|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-205 |
2.15e-98 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 285.35 E-value: 2.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElKNREQV---V 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK-KDINKLrrkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-205 |
8.63e-85 |
|
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: 249.75 E-value: 8.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNREQVVGV 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-193 |
4.15e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 237.69 E-value: 4.15e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNreqvVG 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglPPEKRN----VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHD 193
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLqRELGITFIYVTHD 195
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-195 |
2.54e-76 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 233.04 E-value: 2.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVV 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN--IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLK-LRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1055940219 161 PTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLV 195
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQV 195
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-198 |
8.71e-76 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 227.62 E-value: 8.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnpAELKNRE-- 74
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI--SSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 ----QVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:COG1136 82 rlrrRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 151 MNPR-VLAyDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAE 198
Cdd:COG1136 161 NRPKlILA-DEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAA 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-205 |
3.36e-75 |
|
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: 225.48 E-value: 3.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNreqvVGV 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgvPPERRN----IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 160 EPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03259 156 EPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIA 202
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-205 |
7.62e-75 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 225.66 E-value: 7.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE-------FYLDQEPfNPAELKNRE 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQlniaghqFDFSQKP-SEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVV 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-205 |
1.84e-74 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 224.59 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNRE--QVVG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-205 |
1.86e-73 |
|
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: 219.75 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNP--AELKNREQVVGV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLApknvlkqpkevytkkakelaeslgisdlldsypfqLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVV 172
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
7.34e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 221.12 E-value: 7.34e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKnreqv 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDV 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-198 |
2.79e-72 |
|
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: 218.51 E-value: 2.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKNREQV- 76
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT--DISKLSEKELAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 -----VGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAM 151
Cdd:cd03255 79 frrrhIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAE 198
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAE 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-205 |
4.15e-71 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 219.63 E-value: 4.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpAELKNREQVVGVVF 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 162 TSALDPELRQQVEK-LIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1118 161 FGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVV 205
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-205 |
9.83e-70 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 213.12 E-value: 9.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP----------FNPAEL 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEirlkpdrdgeLVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 KNREQV---VGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIAR 147
Cdd:COG4598 88 RQLQRIrtrLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 148 ALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-205 |
3.08e-69 |
|
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: 211.04 E-value: 3.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQ--DFQLFpHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-205 |
4.08e-69 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 211.03 E-value: 4.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE-------FYLDQEPfNPAELKNRE 74
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlniagnhFDFSKTP-SDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVV 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-194 |
2.32e-68 |
|
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: 208.48 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKnreqvV 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYtKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEAR-ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDI 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-203 |
2.18e-67 |
|
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: 206.75 E-value: 2.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV---V 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQ 203
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADR 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-205 |
3.02e-67 |
|
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: 206.20 E-value: 3.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNREQVVG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-204 |
3.57e-67 |
|
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: 205.18 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQL 204
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-205 |
9.13e-66 |
|
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: 201.54 E-value: 9.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDF--QLFpHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:cd03225 81 FQNPddQFF-GPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVI 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-194 |
2.07e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 198.35 E-value: 2.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepFNPAELKNRE----- 74
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG--QDLSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLR-VTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDL 197
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-193 |
4.97e-64 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 201.46 E-value: 4.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNR 73
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLE-IAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHD 193
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-203 |
5.77e-64 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 198.44 E-value: 5.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSG-----EFYLD-QEPFNPAE--LKN 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDtARSLSQQKglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-205 |
1.88e-63 |
|
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: 204.75 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKN 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQD--FQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-194 |
1.09e-62 |
|
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: 194.34 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFG----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD-QE--PFNPAELKNR 73
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgTDltLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEM 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-205 |
1.31e-61 |
|
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: 192.33 E-value: 1.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV 76
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQ--LFPHLSIFDniTLA-PKNVLKQPKEvyTKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDR--ILAePLRIHGLPDR--EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-205 |
1.98e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.43 E-value: 1.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF--NPAELKNReqvVGV 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVarDPAEVRRR---IGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLApKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-202 |
4.01e-61 |
|
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: 190.53 E-value: 4.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVF 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLR-LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 162 TSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSD 202
Cdd:cd03300 158 LGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSD 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-198 |
2.16e-60 |
|
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: 188.80 E-value: 2.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNP------AEL 70
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 KNREqvVGVVFQDFQLFPHLSIFDNITLapknvlkqPKEVY-----TKKAKELAESLGISDLLDSYPFQLSGGQKQRVAI 145
Cdd:COG4181 88 RARH--VGFVFQSFQLLPTLTALENVML--------PLELAgrrdaRARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 146 ARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAE 198
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-205 |
1.16e-58 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 184.25 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYL---DQEPFNPAELKNR 73
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQ--LFPHLSIFDNITLAPKNVLKQPKEVYTKKAK-ELAESLGIS-DLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVlLLLVGVGLPeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-205 |
8.90e-58 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 185.69 E-value: 8.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVF 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--ICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLK-MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVI 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-203 |
1.10e-57 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 181.61 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKA-----DSGEFYLD-----QEPFNPAELK 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDgkdiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NReqvVGVVFQDFQLFPhLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLD--SYPFQLSGGQKQRVAIARAL 149
Cdd:cd03260 81 RR---VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSDQ 203
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADR 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-205 |
1.34e-57 |
|
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: 181.77 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKNREQVVGVVF 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITL---APKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFglrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVV 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-211 |
1.02e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.47 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELknREQVVg 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsaMPPPEW--RRQVA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHlSIFDNITLAPKNVLKQPKEvytKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRERKFDR---ERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-205 |
1.16e-56 |
|
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: 179.28 E-value: 1.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVvGVV 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLApKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-193 |
2.49e-56 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.84 E-value: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNreqvVGV 79
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAENRH----VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLR-MQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHD 193
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKlGITFVFVTHD 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-194 |
7.01e-56 |
|
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: 177.49 E-value: 7.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNReqvV 77
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireQDPVELRRK---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAE--SLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDI 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-204 |
7.69e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 180.66 E-value: 7.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGefYLDQEPFNPAELKNREQVVGVVF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSG--HIRFHGTDVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNI----TLAPKNvlKQP-KEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK10851 81 QHYALFRHMTVFDNIafglTVLPRR--ERPnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRV 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-205 |
4.99e-55 |
|
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: 172.97 E-value: 4.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQvVGVVF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNItlapknvlkqpkevytkkakelaeslgisdlldsypfQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVA 166
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-197 |
1.17e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 174.47 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKNRE----- 74
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQ--DVTALRGRAlrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNI---TLAPKNVLK-----QPKEVYtKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:COG3638 80 RRIGMIFQQFNLVPRLSVLTNVlagRLGRTSTWRsllglFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFA 197
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLA 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-205 |
2.37e-54 |
|
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: 172.82 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPaeLKNRE----- 74
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNR--LRGRQlpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:TIGR02673 79 RRIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVI 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-205 |
1.09e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.48 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGkkQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAELKnreqvV 77
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalPPAERP-----V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKqPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLGLRPGLK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-198 |
1.46e-53 |
|
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: 170.49 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD-QEPFNPAELKNRE---QVVGV 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNgQETPPLNSKKASKfrrEKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLAPKNVlKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYK-KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAE 198
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-211 |
4.76e-53 |
|
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: 169.40 E-value: 4.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 19 ELDLVIPdGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELK----NREQVVGVVFQDFQLFPHLSIFD 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlpPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 NITLAPKNVLKQPKEVytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVE 174
Cdd:cd03297 95 NLAFGLKRKRNREDRI---SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 175 KLIVSLKEE-GVTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:cd03297 172 PELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-204 |
7.27e-53 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 173.11 E-value: 7.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGV 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLAPKNVlKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 160 EPTSALDPELRQQ--VE--KLIVSLkeeGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK11650 160 EPLSNLDAKLRVQmrLEiqRLHRRL---KTTSLYVTHDQVEAMTLADRV 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
9.07e-53 |
|
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: 169.84 E-value: 9.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnpAELKNRE--QVVG 78
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL--ASLSRRElaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITL--AP-KNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 156 LAYDEPTSALDpeLRQQVE--KLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1120 159 LLLDEPTSHLD--LAHQLEvlELLRRLaRERGRTVVMVLHDLNLAARYADRLV 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-203 |
1.55e-51 |
|
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: 165.97 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQViKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVF 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKRKVDKKEI-ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 162 TSALDPELRqqvEKLIVSLK----EEGVTQIIVTHDLVFAENVSDQ 203
Cdd:cd03299 157 FSALDVRTK---EKLREELKkirkEFGVTVLHVTHDFEEAWALADK 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-205 |
2.49e-51 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.39 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNReqvvgVVFQD 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-----LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNITLAPKNVLKQpkevytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLGLKGQWRD-------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 164 ALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11247 163 ALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-205 |
3.48e-51 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 172.40 E-value: 3.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD---SGEFYLDQEPFNPAELKNREQ 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDF--QLFPhLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:COG1123 84 RIGMVFQDPmtQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-197 |
5.20e-51 |
|
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: 165.05 E-value: 5.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG-KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN---PAELKNREQVV 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNI---TLAPKNVLKQPKEVYTKKAKELA----ESLGISDLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRAlaalERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFA 197
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLA 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-192 |
1.13e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 167.29 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF--GKKQVI--KELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQE---PFNPAELKNR 73
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTH 192
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITH 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-202 |
4.27e-50 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 164.84 E-value: 4.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKA---DSGEFYLDQEP---FNPAEL 70
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllkLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 KN-REQVVGVVFQDFQ--LFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVA 144
Cdd:COG0444 81 RKiRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSD 202
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIAD 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-205 |
4.71e-50 |
|
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: 163.78 E-value: 4.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGK-----KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV 76
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 ---VGVVFQ--DFQLFpHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:TIGR04521 81 rkkVGLVFQfpEHQLF-EETVYKDIAFGPKN-LGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVI 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-204 |
6.21e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.97 E-value: 6.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVFQD 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:PRK11000 84 YALYPHLSVAENMSFGLK-LAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 164 ALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK11000 163 NLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKI 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-194 |
1.06e-49 |
|
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: 164.89 E-value: 1.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKkVSKTFGKKQVikELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP--------FNPAElKN 72
Cdd:COG4148 2 MLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiFLPPH-RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 ReqvVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:COG4148 78 R---IGYVFQEARLFPHLSVRGNLLYGRKRAPRAERRI---SFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSL 194
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-203 |
2.34e-49 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 161.36 E-value: 2.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL----EKAD-SGEFYLDQEP-----FNPAELK 71
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndliPGARvEGEILLDGEDiydpdVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NReqvVGVVFQDFQLFPHlSIFDNITLAPK-NVLKQPKEVytkkaKELAE-SL---GI----SDLLDSYPFQLSGGQKQR 142
Cdd:COG1117 92 RR---VGMVFQKPNPFPK-SIYDNVAYGLRlHGIKSKSEL-----DEIVEeSLrkaALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 143 VAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSDQ 203
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDY 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-205 |
4.68e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 4.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPfnPAELKNReqvVGVV 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--PRRARRR---IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQL---FPhLSIFDNITL---APKNVLKQPKEVYTKKAKELAESLGISDLLDSyPF-QLSGGQKQRVAIARALAMNP 153
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMgryGRRGLFRRPSRADREAVDEALERVGLEDLADR-PIgELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-205 |
6.70e-48 |
|
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: 154.32 E-value: 6.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 dfqlfphlsifdnitlapknvlkqpkevytkkakelaeslgisdlldsypfqLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 163 SALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVI 151
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-194 |
9.11e-48 |
|
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: 154.46 E-value: 9.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG--KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFpHLSIFDNItlapknvlkqpkevytkkakelaeslgisdlldsypfqLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03228 81 VPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:cd03228 122 EATSALDPETEALILEALRALA-KGKTVIVIAHRL 155
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-194 |
1.21e-47 |
|
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: 165.78 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG--KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELknREQV 76
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqIDPASL--RRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 vGVVFQDFQLFpHLSIFDNITLAPKNVlkqPKEvytkKAKELAESLGISDLLDSYP-----------FQLSGGQKQRVAI 145
Cdd:COG2274 552 -GVVLQDVFLF-SGTIRENITLGDPDA---TDE----EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 146 ARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL 670
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-163 |
1.38e-46 |
|
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: 150.49 E-value: 1.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHLSIFDNI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 97 TLAPkNVLKQPKEVYTKKAKELAESLGISDLLD----SYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:pfam00005 81 RLGL-LLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-193 |
1.65e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 152.64 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD---SGEFYLDQEPFN--PAELKNreq 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTalPAEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 vVGVVFQDFQLFPHLSIFDNITLA-PKNVLKQPKEvytKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG4136 78 -IGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVS-LKEEGVTQIIVTHD 193
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHD 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-205 |
2.54e-46 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 152.59 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNReqvvG 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARL----G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VV--FQDFQLFPHLSIFDNITLA----------PKNVLKQPKEVYtKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:cd03219 77 IGrtFQIPRLFPELTVLENVMVAaqartgsgllLARARREEREAR-ERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-205 |
2.85e-46 |
|
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: 151.64 E-value: 2.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQ-VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElknREQVVGVVF 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QD--FQLFPHlSIFDNITLApknvLKQPKEVYTKKAKELaESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLG----LKELDAGNEQAETVL-KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-204 |
2.97e-46 |
|
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: 155.34 E-value: 2.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 32 IVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNreqvVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKE 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTnvPPHLRH----INMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 110 VYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQI 188
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170
....*....|....*.
