTvrAGELTALIGPTGAGKSSVLKGIyrtylpsagrilyrdamghELDLVLASEHqileLRRR 94
Cdd:cd03227 1 KIVLGRfPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILDAI-------------------GLALGGAQSA----TRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 95 EIGFVTQFlhclprqatldvvaqplfalgvsrdVARQRAAELLSAMKLperlwsvspatfSGGERQRVNLARGFI---AK 171
Cdd:cd03227 56 SGVKAGCI-------------------------VAAVSAELIFTRLQL------------SGGEKELSALALILAlasLK 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 172 PR-LLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTrRLADQVVELAP 228
Cdd:cd03227 99 PRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHIKK 155
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-192 |
3.15e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKgiyrtylpsagrilyrdAMGHELDLVLASEHQIlelrRREIGFVTQflh 104
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLIS-----------------AMLGELSHAETSSVVI----RGSVAYVPQ--- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 cLPRQATLDVVAQPLFA-------LGVSRDV-ARQRAAELLSAMKLPErlWSVSPATFSGGERQRVNLARGFIAKPRLLL 176
Cdd:PLN03232 687 -VSWIFNATVRENILFGsdfeserYWRAIDVtALQHDLDLLPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
170
....*....|....*.
gi 1706422447 177 LDEPTSSLDPATAERV 192
Cdd:PLN03232 764 FDDPLSALDAHVAHQV 779
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
39-228 |
6.34e-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: 39.51 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 39 LTALIGPTGAGKSSVLKGI-YRTY--LP--SAGRILYRDAMGH-------ELDLVLASEHQILELRRREIgfvtqFLHCL 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALkYALTgeLPpnSKGGAHDPKLIREgevraqvKLAFENANGKKYTITRSLAI-----LENVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 -PRQATLDVvaqPLfalgvsrdvarqraaellsaMKLPERLwsvspatfSGGERQ------RVNLARGFIAKPRLLLLDE 179
Cdd:cd03240 99 fCHQGESNW---PL--------------------LDMRGRC--------SGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1706422447 180 PTSSLDPAT-AERVIGLIEGLKAEGTAMLAIFHHPETTRRLADQVVELAP 228
Cdd:cd03240 148 PTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
143-197 |
7.47e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 7.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422447 143 PERLWSVSPATFSGGERQ-------------RVNLARGFIAKPRLLLLDEPTSSLDPATAERVIGLIE 197
Cdd:pfam13558 22 SEVETYRRSGGLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLR 89
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
152-224 |
9.80e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 152 ATFSGGERQRVNLARGFI----------AKPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRLAD 221
Cdd:TIGR00618 949 ATLSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPH 1028
|
...
gi 1706422447 222 QVV 224
Cdd:TIGR00618 1029 RIL 1031
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
152-228 |
2.19e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 152 ATFSGGERQRVNLAR--G-------FIakprlllLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPETTRRlADQ 222
Cdd:COG0178 484 GTLSGGEAQRIRLATqiGsglvgvlYV-------LDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRA-ADY 555
|
....*.
gi 1706422447 223 VVELAP 228
Cdd:COG0178 556 IIDIGP 561
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
30-226 |
2.55e-03 |
|
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: 38.63 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSSVLK---GIYRtylPSAGRILyrdamgheLDLVLASEHQILELRRReigFVTQF--LH 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKlltGLYR---PESGEIL--------LDGQPVTADNREAYRQL---FSAVFsdFH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 clprqatldvvaqpLFA--LGVSRDVARQRAAELLSAMKLPERLwsvspaTFSGGERQRVNLARGfiAKPRL-------- 174
Cdd:COG4615 417 --------------LFDrlLGLDGEADPARARELLERLELDHKV------SVEDGRFSTTDLSQG--QRKRLallvalle 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1706422447 175 ----LLLDEPTSSLDPATAE---RVIgLIEgLKAEGTAMLAI------FHhpettrrLADQVVEL 226
Cdd:COG4615 475 drpiLVFDEWAADQDPEFRRvfyTEL-LPE-LKARGKTVIAIshddryFD-------LADRVLKM 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-192 |
4.90e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 37.80 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 25 PSSHNVSFTVRAGELTALIGPTGAGKSSVLKgiyrtylpsagrilyrdAMGHELDlVLASEHQILelrRREIGFVTQFLH 104
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLIS-----------------AMLGELP-PRSDASVVI---RGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 CLprQATldVVAQPLFalGVSRDVARQRAAELLSAMK-----LP--------ERlwsvsPATFSGGERQRVNLARGFIAK 171
Cdd:PLN03130 690 IF--NAT--VRDNILF--GSPFDPERYERAIDVTALQhdldlLPggdlteigER-----GVNISGGQKQRVSMARAVYSN 758
|
170 180
....*....|....*....|.