gi 1055940219 189 IVTHDLVFAENVSDQL 204
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRI 171
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-205 |
5.97e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 152.07 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAELKNREQV 76
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQLFPHLSIFDNI---TLAPKNVLKQPKEVYTKKAKELA----ESLGISDLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgRLGYKPTWRSLLGRFSEEDKERAlsalERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIV 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
7.33e-46 |
|
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: 150.71 E-value: 7.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVvGVV 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-AYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLAPKNvlkQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAAL---YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENV 200
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAA 197
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-194 |
7.76e-46 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.58 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD-QEPFNPAELKNREQVVG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgLDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQ--DFQlFPHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:TIGR04520 81 MVFQnpDNQ-FVGATVEDDVAFGLEN-LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDM 197
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-194 |
1.26e-45 |
|
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: 152.03 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK---------------QVIKELDLV---------IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE 57
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeEILKKTGQTvgvndvsldVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 58 FYLDQEP---FNPAELKN-REQVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPF 133
Cdd:cd03294 81 VLIDGQDiaaMSRKELRElRRKKISMVFQSFALLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 134 QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDL 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-194 |
1.32e-45 |
|
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: 150.38 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDqepFNPAELKNREqvVGVVFQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF---GKPLEKERKR--IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQL---FPhLSIFDNITL---APKNVLKQPKEVYTKKAKELAESLGISDLLDsYPF-QLSGGQKQRVAIARALAMNPRV 155
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMglyGHKGLFRRLSKADKAKVDEALERVGLSELAD-RQIgELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDL 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-205 |
4.65e-45 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 150.50 E-value: 4.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 9 KTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP-------------FNPAELKNREQ 75
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLL-DSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-197 |
1.15e-44 |
|
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: 147.18 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP--FNPAELKNREQVVGVVFQ--DFQLF 87
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPldYSRKGLLERRQRVGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 88 pHLSIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:TIGR01166 83 -AADVDQDVAFGPLNLGLSEAEV-ERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 1055940219 168 ELRQQVEKLIVSLKEEGVTQIIVTHDLVFA 197
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-202 |
1.83e-44 |
|
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: 148.65 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNReqvv 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHRIARL---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVV--FQDFQLFPHLSIFDNITLA---------------PKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQK 140
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAaharlgrgllaallrLPRARREEREA-RERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 141 QRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSD 202
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLAD 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-193 |
1.98e-44 |
|
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: 147.17 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQV-IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpaELKNRE-----Q 75
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAipylrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREI-RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD 193
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-205 |
3.30e-44 |
|
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: 145.66 E-value: 3.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 dfqlfphlsifdnitlapknVLKQpkevytkkakelaesLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:cd03214 81 --------------------ALEL---------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 163 SALDpeLRQQVE--KLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03214 126 SHLD--IAHQIEllELLRRLaRERGKTVVMVLHDLNLAARYADRVI 169
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-192 |
6.76e-44 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.17 E-value: 6.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSktF---GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELknREQ 75
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdLTLESL--RRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 vVGVVFQDFQLFpHLSIFDNITLAPKNVLKQpkEVytKKAKELAeslGISDLLDSYPF-----------QLSGGQKQRVA 144
Cdd:COG1132 416 -IGVVPQDTFLF-SGTIRENIRYGRPDATDE--EV--EEAAKAA---QAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPElrqqVEKLIV-SLKE--EGVTQIIVTH 192
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTE----TEALIQeALERlmKGRTTIVIAH 533
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-193 |
1.45e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 146.55 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK----KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN-P-AElknRe 74
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgPgAD---R- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 qvvGVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLR-LRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHD 193
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-198 |
5.83e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.13 E-value: 5.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKV--SKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVG 78
Cdd:PRK13632 7 MIKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQ--DFQlFPHLSIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK13632 87 IIFQnpDNQ-FIGATVEDDIAFGLENKKVPPKKM-KDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEEGVTQII-VTHD----------LVFAE 198
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDmdeailadkvIVFSE 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-202 |
9.90e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 9.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAElkNREQVV 77
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRD--AQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLA---PKNVLKQPKEVYtKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrepRRGGLIDWRAMR-RRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 155 VLAYDEPTSALDpelRQQVEKL---IVSLKEEGVTQIIVTHDL--VFAenVSD 202
Cdd:COG1129 161 VLILDEPTASLT---EREVERLfriIRRLKAQGVAIIYISHRLdeVFE--IAD 208
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-202 |
1.01e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.03 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--------GKKQVIKELD---LVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NP 67
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 68 AELKNREQVVGVVFQDFQ--LFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVA 144
Cdd:COG4608 88 RELRPLRRRMQMVFQDPYasLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSD 202
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISD 226
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-193 |
1.38e-42 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 142.85 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV- 76
Cdd:TIGR02982 2 ISIRNLNHYYGhgslRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 --VGVVFQDFQLFPHLSIFDNIT----LAPKNVLKQPKEvytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:TIGR02982 82 rrIGYIFQAHNLLGFLTARQNVQmaleLQPNLSYQEARE----RARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHD 193
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLaKEQGCTILMVTHD 201
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-192 |
1.43e-42 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 142.55 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKN---- 72
Cdd:NF038007 1 MLNMQNAEKCYITKtiktKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGK--EVTNLSYsqki 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 --REQVVGVVFQDFQLFPHLSIFDNITLAPK--NVlkqPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARA 148
Cdd:NF038007 79 ilRRELIGYIFQSFNLIPHLSIFDNVALPLKyrGV---AKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:NF038007 156 MVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTH 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-192 |
5.95e-42 |
|
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: 140.71 E-value: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVikELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVF 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKNVLKQpKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190
....*....|....*....|....*....|..
gi 1055940219 162 TSALDPELRQQVEKLIVSL-KEEGVTQIIVTH 192
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLhAETKMTVLMVTH 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-192 |
4.07e-41 |
|
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: 137.35 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG--KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHlSIFDNItlapknvlkqpkevytkkakelaeslgisdlldsypfqLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03246 81 LPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190
....*....|....*....|....*....|...
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-194 |
4.62e-40 |
|
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: 143.36 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFpHLSIFDNITLAPKNVlkQPKEVytkkaKELAESLGISDLLDSYP-----------FQLSGGQKQRVAIARAL 149
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLGRPDA--SDEEL-----EAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARAL 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRL 532
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-205 |
5.46e-40 |
|
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: 139.86 E-value: 5.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 19 ELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAE----LKNREQVVGVVFQDFQLFPHLSIFD 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 NITLAPKNVlkQPKEVYTKKAKeLAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVE 174
Cdd:TIGR02142 95 NLRYGMKRA--RPSERRISFER-VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|..
gi 1055940219 175 KLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLADRVV 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-202 |
8.14e-40 |
|
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: 135.64 E-value: 8.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNREQVvGV 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglPPHERARAGI-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITLA-----PKNVLKQPKEVYTK--KAKELAESLGisdlldsypFQLSGGQKQRVAIARALAMN 152
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGayarrRAKRKARLERVYELfpRLKERRKQLA---------GTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSD 202
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIAD 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-205 |
1.07e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 137.46 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK-----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF----NPAELKN 72
Cdd:PRK13634 3 ITFQKVEHRYQYKtpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQ--DFQLFPHlSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMN-FGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIV 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-208 |
3.35e-39 |
|
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: 134.52 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD----QEPfNPAELknreqvvgVVFQDFQLFPHLSI 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgkqiTEP-GPDRM--------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 93 FDNITLAPKNVLKQ-PKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQ 171
Cdd:TIGR01184 72 RENIALAVDRVLPDlSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 172 QV-EKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKVT 208
Cdd:TIGR01184 152 NLqEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-205 |
5.40e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 136.63 E-value: 5.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKK---VSK-TFGKKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAELK 71
Cdd:PRK11308 9 IDLKKhypVKRgLFKPERLVKALDGVsftLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NREQVVGVVFQDfqlfPHLSifdnitLAPK----NVLKQPKEVYTK--------KAKELAESLGI-SDLLDSYPFQLSGG 138
Cdd:PRK11308 89 LLRQKIQIVFQN----PYGS------LNPRkkvgQILEEPLLINTSlsaaerreKALAMMAKVGLrPEHYDRYPHMFSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 139 QKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVM 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-194 |
5.87e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 133.94 E-value: 5.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFgkKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVV 80
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLAPKNVLK---QPKEvytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGLNPGLKlnaAQRE----KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSL 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-193 |
6.27e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 137.66 E-value: 6.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnpAELKNREQVVGVV 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--SHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLApknvLKQ---PKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG----LKQdklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHD 193
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHD 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-202 |
6.28e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 134.27 E-value: 6.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL-----EKADSGEFYLD-QEPF--NPAELKNR 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDgQDIFkmDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVgvvFQDFQLFPHLSIFDNITLAPK-NVLKQPKEVYTKKAKELAESLG----ISDLLDSYPFQLSGGQKQRVAIARA 148
Cdd:PRK14247 84 VQMV---FQIPNPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSD 202
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISD 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-205 |
7.66e-39 |
|
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: 132.70 E-value: 7.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTlAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF--NPAELKnreQVVGV 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVlkQPQKLR---RRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDniTLAPKNVLK--QPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIAWLKgiPSKEV-KARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEEGVTqIIVTHDLVFAENVSDQLL 205
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIV-ILSTHIVEDVESLCNQVA 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-194 |
7.72e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 139.39 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAElkNREQVV 77
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirSPRD--AIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLA--PKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 156 LAYDEPTSALDPelrQQVEKLIV---SLKEEGVTQIIVTHDL 194
Cdd:COG3845 163 LILDEPTAVLTP---QEADELFEilrRLAAEGKSIIFITHKL 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-203 |
7.95e-39 |
|
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: 131.40 E-value: 7.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAelknreqvvgvvf 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 qdfqlfphlsifdnitlapknvlkQPKEvytkkakelAESLGISdlldsYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03216 68 ------------------------SPRD---------ARRAGIA-----MVYQLSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADR 151
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
19-211 |
1.63e-38 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 132.29 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 19 ELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKNREQVVGVVFQDFQLFPHLSIFDNITL 98
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 99 APKNVLKQpKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIV 178
Cdd:TIGR01277 94 GLHPGLKL-NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....