gi 1706422447 172 PRLLLLDEPTSSLDPATAERV 192
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQV 779
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-209 |
4.96e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 15 FQLHEQNKLIPSShnvsFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRilYRDAMGHELDLVLASEHQIL--ELR 92
Cdd:PRK10938 11 FRLSDTKTLQLPS----LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--RQSQFSHITRLSFEQLQKLVsdEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 93 RREigfvTQFLHclPRQATLDVVAQPLFALGVSRDVARQRAAELLSAMKLPERLWSVspatFSGGERQRVNLARGFIAKP 172
Cdd:PRK10938 85 RNN----TDMLS--PGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEP 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 173 RLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAI 209
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-213 |
5.21e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSS---VLKGiyrtylpsagrilyRDAMGH-ELDLVLASEHQILELRRREIGFVTQF-LH 104
Cdd:PLN03140 899 VTGAFRPGVLTALMGVSGAGKTTlmdVLAG--------------RKTGGYiEGDIRISGFPKKQETFARISGYCEQNdIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 105 ClPRQATLDVVAQPLFaLGVSRDVARQ-------RAAELLSAMKLPERLWSVSPAT-FSGGERQRVNLARGFIAKPRLLL 176
Cdd:PLN03140 965 S-PQVTVRESLIYSAF-LRLPKEVSKEekmmfvdEVMELVELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....*..
gi 1706422447 177 LDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHP 213
Cdd:PLN03140 1043 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1079
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-211 |
5.22e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 37.64 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 30 VSFTVRAGELTALIGPTGAGKSS---VLKGIYRtylPSAGRILyrdamgheLDLVLASEHQILELRRREIGFVTQFlHCL 106
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTlamLLTGLYQ---PQSGEIL--------LDGKPVTAEQPEDYRKLFSAVFTDF-HLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 107 PRqaTLDVVAQPlfalgvsrdVARQRAAELLSAMKLPERL----WSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTS 182
Cdd:PRK10522 410 DQ--LLGPEGKP---------ANPALVEKWLERLKMAHKLeledGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190
....*....|....*....|....*....|.
gi 1706422447 183 SLDPaTAERVI--GLIEGLKAEGTAMLAIFH 211
Cdd:PRK10522 479 DQDP-HFRREFyqVLLPLLQEMGKTIFAISH 508
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-68 |
7.00e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.18 E-value: 7.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1706422447 29 NVSFTVRAGELTALIGPTGAGKSSVLKGIYRTYLPSAGRI 68
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
171-214 |
7.67e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.98 E-value: 7.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1706422447 171 KPRLLLLDEPTSSLDPATAERVIGLIEGLKAEGTAMLAIFHHPE 214
Cdd:pfam13304 257 KGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
135-211 |
9.67e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 36.71 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422447 135 ELLSAMKLpERLWSVSPATFSGGERQRVNLARGFIAKPRLLLLDEPTSSLD---PATAERVIG-LIEGLKAegtAMLAIF 210
Cdd:PRK13409 436 EIIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKAIRrIAEEREA---TALVVD 511
|
.
gi 1706422447 211 H 211
Cdd:PRK13409 512 H 512
|
|
| |