gi 1055940219 179 SL-KEEGVTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:TIGR01277 173 QLcSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-197 |
2.12e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 132.21 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQ----VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNP------AEL 70
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 knREQVVGVVFQDFQLFPHLSIFDNITLAPknVLKQPKEVYTKK-AKELAESLGISDLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:PRK10584 86 --RAKHVGFVFQSFMLIPTLNALENVELPA--LLRGESSRQSRNgAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFA 197
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLA 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-202 |
2.53e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 132.66 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL-----EKADSGEFYLD-----QEPFNPAELK 71
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFgrniySPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NReqvVGVVFQDFQLFPHLSIFDNITLAPK--NVLKQPKEV------YTKKAKELAEslgISDLLDSYPFQLSGGQKQRV 143
Cdd:PRK14267 85 RE---VGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKELdervewALKKAALWDE---VKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSD 202
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSD 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-205 |
2.98e-38 |
|
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: 138.75 E-value: 2.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFpHLSIFDNITLAPKNVLKQpkevytkkakELAESL---GISDLLDSYP-----------FQLSGGQKQRVAI 145
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLARPDATDE----------ELWAALervGLGDWLAALPdgldtwlgeggRRLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 146 ARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLkEEGVTQIIVTHDLVFAENVsDQLL 205
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERM-DRIL 540
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-204 |
3.28e-38 |
|
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: 131.19 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE-FYLDQEPFNPAELKNReqvVGVV 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEiTFDGKSYQKNIEALRR---IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLAPKNVLKQPKEVytkkaKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRI-----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
1.60e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.35 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP--FNPAELKNREQVV 77
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQ--DFQLFPHlSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFGPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD 193
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD 196
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-205 |
9.54e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 128.80 E-value: 9.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF---------GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKN 72
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQDfqlfPhlsifdNITLAPKN----VLKQPKEVYTK-----KAKELAESLGISDLL----DSYPFQLSGGQ 139
Cdd:COG4167 85 RCKHIRMIFQD----P------NTSLNPRLnigqILEEPLRLNTDltaeeREERIFATLRLVGLLpehaNFYPHMLSSGQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 140 KQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-204 |
1.21e-36 |
|
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: 127.66 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV-VGVV 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNItLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:cd03218 81 PQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEGVTQIIVTHdlvfaeNVSDQL 204
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDH------NVRETL 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-202 |
1.21e-36 |
|
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: 127.62 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQ--VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpAELKNREQVVGV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITL-AP-KNVlkqPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyARlKGL---PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDLVFAENVSD 202
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCD 200
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-194 |
1.99e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 130.99 E-value: 1.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK--KQVIKELD----------------------LVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSG 56
Cdd:COG4175 3 KIEVRNLYKIFGKrpERALKLLDqgkskdeilektgqtvgvndasFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 57 EFYLDQEPF---NPAELKN-REQVVGVVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYP 132
Cdd:COG4175 83 EVLIDGEDItklSKKELRElRRKKMSMVFQHFALLPHRTVLENVAFGLE-IQGVPKAERRERAREALELVGLAGWEDSYP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 133 FQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:COG4175 162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELqAKLKKTIVFITHDL 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-204 |
2.89e-36 |
|
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: 128.66 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 9 KTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---FYLDQEPfNPAELKnreQVVGVVFQDFQ 85
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvAGYDVVR-EPRKVR---RSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 86 LFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSAL 165
Cdd:TIGR01188 77 VDEDLTGRENLEMMGR-LYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 166 DPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRI 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-193 |
7.18e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 132.93 E-value: 7.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF--GKKQ--VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKN---- 72
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQ--DVATLDAdala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 --REQVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:PRK10535 82 qlRREHFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD 193
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-205 |
7.38e-36 |
|
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: 125.80 E-value: 7.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHlSIFDNITLAPKNVlkqPKEVYTKKAKELAESLGISDLLDSYPFQ-------LSGGQKQRVAIARALAMNP 153
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNA---TDEEVIEAAKEAGAHDFIMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDLVFAENvSDQLL 205
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKIL 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-210 |
1.10e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.97 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELknreqvvG 78
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpGAER-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQ-LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQI-IVTHDLVFAENVSDQLLKVTPN 210
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-194 |
1.49e-35 |
|
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: 125.04 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVskTFG---KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVG 78
Cdd:cd03253 1 IEFENV--TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFpHLSIFDNITLAPKNVLKQpkEVYtkkakELAESLGISDLLDSYPFQ-----------LSGGQKQRVAIAR 147
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDE--EVI-----EAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 148 ALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-205 |
1.63e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.00 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQD--FQLFPhLSI 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 93 FDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQ 172
Cdd:PRK13647 98 WDDVAFGPVNMGLDKDEV-ERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|...
gi 1055940219 173 VEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-192 |
1.92e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNRE--QVVGVVFQ--DFQLFPH 89
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 lSIFDNITLAPKNVLKQPKEVYtKKAKELAESLGIS--DLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIE-NRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180
....*....|....*....|....*.
gi 1055940219 168 ELRQQVEKLIVSLKEE-GVTQIIVTH 192
Cdd:PRK13637 178 KGRDEILNKIKELHKEyNMTIILVSH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-194 |
2.38e-35 |
|
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: 124.57 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK---QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVG 78
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPhLSIFDNITLApknvLKQPKEVYTKKAKELAESLG-ISDLLDSYP-------FQLSGGQKQRVAIARALA 150
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYG----KPDATDEEVEEAAKKANIHDfIMSLPDGYDtlvgergSQLSGGQKQRIAIARALL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRL 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-194 |
2.90e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 126.35 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK-----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---FYLDQEPFNPAELKNR 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQV---------------------VGVVFQ--DFQLFPHlSIFDNITLAPKNVLKQPKEVYtKKAKELAESLGIS-DLLD 129
Cdd:PRK13651 83 VLEklviqktrfkkikkikeirrrVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAK-KRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 130 SYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-192 |
5.32e-35 |
|
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: 122.27 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 5 KKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL--EKADSGEFYLDQEPFNPAELKNReqvVGVVFQ 82
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI---IGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQLFPHLSIFdnitlapknvlkqpkevytkkakelaESLGISDLLDSypfqLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:cd03213 90 DDILHPTLTVR--------------------------ETLMFAAKLRG----LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190
....*....|....*....|....*....|
gi 1055940219 163 SALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-194 |
1.08e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.19 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP--FNPAELKNREQVVGVVFQ--DFQLFPhL 90
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRKGLMKLRESVGMVFQdpDNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 91 SIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELR 170
Cdd:PRK13636 99 SVYQDVSFGAVN-LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180
....*....|....*....|....*
gi 1055940219 171 QQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK13636 178 SEIMKLLVEMQKElGLTIIIATHDI 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-203 |
1.80e-34 |
|
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: 128.00 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFG--KKQVIKELD---LVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFY-------LDQEPFNPA 68
Cdd:TIGR03269 279 IIKVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 69 ELKNREQVVGVVFQDFQLFPHLSIFDNITLAPKnvLKQPKEVYTKKAKELAESLGISD-----LLDSYPFQLSGGQKQRV 143
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIG--LELPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQ 203
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDR 497
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-202 |
1.99e-34 |
|
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: 122.01 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfnpaELKNR--EQVV- 77
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE-----DITGLppHRIAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 -GVVF--QDFQLFPHLSIFDNITLA------PKNVLKQPKEVYTK--KAKELAESLGisdlldsypFQLSGGQKQRVAIA 146
Cdd:COG0410 78 lGIGYvpEGRRIFPSLTVEENLLLGayarrdRAEVRADLERVYELfpRLKERRRQRA---------GTLSGGEQQMLAIG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSD 202
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIAD 204
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-204 |
1.99e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 121.71 E-value: 1.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---FYLDQEPfNPAELKNReqvVG 78
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvAGHDVVR-EPREVRRR---IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHAR-LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQL 204
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-205 |
2.28e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 121.23 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElknrEQVVGVVF 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDN-ITLAP-KNVlkqPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03269 77 EERGLYPKMKVIDQlVYLAQlKGL---KKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-194 |
2.56e-34 |
|
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: 122.12 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLE-KADSGEFYLDQEPF---NPAELKNReqv 76
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRggeDVWELRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQLF--PHLSI--------FDNITLApknvlKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:COG1119 80 IGLVSPALQLRfpRDETVldvvlsgfFDSIGLY-----REPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQII-VTHDL 194
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHV 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-205 |
5.81e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 5.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKN-------R 73
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 eqvvGvvfqdfqLFPHLSIFDNIT-LApknVLKQ-PKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAM 151
Cdd:COG4152 81 ----G-------LYPKMKVGEQLVyLA---RLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIV 200
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-202 |
6.16e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 121.69 E-value: 6.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLE-------KADSGEFYLDQEPFNPAELKNREQVvGVVFQDFQL 86
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVDGKVLYFGKDIFQIDAIKLRKEV-GMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 87 FPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLG----ISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 163 SALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSD 202
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVAD 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-194 |
6.88e-34 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 126.34 E-value: 6.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 9 KTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAdSGEFYLDQEP---FNPAELKNREQVVGVVFQD-F 84
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDldgLSRRALRPLRRRMQVVFQDpF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 85 Q-LFPHLSIFDNIT--LAPKNVLKQPKEVyTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:COG4172 373 GsLSPRMTVGQIIAegLRVHGPGLSAAER-RARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 161 PTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLqREHGLAYLFISHDL 486
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-205 |
8.83e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.99 E-value: 8.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAEL-KNReqv 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaaWSPWELaRRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 vGVVFQDFQL-FPhLSIFDNITL--APKNVLKQPKEVYTKKAKELAeslGISDLLD-SYPfQLSGGQKQRVAIARALA-- 150
Cdd:COG4559 78 -AVLPQHSSLaFP-FTVEEVVALgrAPHGSSAAQDRQIVREALALV---GLAHLAGrSYQ-TLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 151 -----MNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRIL 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-194 |
9.88e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.40 E-value: 9.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQ--VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVG 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQ--DFQLFPHLSIFDnITLAPKNVLkQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK13648 87 IVFQnpDNQFVGSIVKYD-VAFGLENHA-VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDL 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-202 |
1.16e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 121.04 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLE------KADSGEFYLDQEPF----NPAELK 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGKVTFHGKNLYapdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NReqvVGVVFQDFQLFPHlSIFDNITLAPK-NVLK-QPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:PRK14243 91 RR---IGMVFQKPNPFPK-SIYDNIAYGARiNGYKgDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSD 202
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-204 |
1.24e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNP------AELKNREqvVGVVFQDFQLFPH 89
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAELRNQK--LGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 LSIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPEL 169
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEI-NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1055940219 170 RQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK11629 181 ADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-194 |
1.25e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.98 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfNPAELKNRE----- 74
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLKNREvpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVVGVVFQDFQLFPHLSIFDNITLaPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
1.47e-33 |
|
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: 119.85 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF------GKK-QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQ--EPFNPAELK 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdgGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NRE------QVVGVVFQDFQLFPHLSIFDnITLAPKNVLKQPKEVYTKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVA 144
Cdd:COG4778 84 PREilalrrRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKVTP 209
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-205 |
1.56e-33 |
|
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: 125.63 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepfnpAELK--NREQ---VVGVVFQDFQL 86
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDG-----ADLSqwDREElgrHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 87 FPHlSIFDNI---TLAPknvlkqPKEVYtkKAKELAeslGISDLLDSYP-----------FQLSGGQKQRVAIARALAMN 152
Cdd:COG4618 418 FDG-TIAENIarfGDAD------PEKVV--AAAKLA---GVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVfAENVSDQLL 205
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLL 537
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-192 |
2.39e-33 |
|
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: 118.85 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFgKKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYL---DQEPFNPAELKnreQ 75
Cdd:cd03245 3 IEFRNVSFSY-PNQEIPALDNVsltIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtDIRQLDPADLR---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDFQLFpHLSIFDNITLAPKNVLKQpkEVYtkkakELAESLGISDLLDSYP-----------FQLSGGQKQRVA 144
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGAPLADDE--RIL-----RAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPELRqqvEKLIVSLKE--EGVTQIIVTH 192
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQllGDKTLIIITH 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
3.26e-33 |
|
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: 124.32 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHlSIFDNITLAPKNVlkqpkevytkKAKELAESL--------------GISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLARPDA----------SDAEIREALeragldefvaalpqGLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDLVFAEN 199
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL 522
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-203 |
5.81e-33 |
|
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: 117.85 E-value: 5.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD--QEPFNPAELKNRe 74
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 qvVGVVFQDFQLFPHLSIFDNIT-------LAPKNVlkqpkevyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIAR 147
Cdd:cd03266 80 --LGFVSDSTGLYDRLTARENLEyfaglygLKGDEL--------TARLEELADRLGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 148 ALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDR 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-194 |
1.99e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGK-----KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQ----EPFNPAELKN 72
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQdfqlFPHLSIFDN-----ITLAPKNvLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIA 146
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGPKN-FKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLK-EEGVTQIIVTHDL 194
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDM 206
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-202 |
2.83e-32 |
|
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: 116.34 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNreqvVGVVF 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK----IGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKNVlkqpkEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLL-----GLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSD 202
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLAD 192
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-202 |
3.76e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.60 E-value: 3.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQ--DFQLFPHlSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK13652 83 VFQnpDDQIFSP-TVEQDIAFGPIN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSD 202
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMAD 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-194 |
5.61e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.14 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVV 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVsfhVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQ--DFQlFPHLSIFDNITLAPKNVlKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:PRK13650 84 GMVFQnpDNQ-FVGATVEDDVAFGLENK-GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-194 |
5.63e-32 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 116.79 E-value: 5.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnPA----ELKNREQV 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAmsrsRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDV 204
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-205 |
5.72e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 5.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNReqvV 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladWSPAELARR---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQL-FPhLSIFDNITL--APKNVLKQPKEVYTKKAKELAeslGISDLLD-SYPfQLSGGQKQRVAIARALA--- 150
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMgrAPHGLSRAEDDALVAAALAQV---DLAHLAGrDYP-QLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 151 ---MNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-203 |
1.37e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 115.96 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 11 FGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD------QEPFNPAELKNREQVVGVVFQDF 84
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGdvllggRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 85 QLFPhLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLG----ISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSDQ 203
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDR 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
1.56e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 114.74 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV-VGV 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNItLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:COG1137 83 LPQEASIFRKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190
....*....|....*....|....*....|
gi 1055940219 160 EPTSALDP----ELRqqveKLIVSLKEEGV 185
Cdd:COG1137 162 EPFAGVDPiavaDIQ----KIIRHLKERGI 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-194 |
2.53e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 114.25 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQ--VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFpHLSIFDNITLAPKNVlkQPKEVytKKAKELAESLG-ISDLLDSYP-------FQLSGGQKQRVAIARALAM 151
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYGRPGA--TREEV--EEAARAANAHEfIMELPEGYDtvigergVKLSGGQRQRIAIARALLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRL 197
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-205 |
2.63e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 113.77 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPaeLKNREQV---VGV 79
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK--LPPHERAragIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNITL----APKNVLKQPKEVYtkkakELAESLgiSDLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTglaaLPRRSRKIPDEIY-----ELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYY 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
4.31e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 115.72 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQ-----VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSG-----EFYLDQEPF----- 65
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgDIYIGDKKNnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 66 ---NPAELKNREQV---VGVVFQ--DFQLFPHlSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGI-SDLLDSYPFQLS 136
Cdd:PRK13631 101 tnpYSKKIKNFKELrrrVSMVFQfpEYQLFKD-TIEKDIMFGPVA-LGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 137 GGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-194 |
4.37e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.03 E-value: 4.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK-----KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAElkNR 73
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklPEY--KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQL--FPHLSIFDNITLAPKN---------VLKQPKEVYTKKAKELaeSLGISDLLDSYPFQLSGGQKQr 142
Cdd:COG1101 79 AKYIGRVFQDPMMgtAPSMTIEENLALAYRRgkrrglrrgLTKKRRELFRELLATL--GLGLENRLDTKVGLLSGGQRQ- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 143 vaiARALAM----NPRVLAYDEPTSALDPELRQQVEKL---IVslKEEGVTQIIVTHDL 194
Cdd:COG1101 156 ---ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELtekIV--EENNLTTLMVTHNM 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-200 |
4.55e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 118.63 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKT----TLLRVLAGLEKADSGEFYLDQEP---FNPAELKN-REQVVGVVFQD 83
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDllgLSERELRRiRGNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQ--LFPHLSIFDNI--TLAPKNVLkqPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:COG4172 101 PMtsLNPLHTIGKQIaeVLRLHRGL--SGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLK-EEGVTQIIVTHDL--V--FAENV 200
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQrELGMALLLITHDLgvVrrFADRV 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-192 |
5.46e-31 |
|
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: 118.60 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepfnpAELK--NREQV---VGVVFQDFQL 86
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG-----ADLKqwDRETFgkhIGYLPQDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 87 FPHlSIFDNITLAPKNVlkQPKEVYtkkakELAESLGISDLLDSYP-----------FQLSGGQKQRVAIARALAMNPRV 155
Cdd:TIGR01842 404 FPG-TVAENIARFGENA--DPEKII-----EAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-192 |
6.23e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG-----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpAELKNRE-- 74
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT-STSKNKDik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 ---QVVGVVFQdfqlFPHLSIFDNITLapKNVLKQPKE--VYTKKAKELA-ESL---GIS-DLLDSYPFQLSGGQKQRVA 144
Cdd:PRK13649 82 qirKKVGLVFQ----FPESQLFEETVL--KDVAFGPQNfgVSQEEAEALArEKLalvGISeSLFEKNPFELSGGQMRRVA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 145 IARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-211 |
9.88e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 9.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQEpfnpaelk 71
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigYFDQH-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 nreqvvgvvfQDfQLFPHLSIFDNIT-LAPK-------NVLKQ----PKEVYTKkakelaeslgISDlldsypfqLSGGQ 139
Cdd:COG0488 387 ----------QE-ELDPDKTVLDELRdGAPGgteqevrGYLGRflfsGDDAFKP----------VGV--------LSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 140 KQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLivsLKE-EGvTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
6-192 |
1.16e-30 |
|
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: 112.36 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 6 KVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL---EKADSGEFYLDQEPFNPAELKNReqvVGVVFQ 82
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKC---VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQLFPHLSIFDNITLAPKNVL--KQPKEVYTKKAKELAES-LGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLprKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-203 |
1.22e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.09 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDqepfnpaelknREQVVGVVFQD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----------KGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNIT--LAP-KNVLKQPKEVYTK----------------------------KAKELAESLGISDLLDSYP 132
Cdd:COG0488 70 PPLDDDLTVLDTVLdgDAElRALEAELEELEAKlaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 133 F-QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLivsLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:COG0488 150 VsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSHDRYFLDRVATR 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-194 |
2.19e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.47 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 7 VSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKNREQVVGVVFQD 83
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlakLNRAQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 F--QLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISD-LLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:PRK10419 98 SisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDL 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
2.37e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 116.69 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFpHLSIFDNITLAPKNVlkQPKEVYtkkakELAESLGISDLLDSYP-----------FQLSGGQKQRVAIARAL 149
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLARPDA--TDEELW-----AALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSlKEEGVTQIIVTHDL 194
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-205 |
2.49e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.65 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 11 FGKKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF-YLDQE--PFNPAELKNREQVVGVVFQD- 83
Cdd:PRK15079 28 WQPPKTLKAVDGVtlrLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDllGMKDDEWRAVRSDIQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 -FQLFPHLSIFDNI-----TLAPKnvlkQPKEVYTKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK15079 108 lASLNPRMTIGEIIaeplrTYHPK----LSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-205 |
2.62e-30 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 112.22 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVF 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLA--PKNVL---KQPKEVytKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGriPHRSLwagDSPHDA--AVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 157 AYDEPTSALDpeLRQQVE--KLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR03873 160 LLDEPTNHLD--VRAQLEtlALVRELAATGVTVVAALHDLNLAASYCDHVV 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-205 |
3.37e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.75 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF---GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVG 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHlSIFDNITLAPKnvlKQPKEVYTKKAKELAESLGISDLLDSYPF-------QLSGGQKQRVAIARALAM 151
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLT---DTPDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKlivSLKEEGVTQIIVTHDLVFAENvSDQLL 205
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQIL 684
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-194 |
4.84e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG-----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNP----AELKN 72
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REQVVGVVFQdfqlFPHLSIFDNITLapKNVLKQPKE--VYTKKAKELA----ESLGIS-DLLDSYPFQLSGGQKQRVAI 145
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENTVL--KDVEFGPKNfgFSEDEAKEKAlkwlKKVGLSeDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 146 ARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNM 205
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-195 |
5.23e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 116.12 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLD-----QepFNPAELknRE 74
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDgvdirQ--IDPADL--RR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 QVvGVVFQDFQLFpHLSIFDNITLAPKNVLKQpkEVYtkkakELAESLGISDLLDSYP-----------FQLSGGQKQRV 143
Cdd:TIGR03375 540 NI-GYVPQDPRLF-YGTLRDNIALGAPYADDE--EIL-----RAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAV 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDpelRQQVEKLIVSLKE--EGVTQIIVTH-----DLV 195
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMD---NRSEERFKDRLKRwlAGKTLVLVTHrtsllDLV 666
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-194 |
5.47e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 111.65 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQ--DFQlFPHLSIFDNITLAPKNVlKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK13635 86 VFQnpDNQ-FVGATVQDDVAFGLENI-GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDL 201
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-208 |
1.50e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQL-F-------------PHLSIFDNITLAPKNVLKQPkevytkkakelAESLGISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:PRK09536 83 PQDTSLsFefdvrqvvemgrtPHRSRFDTWTETDRAAVERA-----------MERTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKVT 208
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-194 |
3.34e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.12 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKkVSKTFGKKQVikELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYL--------DQEPFNPAELKN 72
Cdd:PRK11144 1 MLELN-FKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaEKGICLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 reqvVGVVFQDFQLFPHLSIFDNITLAPKNVLKQpkevytkKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:PRK11144 78 ----IGYVFQDARLFPHYKVRGNLRYGMAKSMVA-------QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 153 PRVLAYDEPTSALD-P---ELRQQVEKLIVSLKeegvTQII-VTHDL 194
Cdd:PRK11144 147 PELLLMDEPLASLDlPrkrELLPYLERLAREIN----IPILyVSHSL 189
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-194 |
5.19e-29 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 5 KKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNR-EQVVGVVFQD 83
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1055940219 164 ALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-205 |
1.21e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL---EKADSGEFYLDQEPFNPAELKNREQV 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQ--DFQlFPHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK13640 86 VGIVFQnpDNQ-FVGATVGDDVAFGLEN-RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAeNVSDQLL 205
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVL 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-194 |
1.35e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.78 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 11 FGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQEPFNPAELKNReqVVGVVf 81
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrraggarvaYVPQRSEVPDSLPLT--VRDLV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 qDFQLFPHLSIFDNITLAPKNVLkqpkevytkkAKELaESLGISDLLDSyPFQ-LSGGQKQRVAIARALAMNPRVLAYDE 160
Cdd:NF040873 79 -AMGRWARRGLWRRLTRDDRAAV----------DDAL-ERVGLADLAGR-QLGeLSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....
gi 1055940219 161 PTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-204 |
1.54e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPaelknreqvvgvv 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLAPKNV-------------------LKQPKEVYTKKAkelAESLGISDLLDSYPFQLSGGQKQ 141
Cdd:PRK11231 69 LSSRQLARRLALLPQHHLTPEGItvrelvaygrspwlslwgrLSAEDNARVNQA---MEQTRINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 142 RVAIARALAMNPRVLAYDEPTSALDpeLRQQVE--KLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLD--INHQVElmRLMRELNTQGKTVVTVLHDLNQASRYCDHL 208
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-205 |
1.58e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 107.57 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKK---------QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELK 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NREQVVGVVFQDfqlfPHLSifdnitLAPKNVLKQ----PKEVYTK-----KAKELAESLGISDLLDS----YPFQLSGG 138
Cdd:PRK15112 84 YRSQRIRMIFQD----PSTS------LNPRQRISQildfPLRLNTDlepeqREKQIIETLRQVGLLPDhasyYPHMLAPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 139 QKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVL 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
3.14e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnPAELKNREQVVGVVF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPKnVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 162 TSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
3.34e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.40 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL-----EKADSGEF-YLDQEPFNP----AEL 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIvYNGHNIYSPrtdtVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 KNReqvVGVVFQDFQLFPhLSIFDNIT-------LAPKNVLKQPKEVYTKKAKELAEslgISDLLDSYPFQLSGGQKQRV 143
Cdd:PRK14239 85 RKE---IGMVFQQPNPFP-MSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWDE---VKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDLVFAENVSDQ 203
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-197 |
3.46e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.64 E-value: 3.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSgefyldqEPFNPAEL---------- 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK-------SAGSHIELlgrtvqregr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 ------KNREQvVGVVFQDFQLFPHLSIFDNITLAP-------KNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSG 137
Cdd:PRK09984 77 lardirKSRAN-TGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 138 GQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKE-EGVTQIIVTHDLVFA 197
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYA 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-192 |
3.66e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.13 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFG-----KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQ----EPFNPAELK 71
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NREQVVGVVFQ--DFQLFPHlSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARA 148
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQN-FGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-204 |
7.81e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.20 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQV---------IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQ---EPFNPAELK 71
Cdd:PRK10070 22 FKYIEQGLSKEQIlektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 N-REQVVGVVFQDFQLFPHLSIFDNITLApKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALA 150
Cdd:PRK10070 102 EvRRKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 151 MNPRVLAYDEPTSALDPELRQQVEKLIVSLK-EEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK10070 181 INPDILLMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-207 |
1.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.86 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK-----QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnPAELKNREQV 76
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI-PANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 ------VGVVFQ--DFQLFPHlSIFDNITLAPKNVLKQPKEVYtKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIAR 147
Cdd:PRK13645 86 krlrkeIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAY-KKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 148 ALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLvfaenvsDQLLKV 207
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNM-------DQVLRI 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-177 |
1.39e-27 |
|
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: 104.09 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHlSIFD 94
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 NITLApknvLKQpkeVYTKKAKELAESLG----ISDLLDSYPF-------QLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:cd03248 107 NIAYG----LQS---CSFECVKEAAQKAHahsfISELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170
....*....|....
gi 1055940219 164 ALDPELRQQVEKLI 177
Cdd:cd03248 180 ALDAESEQQVQQAL 193
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-205 |
2.07e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 108.65 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG--KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHlSIFDNITLApknvlkQPKEVYTKKAKELAESLGISDLLDSYPF-----------QLSGGQKQRVAIARA 148
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYG------RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARA 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDLVFAENvSDQLL 205
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIV 538
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-194 |
2.17e-27 |
|
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: 108.75 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSktFG---KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKnreQ 75
Cdd:COG5265 358 VRFENVS--FGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdVTQASLR---A 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDFQLFpHLSIFDNI-------TLApknvlkqpkEVYtkKAKELAEslgISDLLDSYP-----------FQLSG 137
Cdd:COG5265 433 AIGIVPQDTVLF-NDTIAYNIaygrpdaSEE---------EVE--AAARAAQ---IHDFIESLPdgydtrvgergLKLSG 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 138 GQKQRVAIARALAMNPRVLAYDEPTSALDpelrQQVEKLIV-SLKE--EGVTQIIVTHDL 194
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALD----SRTERAIQaALREvaRGRTTLVIAHRL 553
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-192 |
4.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK------KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepFNPAELKNR- 73
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 --EQVVGVVFQ--DFQLFPHLsIFDNITLAPKNVLKQPKEVyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARAL 149
Cdd:PRK13633 82 diRNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEI-RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTH 192
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-202 |
4.38e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 103.96 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADsGEFYLDQ--EPFNPAELKNREQV--- 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrvEFFNQNIYERRVNLnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 ---VGVVFQDFQLFPhLSIFDNITLAPKNVLKQPK-------EVYTKKAKELAEslgISDLLDSYPFQLSGGQKQRVAIA 146
Cdd:PRK14258 87 rrqVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDE---IKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLK-EEGVTQIIVTHDLVFAENVSD 202
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-205 |
5.10e-27 |
|
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: 101.24 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG--KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElKNREQVVGV 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFphlsifdnitlapknvlkqpkevytkkAKELAESLGIsdlldsypfQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03247 80 LNQRPYLF---------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGvTQIIVTHDLVFAENVsDQLL 205
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDK-TLIWITHHLTGIEHM-DKIL 167
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-194 |
8.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.53 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQ-EPFNPAELKNREQVVG 78
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQL-FPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAEsLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
1.07e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.53 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFnPAELKNREQVVGVVF 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-PARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QdfqlfphlsiFDNitLAPKNVLKQPKEVYTK----KAKELAESlgISDLL---------DSYPFQLSGGQKQRVAIARA 148
Cdd:PRK13536 121 Q----------FDN--LDLEFTVRENLLVFGRyfgmSTREIEAV--IPSLLefarleskaDARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRL 242
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-194 |
5.43e-26 |
|
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: 100.25 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFpHLSIFDN 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 ITLAPKNVlkqPKEVYTKKAKELAESLGISDLLDSYP-------FQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE 168
Cdd:cd03252 96 IALADPGM---SMERVIEAAKLAGAHDFISELPEGYDtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|....*....
gi 1055940219 169 lrqqVEKLIVSLKEE---GVTQIIVTHDL 194
Cdd:cd03252 173 ----SEHAIMRNMHDicaGRTVIIIAHRL 197
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-207 |
5.51e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.72 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKN-REQVvG 78
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlRNQV-A 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFpHLSIFDNITLAPKnvlkqpkEVYTK----KAKELAESLG-ISDL---LDSYPFQ----LSGGQKQRVAIA 146
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYART-------EQYSReqieEAARMAYAMDfINKMdngLDTVIGEngvlLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGvTQIIVTHDLVFAENvSDQLLKV 207
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEILVV 551
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-205 |
8.07e-26 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 99.75 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 20 LDLVIPDGKTLAIVGPSGGGKTT----LLRVLAGLEKADSGEFYLDQEPFNPAELKNREqvVGVVFQDFQ--LFPHLSIF 93
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRH--IATIMQNPRtaFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 DNITLAPKNVLKqpkevYTKKAKELA----ESLGISD---LLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALD 166
Cdd:TIGR02770 83 NHAIETLRSLGK-----LSKQARALIlealEAVGLPDpeeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 167 PELRQQVEKLIVSLKEE-GVTQIIVTHDL-VFAEnVSDQLL 205
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLfGTGILLITHDLgVVAR-IADEVA 197
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-208 |
1.04e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 99.81 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpfnpaELKNREQV---- 76
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT-----DLTGLDEHeiar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 --VGVVFQDFQLFPHLSIFDNITLApknvLKQPKEVYT-----------KKAKELAESLGISDLLDSYPFQLSGGQKQRV 143
Cdd:COG4674 85 lgIGRKFQKPTVFEELTVFENLELA----LKGDRGVFAslfarltaeerDRIEEVLETIGLTDKADRLAGLLSHGQKQWL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGvTQIIVTHDLVFAENVSDqllKVT 208
Cdd:COG4674 161 EIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH-SVVVVEHDMEFVRQIAR---KVT 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-204 |
1.09e-25 |
|
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: 103.37 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADS--GEFYLDQEPFNPAELKNREQV-V 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVY---TKKAKELAESLGISDLLDSYPF-QLSGGQKQRVAIARALAMNP 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-211 |
1.61e-25 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 96.36 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEfyldqepfnpaelknreqvvgvvf 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 qdfqlfphlsifdnITLAPKNVLkqpkevytkkakelaeslgisdlldSYPFQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:cd03221 57 --------------VTWGSTVKI-------------------------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 162 TSALDPElrqQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:cd03221 98 TNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-205 |
2.45e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.12 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAELKNReqvvGVVF-----QDFQLF 87
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrSPRDAIRA----GIAYvpedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 88 PHLSIFDNITLapknvlkqpkevytkkakelaeslgisdlldsyPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:cd03215 91 LDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 168 ELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-194 |
3.26e-25 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 102.51 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAELknREQVvGVVFQDFQLFPHlS 91
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiaDPAWL--RRQM-GVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 IFDNITLAPKNVlkqPKEVYTKKAKeLAESLG-ISDLLDSYPFQ-------LSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:TIGR01846 547 IRDNIALCNPGA---PFEHVIHAAK-LAGAHDfISELPQGYNTEvgekganLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190
....*....|....*....|....*....|....
gi 1055940219 164 ALDPElrqqVEKLIVSLKEE---GVTQIIVTHDL 194
Cdd:TIGR01846 623 ALDYE----SEALIMRNMREicrGRTVIIIAHRL 652
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-194 |
4.50e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHlSIFDNITLAPKNVlkQPKEVYtkKAKELAESLG-ISDLLDSYPF-------QLSGGQKQRVAIARALAMN 152
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVGRPDA--TDEEMR--AAAERAQAHDfIERKPDGYDTvvgergrQLSGGERQRLAIARALLKD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRL 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-194 |
5.05e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 97.79 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF-YLDQEPFnpaelKNREQVV---GVVF-QDFQLFP 88
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPW-----KRRKKFLrriGVVFgQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 89 HLSIFDNITLApKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE 168
Cdd:cd03267 109 DLPVIDSFYLL-AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180
....*....|....*....|....*..
gi 1055940219 169 LRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:cd03267 188 AQENIRNFLKEYnRERGTTVLLTSHYM 214
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-205 |
2.35e-24 |
|
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: 95.69 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKnreqvVGVVFQDFQL---FPhLSIFDNITLAPKNV 103
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQRHEFawdFP-ISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 104 ---LKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL 180
Cdd:TIGR03771 80 igwLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180
....*....|....*....|....*
gi 1055940219 181 KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR03771 160 AGAGTAILMTTHDLAQAMATCDRVV 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
3.24e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.94 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPfnPAELKNREQVVGVV 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD--IDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFqLFPHLSIFDNITLApKNVLKQPKEvytkKAKELAESLGISDLLDsYPFQ-LSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PRK13539 80 HRNA-MKPALTVAENLEFW-AAFLGGEEL----DIAAALEAVGLAPLAH-LPFGyLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-194 |
3.31e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.08 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF-------------------GKKQV--IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFY 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 60 -LDQEPFnpaelKNREQVV---GVVF-QDFQLFPHLSIFDNITLApKNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQ 134
Cdd:COG4586 81 vLGYVPF-----KRRKEFArriGVVFgQRSQLWWDLPAIDSFRLL-KAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 135 LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDM 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-192 |
4.07e-24 |
|
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: 93.37 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVS-KTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---------FYLDQEP-FNPAEL 70
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRigmpegedlLFLPQRPyLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 knREQVVgvvfqdfqlfphlsifdnitlapknvlkqpkevytkkakelaeslgisdlldsYPFQ--LSGGQKQRVAIARA 148
Cdd:cd03223 81 --REQLI-----------------------------------------------------YPWDdvLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLivsLKEEGVTQIIVTH 192
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQL---LKELGITVISVGH 146
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-192 |
4.50e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.11 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---------FYLDQEPFNPAE-LknREQVvgvvfqdfq 85
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiarpagarvLFLPQRPYLPLGtL--REAL--------- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 86 LFPHLSifDNITLAP-KNVLKQ---PKevytkkakeLAESLGISDLLDSypfQLSGGQKQRVAIARALAMNPRVLAYDEP 161
Cdd:COG4178 447 LYPATA--EAFSDAElREALEAvglGH---------LAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|...
gi 1055940219 162 TSALDPELRQQVEKLivsLKEE--GVTQIIVTH 192
Cdd:COG4178 513 TSALDEENEAALYQL---LREElpGTTVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-197 |
4.71e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNR-EQVVGVVF 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITL----APKNVLKQPKEVYTkkAKELAESLGIsDLLDSYPFQ-LSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK11288 86 QELHLVPEMTVAENLYLgqlpHKGGIVNRRLLNYE--AREQLEHLGV-DIDPDTPLKyLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH--DLVFA 197
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHrmEEIFA 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-203 |
1.42e-23 |
|
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: 97.57 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLE--KADSGEF-----------YLDQEPF--- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVERPSKvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 66 -----------------NPAE--LKNREQVVGVVFQ-DFQLFPHLSIFDNItLAPKNVLKQPKEVYTKKAKELAESLGIS 125
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDklRRRIRKRIAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 126 DLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEK-LIVSLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-200 |
1.43e-23 |
|
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: 97.89 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFG-KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHlSIFDNITLAPKNVLKQPKevyTKKAKELAE--------SLGISDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKENVSQDE---IWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEgvTQIIVTHDLVFAENV 200
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS 675
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-205 |
1.62e-23 |
|
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: 93.37 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF----------------------GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFY 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 60 LDQEPFNPAELknreqvvGVVFQdfqlfPHLSIFDNITLapkNVL---KQPKEVYTKKA--KELAEsLGisDLLDsYPF- 133
Cdd:cd03220 81 VRGRVSSLLGL-------GGGFN-----PELTGRENIYL---NGRllgLSRKEIDEKIDeiIEFSE-LG--DFID-LPVk 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 134 QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRAL 213
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-194 |
1.95e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.28 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 11 FGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 91 SIFDniTLAPKNVLKQPkeVYTKKAKELAESL-------GISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:PRK10253 97 TVQE--LVARGRYPHQP--LFTRWRKEDEEAVtkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190
....*....|....*....|....*....|..
gi 1055940219 164 ALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDL 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-194 |
3.48e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElKNREQVVGV- 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 -VFQDFQLFPHLSIFDNITLA-PKNvlkqpkEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK15439 90 lVPQEPLLFPNLSVKENILFGlPKR------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 158 YDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKL 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-194 |
6.97e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 6.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFG-KKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLekAD-SGEFYLDQEPFNPAEL----- 70
Cdd:PRK11022 3 LLNVDKLSVHFGdESAPFRAVDRIsysVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMAEKLEFNGQDLqrise 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 71 KNREQVVG----VVFQD--FQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQ 141
Cdd:PRK11022 81 KERRNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1055940219 142 RVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDL 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-207 |
8.07e-23 |
|
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: 95.39 E-value: 8.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTF-GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQEPfnpaELKNR 73
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArpqpgikvgYLPQEP----QLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 74 EQVVGVVFQDFQLFPH-LSIFDNITLApknvLKQPKEVYTKKAKELAESLGISDLLDSYPFQ------------------ 134
Cdd:TIGR03719 83 KTVRENVEEGVAEIKDaLDRFNEISAK----YAEPDADFDKLAAEQAELQEIIDAADAWDLDsqleiamdalrcppwdad 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 135 ---LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPElrqQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKV 207
Cdd:TIGR03719 159 vtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILEL 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-205 |
1.02e-22 |
|
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: 90.99 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQ-----VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF-------YLDQEPFnpae 69
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsvpgsiaYVSQEPW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 70 LKN---REQVV-GVVF---------------QDFQLFPHLsifDNItlapknvlkqpkevytkkakELAESlGISdllds 130
Cdd:cd03250 77 IQNgtiRENILfGKPFdeeryekvikacalePDLEILPDG---DLT--------------------EIGEK-GIN----- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 131 ypfqLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQV-EKLIVSLKEEGVTQIIVTHDLVFAENVsDQLL 205
Cdd:cd03250 128 ----LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQLQLLPHA-DQIV 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-194 |
1.15e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----------------------GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 59 YLDQEPFNPAELknreqvvGVVFQdfqlfPHLSIFDNITLapkN--VLKQPKEVYTKKAKELAESLGISDLLD----SYp 132
Cdd:COG1134 84 EVNGRVSALLEL-------GAGFH-----PELTGRENIYL---NgrLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 133 fqlSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:COG1134 148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSM 206
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-194 |
1.32e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 93.05 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELD---LVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKaDSGEFYLDQEPFNPAEL-----KNREQVVG----VVFQDF 84
Cdd:COG4170 20 VKAVDrvsLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIDLlklspRERRKIIGreiaMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 85 Q--LFPHLSIFDNITLA-PKNVLK----QPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:COG4170 99 SscLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDhkdIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDL 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-202 |
1.49e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAE---LKNREQVvGVVFQD--FQLFp 88
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQV-ATVFQDpeQQIF- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 89 HLSIFDNITLAPKNVLKQPKEVytkkAKELAESLGISDL--LDSYPFQ-LSGGQKQRVAIARALAMNPRVLAYDEPTSAL 165
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEI----TRRVDEALTLVDAqhFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 166 DPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSD 202
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISD 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-203 |
1.60e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 94.47 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADS--GEFYLDQEPFNPAELKNREQVvG 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEAL-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVF--QDFQLFPHLSIFDNITL----APKNVLKQPkEVYtKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:NF040905 80 IVIihQELALIPYLSIAENIFLgnerAKRGVIDWN-ETN-RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQ 203
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADS 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-192 |
1.85e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFG------KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEK--ADSGEFYLDQEPFNpaelknre 74
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 qvvgvvfqdfqlfPHLSIFDNItlapknvlkqPKEVYTKKAKELAESLGISD---LLDSYPfQLSGGQKQRVAIARALAM 151
Cdd:COG2401 98 -------------REASLIDAI----------GRKGDFKDAVELLNAVGLSDavlWLRRFK-ELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTH 192
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-193 |
2.05e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHlSIFDNITLAPKNVLKQPKEvyTKKAKELAEsLGISD-LLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLER-FALPDtILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 EPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHD 193
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvREQNIAVLWVTHD 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-194 |
3.06e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQV-VGV 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHLSIFDNI---TLAPKNVLKQPKEVYTK---KAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigRHLTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKL 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-192 |
4.40e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 90.13 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEK--ADSGEFYLDQEpfNPAELKNREQV---V 77
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGE--DILELSPDERAragI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLKQPKEV--YTKKAKELAESLGIS-DLLDSYPFQ-LSGGQKQRVAIARALAMNP 153
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNFLRTALNARRGEELSAreFLKLLKEKMKELGLDeDFLDRYVNEgFSGGEKKRNEILQMLLLEP 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:COG0396 160 KLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
30-194 |
5.73e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 30 LAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPF---NPAE-LKNreqvvGVVF-----QDFQLFPHLSIFDNITLA- 99
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirSPRDaIRA-----GIAYvpedrKGEGLVLDLSIRENITLAs 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 100 -----PKNVLKQPKEvyTKKAKELAESLGI--SDlldsyPFQ----LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE 168
Cdd:COG1129 356 ldrlsRGGLLDRRRE--RALAEEYIKRLRIktPS-----PEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
170 180
....*....|....*....|....*.
gi 1055940219 169 LRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:COG1129 429 AKAEIYRLIRELAAEGKAVIVISSEL 454
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-194 |
8.83e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 9 KTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTT----LLRVLAGlekadSGEFYLDQEP---FNPAELKNREQVVGVVF 81
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPlhnLNRRQLLPVRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QD--FQLFPHLSIFDNItlAPKNVLKQP---KEVYTKKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:PRK15134 369 QDpnSSLNPRLNVLQII--EEGLRVHQPtlsAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL 194
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDL 486
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
1.02e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 90.55 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTF----GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD---SGEfyldqEPFNPAELKN- 72
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGS-----ATFNGREILNl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 --------REQVVGVVFQD--FQLFPHLSIFDNITlapkNVLKQPKEVytKKAKELAESLgisDLLDS------------ 130
Cdd:PRK09473 87 pekelnklRAEQISMIFQDpmTSLNPYMRVGEQLM----EVLMLHKGM--SKAEAFEESV---RMLDAvkmpearkrmkm 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 131 YPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQII-VTHDLVFAENVSDQLL 205
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVL 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-207 |
1.03e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNREqvvG 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARM---G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VV--FQDFQLFPHLSIFDNITLAP---------KNVLKQP------KEVYTKKAKELaESLGISDLLDSYPFQLSGGQKQ 141
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLLVAQhqqlktglfSGLLKTPafrraeSEALDRAATWL-ERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 142 RVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLLKV 207
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-205 |
1.06e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.18 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQE-PFNPAELKNrEQVVGVvfQDFqLFPHLSIFDNitlapkNVLK 105
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKiSYKPQYIKP-DYDGTV--EDL-LRSITDDLGS------SYYK 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 106 QpkevytkkakELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-G 184
Cdd:PRK13409 435 S----------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErE 504
|
170 180
....*....|....*....|.
gi 1055940219 185 VTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13409 505 ATALVVDHDIYMIDYISDRLM 525
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-205 |
1.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVV 77
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQD-FQLFPHLSIFDNITLAPKNvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK13642 84 GMVFQNpDNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENvSDQLL 205
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRIL 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-201 |
1.69e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.84 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQE---PFNPAELKNREQVVGVVFQD--FQLFPHLSIFDNIT--LA 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMepLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 100 PKNVLkqPKEVYTKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIV 178
Cdd:PRK10261 430 VHGLL--PGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180
....*....|....*....|....
gi 1055940219 179 SLKEE-GVTQIIVTHDLVFAENVS 201
Cdd:PRK10261 508 DLQRDfGIAYLFISHDMAVVERIS 531
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-205 |
3.09e-21 |
|
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: 87.85 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 24 IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE--FYLDQEPFNPAELKNREQvvGVVfQDFqLFphlSIFDNITLAPk 101
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDieIELDTVSYKPQYIKADYE--GTV-RDL-LS---SITKDFYTHP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 102 nvlkqpkevYTKKakELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLK 181
Cdd:cd03237 94 ---------YFKT--EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*
gi 1055940219 182 EEG-VTQIIVTHDLVFAENVSDQLL 205
Cdd:cd03237 163 ENNeKTAFVVEHDIIMIDYLADRLI 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-202 |
3.54e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.76 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADS--GEFYLDQEPFNPAELKNREQV-V 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLA----PKNVLKQPKevYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGneitPGGIMDYDA--MYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL--VFAenVSD 202
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLneVKA--ISD 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-202 |
3.77e-21 |
|
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: 87.81 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 22 LVIP-DGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFylDQEP--------FNPAELKN-----REQVVGVVFQdfqlf 87
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeildeFRGSELQNyftklLEGDVKVIVK----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 88 PHlsifdNITLAPKNVLKQPKEVYTKKAK-----ELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:cd03236 93 PQ-----YVDLIPKAVKGKVGELLKKKDErgkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 163 SALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSD 202
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSD 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
4.37e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELKnreQV 76
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadYSEAALR---QA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 VGVVFQDFQLFPHlSIFDNITLApknvlkQPkevyTKKAKELAESL---GISDLLDSYP----------FQLSGGQKQRV 143
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA------AP----NASDEALIEVLqqvGLEKLLEDDKglnawlgeggRQLSGGEQRRL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDLV 195
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT 535
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-205 |
5.23e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 5.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKadsgefYLDQEPFNPAELKN------REQV--VGvvfQDFQ 85
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP------YQGSLKINGIELREldpeswRKHLswVG---QNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 86 LFpHLSIFDNITLAPKNVLKQpkevytkKAKELAESLGISDLLDSYPF-----------QLSGGQKQRVAIARALAMNPR 154
Cdd:PRK11174 434 LP-HGTLRDNVLLGNPDASDE-------QLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKlivSLKE--EGVTQIIVTHDLVFAENVsDQLL 205
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQ---ALNAasRRQTTLMVTHQLEDLAQW-DQIW 554
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-192 |
9.64e-21 |
|
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: 85.49 E-value: 9.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDfQLFPHLS 91
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP-GLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 IFDNITLApkNVLKQPKEVYTKKAKELAESLGISDLldsyPF-QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELR 170
Cdd:TIGR01189 90 ALENLHFW--AAIHGGAQRTIEDALAAVGLTGFEDL----PAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|..
gi 1055940219 171 QQVEKLIVSLKEEGVTQIIVTH 192
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-205 |
1.65e-20 |
|
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: 88.69 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQE-PFNPAELKN--REQVvgvvfQDFqlfphlsIFDNITlapknv 103
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKiSYKPQYISPdyDGTV-----EEF-------LRSANT------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 104 lkqpKEVYTKKAK-ELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKE 182
Cdd:COG1245 428 ----DDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170 180
....*....|....*....|....
gi 1055940219 183 E-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:COG1245 504 NrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-192 |
2.51e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.18 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD---SGEFYLDQEPFNPAELKnreQVVGVVFQDFQLFP 88
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMR---AISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 89 HLSIFDNITLAPKnvLKQPKEVYTKK----AKELAESLGISDLLDS---YPFQ---LSGGQKQRVAIARALAMNPRVLAY 158
Cdd:TIGR00955 113 TLTVREHLMFQAH--LRMPRRVTKKEkrerVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190
....*....|....*....|....*....|....
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-204 |
2.69e-20 |
|
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: 88.30 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 22 LVIP-DGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFylDQEPfnpaelkNREQVVGvVFQDFQLFPHLS-IFDN---- 95
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP-------SWDEVLK-RFRGTELQDYFKkLANGeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 ------ITLAPKNVLKQPKEVYTK-----KAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSA 164
Cdd:COG1245 163 ahkpqyVDLIPKVFKGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 165 LDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:COG1245 243 LDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-194 |
2.98e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 2.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 26 DGKTLAIVGPSGGGKTTLLRVLAGLEKAdSGEFYLDQEP---FNPAELKNR-----EQVVGV----VFQDFQLfpHLSif 93
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPlsdWSAAELARHraylsQQQSPPfampVFQYLAL--HQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 dnitlAPKNVLKQPKEVYtkkakELAESLGISDLLDSYPFQLSGGQKQRVAIARAL-----AMNP--RVLAYDEPTSALD 166
Cdd:COG4138 96 -----AGASSEAVEQLLA-----QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
170 180 190
....*....|....*....|....*....|
gi 1055940219 167 peLRQQV--EKLIVSLKEEGVTQIIVTHDL 194
Cdd:COG4138 166 --VAQQAalDRLLRELCQQGITVVMSSHDL 193
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
3.22e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYldqepfNPAELKnreqvVGVV 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPH--LSIFDNITLAPKnvlkqpkevyTKKAKELA--ESLGISDLLDsYPFQ-LSGGQKQRVAIARALAMNPRV 155
Cdd:PRK09544 73 PQKLYLDTTlpLTVNRFLRLRPG----------TKKEDILPalKRVQAGHLID-APMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
5.19e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 87.37 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF-YLDQE-PFN-PAElkNREQVV 77
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEvTFNgPKS--SQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKNVLK----QPKEVYTKKAKELAEsLGISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIFLGREFVNRfgriDWKKMYAEADKLLAR-LNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-207 |
5.91e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN--PAELKNREqVVG 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMRE-AVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLgiSDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVthdlvfaENVSDQLLKV 207
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV-------EQNANQALKL 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-205 |
1.02e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKT-TLLRVLAGLEKA----DSGEFYLDQEPFNPAELKNREQV---------VGVV 80
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQVIELSEQSAAqmrhvrgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQD--FQLFPHLSIFDNITLAPKNVLKQPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEE---GVtqIIVTHDLVFAENVSDQLL 205
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEmsmGV--IFITHDMGVVAEIADRVL 240
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-194 |
5.13e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 83.31 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKaDSGEFYLDQEPFNPAEL-----KNREQVVG----VVFQ 82
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLlrlspRERRKLVGhnvsMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQ--LFPHLSIFDNITLA-PKNVLK----QPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVAIARALAMN 152
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNiPGWTYKgrwwQRFGWRKRRAIELLHRVGIKDhkdAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQI-IVTHDL 194
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIlLISHDL 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-193 |
6.77e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.25 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQV-IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLsifdnitLAPKNVLKQPKEVYTKKAK-ELAESLGISD--LLDsypFQLSGGQKQRVAIARALAMNPRVLA 157
Cdd:PRK10522 403 FTDFHLFDQL-------LGPEGKPANPALVEKWLERlKMAHKLELEDgrISN---LKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 158 YDEPTSALDPELRQQV-EKLIVSLKEEGVTQIIVTHD 193
Cdd:PRK10522 473 LDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHD 509
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-192 |
7.88e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 8 SKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADS--GEFYLDQEPFNPAELKNreqvVGVVFQDFQ 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKR----TGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 86 LFPHLSIFDniTLAPKNVLKQPKEVYTKKAKELAESLgISDLL----------DSYPFQLSGGQKQRVAIARALAMNPRV 155
Cdd:PLN03211 151 LYPHLTVRE--TLVFCSLLRLPKSLTKQEKILVAESV-ISELGltkcentiigNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-194 |
1.12e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 83.61 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGK-KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDfqlfPHL---SIFDNITLAPKNVLKQPKEVY-TKKAKELAESL--GISDLLDSYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK10790 421 QQD----PVVladTFLANVTLGRDISEEQVWQALeTVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEgVTQIIVTHDL 194
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRL 535
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-192 |
1.91e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.49 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLE--KADSGEFYLDQEPFNPAELKNREQV-VG 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDfqlfphlsifdnitlapknvlkqPKEVytkkakelaESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:cd03217 81 LAFQY-----------------------PPEI---------PGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....
gi 1055940219 159 DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-194 |
2.18e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.77 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKK---QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYL-DQEPFNPAELKNREQVV 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHlSIFDNI-----------------------------------------------TLAPKNVLKQPKEV 110
Cdd:PTZ00265 463 GVVSQDPLLFSN-SIKNNIkyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 111 YTKKAKEL---AESLGISDLLDSYP-----------FQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKL 176
Cdd:PTZ00265 542 QTIKDSEVvdvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*....
gi 1055940219 177 IVSLK-EEGVTQIIVTHDL 194
Cdd:PTZ00265 622 INNLKgNENRITIIIAHRL 640
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-204 |
5.61e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDfQLFPHLS 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP-GIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 IFDNIT-LAPKNVLKQPKEVytkkakeLAEsLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELR 170
Cdd:cd03231 90 VLENLRfWHADHSDEQVEEA-------LAR-VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 171 QQVEKLIVSLKEEGVTQIIVTH-DLVFAENVSDQL 204
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-194 |
6.60e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 22 LVIP-DGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFylDQEPfnpaelkNREQVV----GVVFQDFqlFPHLSifDN- 95
Cdd:PRK13409 93 LPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP-------SWDEVLkrfrGTELQNY--FKKLY--NGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 ---------ITLAPKNV-------LKQPKEvyTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PRK13409 160 ikvvhkpqyVDLIPKVFkgkvrelLKKVDE--RGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKeEGVTQIIVTHDL 194
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELA-EGKYVLVVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-200 |
7.27e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 80.93 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFG-KKQVIKELDL-VIPDGKtLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQEPfnpaelkn 72
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDISLsFFPGAK-IGVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgikvgYLPQEP-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 reqvvgvvfqdfQLFPHLSIFDNITLA---PKNVLKQPKEVYTKKAK------ELAESLG-ISDLLDSY----------- 131
Cdd:PRK11819 80 ------------QLDPEKTVRENVEEGvaeVKAALDRFNEIYAAYAEpdadfdALAAEQGeLQEIIDAAdawdldsqlei 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 132 --------PF-----QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPElrqQVEKLIVSLKEEGVTQIIVTHDLVFAE 198
Cdd:PRK11819 148 amdalrcpPWdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLD 224
|
..
gi 1055940219 199 NV 200
Cdd:PRK11819 225 NV 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-205 |
1.16e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQ---VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVL------------------------------- 47
Cdd:PTZ00265 1166 IEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 48 ----AGLEKAD-------------------SGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFpHLSIFDNITLAPKNVL 104
Cdd:PTZ00265 1246 eeqnVGMKNVNefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 105 KQPkevyTKKAKELAeslGISDLLDSYPFQ-----------LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQV 173
Cdd:PTZ00265 1325 RED----VKRACKFA---AIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270
....*....|....*....|....*....|..
gi 1055940219 174 EKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PTZ00265 1398 EKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-205 |
1.19e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 7 VSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF-YL--DQEPFNPAELKNREQVV------ 77
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRmrDGQLRDLYALSEAERRRllrtew 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQ--LFPHLSifdnitlAPKNVLKQPKEV----YTK---KAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIAR 147
Cdd:PRK11701 92 GFVHQHPRdgLRMQVS-------AGGNIGERLMAVgarhYGDiraTAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 148 ALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLL 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-194 |
1.58e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 24 IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNreqVVGVVFQDFQL---FPHLsiFDNITLAP 100
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKN---LVAYVPQSEEVdwsFPVL--VEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 101 K----NVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKL 176
Cdd:PRK15056 105 RyghmGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170
....*....|....*...
gi 1055940219 177 IVSLKEEGVTQIIVTHDL 194
Cdd:PRK15056 185 LRELRDEGKTMLVSTHNL 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-201 |
1.80e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKT-TLLRVLAGLEKAD----SGEFYLDQEPFNPAELKNREQVVG----VVFQDf 84
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 85 qlfPHLSifdnitLAP-KNVLKQPKEV---YTKKAKELAESLGISDL-----------LDSYPFQLSGGQKQRVAIARAL 149
Cdd:PRK15134 101 ---PMVS------LNPlHTLEKQLYEVlslHRGMRREAARGEILNCLdrvgirqaakrLTDYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE-GVTQIIVTHDL----VFAENVS 201
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLsivrKLADRVA 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-193 |
2.05e-17 |
|
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: 79.84 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQ-----VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAelkNRE-- 74
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD---NREay 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 75 -QVVGVVFQDFQLFPHLsifdnitlapknvLKQPKEVYTKKAKELAESLGISDLLDsypFQ--------LSGGQKQRVAI 145
Cdd:COG4615 405 rQLFSAVFSDFHLFDRL-------------LGLDGEADPARARELLERLELDHKVS---VEdgrfsttdLSQGQRKRLAL 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 146 ARALAMNPRVLAYDEPTSALDPELRqQV--EKLIVSLKEEGVTQIIVTHD 193
Cdd:COG4615 469 LVALLEDRPILVFDEWAADQDPEFR-RVfyTELLPELKARGKTVIAISHD 517
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-194 |
5.80e-17 |
|
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: 75.99 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTF--GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGV 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 VFQDFQLFPHlSIFDNitLAPKNvLKQPKEVY--TKKA--KELAESL--GISDLLDSYPFQLSGGQKQRVAIARALAMNP 153
Cdd:cd03244 83 IPQDPVLFSG-TIRSN--LDPFG-EYSDEELWqaLERVglKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIvslKEE--GVTQIIVTHDL 194
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTI---REAfkDCTVLTIAHRL 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-194 |
7.67e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 76.28 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKT----TLLRVL-AGLEKAdSGEFYLDQEPFNPAELKNREqvVGVVFQDfqlfPHlS 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPCALRGRK--IATIMQN----PR-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 IFDNI----TLAPKNVLKQPKEVYTKKAKELAESLGISD---LLDSYPFQLSGGQKQRVAIARAL-AMNPRVLAyDEPTS 163
Cdd:PRK10418 91 AFNPLhtmhTHARETCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALlCEAPFIIA-DEPTT 169
|
170 180 190
....*....|....*....|....*....|..
gi 1055940219 164 ALDPELRQQVEKLIVSL-KEEGVTQIIVTHDL 194
Cdd:PRK10418 170 DLDVVAQARILDLLESIvQKRALGMLLVTHDM 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-205 |
8.79e-17 |
|
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: 78.05 E-value: 8.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQepfnpaelkN 72
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigetvklaYVDQ---------S 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REqvvgvvfqdfqlfphlsifdniTLAPKnvlkqpKEVYtkkaKELAESLGISDL----------LDSYPF--------- 133
Cdd:TIGR03719 394 RD----------------------ALDPN------KTVW----EEISGGLDIIKLgkreipsrayVGRFNFkgsdqqkkv 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 134 -QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKlivSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR03719 442 gQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE---ALLNFAGCAVVISHDRWFLDRIATHIL 511
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-211 |
9.89e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.62 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFyldqepfnpaelKNREQV-VGVV 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENAnIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDfqlfpHLSIFDN-ITLAP-KNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAY 158
Cdd:PRK15064 388 AQD-----HAYDFENdLTLFDwMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 159 DEPTSALDPElrqQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLLKVTPNQ 211
Cdd:PRK15064 463 DEPTNHMDME---SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-205 |
1.38e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAElknREQVVGVVFQDFQLFPHLSIFDN 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 ITLApknvlkqpKEVYTKKAKELAES----LGISDLLDSYPFQLSGGQKQRVAIARaLAMNPRVL-AYDEPTSALDPELR 170
Cdd:PRK13543 103 LHFL--------CGLHGRRAKQMPGSalaiVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 171 QQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRML 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-194 |
1.49e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKAdSGEFYLDQEP---FNPAELKNR-----EQVVGV----VFQDFQLFphlsifd 94
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPleaWSAAELARHraylsQQQTPPfampVFQYLTLH------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 nitLAPKNVLKQPKEVYTkkakELAESLGISDLLDSYPFQLSGGQKQRVAIARAL-----AMNP--RVLAYDEPTSALDp 167
Cdd:PRK03695 94 ---QPDKTRTEAVASALN----EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLD- 165
|
170 180
....*....|....*....|....*....
gi 1055940219 168 eLRQQV--EKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK03695 166 -VAQQAalDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-205 |
3.24e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.82 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQD 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNITLA--P-KNVLKQPKEVYTKKAKELAESLGI----SDLLDSypfqLSGGQKQRVAIARALAMNPRVL 156
Cdd:PRK10575 94 LPAAEGMTVRELVAIGryPwHGALGRFGAADREKVEEAISLVGLkplaHRLVDS----LSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLV 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-196 |
6.48e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.13 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFY-----LDQEPFNPAELKNREQVVGVVFQDFQLfpHLS 91
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYSVAYAAQKPWLL--NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 IFDNITL-APKNvlkqpKEVYtkkaKELAESLGISDLLDSYPF-----------QLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:cd03290 95 VEENITFgSPFN-----KQRY----KAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 160 EPTSALDPELRQQV--EKLIVSLKEEGVTQIIVTHDLVF 196
Cdd:cd03290 166 DPFSALDIHLSDHLmqEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-205 |
6.73e-16 |
|
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: 75.25 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLV---IPDGKTLAIVGPSGGGKTTLLRVLAGL-EKADSGEFYLDQEPFNPAE-LKNREQVVGVVFQDFQ---LFP 88
Cdd:TIGR02633 273 RKRVDDVsfsLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 89 HLSIFDNITLApknVLKQpkevYTKK-----AKELA---ESLGISDLLDSYPF----QLSGGQKQRVAIARALAMNPRVL 156
Cdd:TIGR02633 353 ILGVGKNITLS---VLKS----FCFKmridaAAELQiigSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 157 AYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL 474
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
34-192 |
1.61e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 34 GPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVvGVVFQDFQLFPHLSIFDNITLAPKnvLKQ-PKEVYT 112
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRV-GYMSQAFSLYGELTVRQNLELHAR--LFHlPAAEIA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 113 KKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL-KEEGVTQIIVT 191
Cdd:NF033858 376 ARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFIST 455
|
.
gi 1055940219 192 H 192
Cdd:NF033858 456 H 456
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-208 |
5.49e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 5.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 19 ELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpaelKNREQvvgvvFQDFQLF--------PHL 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDE-----YHQDLLYlghqpgikTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 91 SIFDNITLApknvLKQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARaLAMNPRVL-AYDEPTSALDPEL 169
Cdd:PRK13538 90 TALENLRFY----QRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALAR-LWLTRAPLwILDEPFTAIDKQG 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1055940219 170 RQQVEKLIVSLKEEGVTQIIVTHDLVFAenVSDQLLKVT 208
Cdd:PRK13538 165 VARLEALLAQHAEQGGMVILTTHQDLPV--ASDKVRKLR 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
8.18e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQepfnpaelkN 72
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigetvklaYVDQ---------S 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 73 REqvvgvvfqdfQLFPHLSIF-------DNITLAPKNVlkqPKEVYT-----------KKAKelaeslgisdlldsypfQ 134
Cdd:PRK11819 396 RD----------ALDPNKTVWeeisgglDIIKVGNREI---PSRAYVgrfnfkggdqqKKVG-----------------V 445
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 135 LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE-LR 170
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVEtLR 482
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-202 |
1.09e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEP---FNPAELknREQVVGVVFQDFQ---LFPH 89
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDitgLSPRER--RRLGVAYIPEDRLgrgLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 LSIFDNITL--------APKNVLKQpkevytKKAKELAESL---------GISDLLDSypfqLSGGQKQRVAIARALAMN 152
Cdd:COG3845 351 MSVAENLILgryrrppfSRGGFLDR------KAIRAFAEELieefdvrtpGPDTPARS----LSGGNQQKVILARELSRD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL--VFAenVSD 202
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLdeILA--LSD 470
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-192 |
6.39e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNR-EQVVGVVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQLFPHLSIFDNITLA--PKnvlkqpKEVYTKKAKELAESLGISDLLD------SYPFQLSGGQKQRVAIARALAMNPR 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryPT------KGMFVDQDKMYRDTKAIFDELDididprAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 155 VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-205 |
8.28e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 18 KELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVvGVVF--QDFQ---LFPHLSI 92
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYlpEDRQssgLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 93 FDNITLAPKNVLKqpkeVYTKKAKELA------ESLGI--SDLlDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSA 164
Cdd:PRK15439 359 AWNVCALTHNRRG----FWIKPARENAvleryrRALNIkfNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 165 LDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-205 |
1.16e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFN---PAE-LKNreqvvGVVF--QDFQ---LFPHLSIFDNIT 97
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrsPQDgLAN-----GIVYisEDRKrdgLVLGMSVKENMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 98 LApknVLKQpkevYTKKAKEL---AESLGISDLLDSYPFQ----------LSGGQKQRVAIARALAMNPRVLAYDEPTSA 164
Cdd:PRK10762 353 LT---ALRY----FSRAGGSLkhaDEQQAVSDFIRLFNIKtpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 165 LDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK10762 426 VDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRIL 466
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
8-204 |
2.35e-13 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 65.29 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 8 SKTFGKKQVIKELDlVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepfnpaelknreqvvgvvfqdfqlf 87
Cdd:cd03222 7 VKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 88 phlsifdnITLAPKnvlkqPKEVytkkakelaeslgisdlldsypfQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:cd03222 61 --------ITPVYK-----PQYI-----------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 168 ELRQQVEKLIVSLKEEGV-TQIIVTHDLVFAENVSDQL 204
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRI 142
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-190 |
2.44e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 21 DLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFyldQEPFNPAELKNREQVVGVVFQDFQLFPHlsifDNITLAP 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGER---QSQFSHITRLSFEQLQKLVSDEWQRNNT----DMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 101 KNVLKQPKEV---YTKKA---KELAESLGISDLLDSyPF-QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQV 173
Cdd:PRK10938 96 DDTGRTTAEIiqdEVKDParcEQLAQQFGITALLDR-RFkYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170
....*....|....*..
gi 1055940219 174 EKLIVSLKEEGVTQIIV 190
Cdd:PRK10938 175 AELLASLHQSGITLVLV 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-192 |
2.51e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAG-----------L--EKADSGEFYLDqepfnpa 68
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLfgRRRGSGETIWD------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 69 eLKnreQVVGVVFQDFQLFPHLSI----------FDNItlapkNVLKQPKEVYTKKAKELAESLGISDLLDSYPFQ-LSG 137
Cdd:PRK10938 334 -IK---KHIGYVSSSLHLDYRVSTsvrnvilsgfFDSI-----GIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSW 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 138 GQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQII-VTH 192
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSH 460
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-204 |
3.37e-13 |
|
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: 67.73 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 4 LKKVSKTFGKKQViKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpAELKNREQVVGVVFQD 83
Cdd:TIGR01257 934 LVKIFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLFPHLSIFDNITLAPKNVLKQPKEVYTKkAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQLE-MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 164 ALDPELRQQVEKLIVSLKeEGVTQIIVTHDLVFAENVSDQL 204
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-194 |
3.39e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHlSIF 93
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 DNITLAPKNVLKQPKEvytkKAKELAE-SLGISDLLDSYPFQ-------LSGGQKQRVAIARALAMNPRVLAYDEPTSAL 165
Cdd:PRK10789 407 NNIALGRPDATQQEIE----HVARLASvHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190
....*....|....*....|....*....|.
gi 1055940219 166 DPELRQQVEKlivSLKE--EGVTQIIVTHDL 194
Cdd:PRK10789 483 DGRTEHQILH---NLRQwgEGRTVIISAHRL 510
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-196 |
3.41e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 8 SKTfgKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGlekadsgefyldqepfnpaELKNREQVVGVVFQDFQLF 87
Cdd:PLN03232 626 SKT--SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------------------ELSHAETSSVVIRGSVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 88 PHLSIFDNITLApKNVL---KQPKEVYTKKAKELAeslgISDLLDSYP-----------FQLSGGQKQRVAIARALAMNP 153
Cdd:PLN03232 685 PQVSWIFNATVR-ENILfgsDFESERYWRAIDVTA----LQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 154 RVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVF 196
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF 802
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-199 |
4.91e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQ--EPFNP---- 67
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevaYFDQhrAELDPektv 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 68 ----AELKNREQVVGV------VFQDFqLFPhlsifdnitlapknvlkqPKEVYTK-KAkelaeslgisdlldsypfqLS 136
Cdd:PRK11147 401 mdnlAEGKQEVMVNGRprhvlgYLQDF-LFH------------------PKRAMTPvKA-------------------LS 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 137 GGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLkeEGvTQIIVTHDLVFAEN 199
Cdd:PRK11147 443 GGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY--QG-TVLLVSHDRQFVDN 502
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-191 |
5.87e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE---FYLDQepfnpAELKNREQV-- 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvevLGGDM-----ADARHRRAVcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 77 --------VGVvfqdfQLFPHLSIFDNI----TLapknvlkqpkevYTKKAKELAESlgISDLLDS---YPF------QL 135
Cdd:NF033858 77 riaympqgLGK-----NLYPTLSVFENLdffgRL------------FGQDAAERRRR--IDELLRAtglAPFadrpagKL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 136 SGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEE--GVTQIIVT 191
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVAT 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-205 |
6.10e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGL-EKADSGEFYLDQEPF---NPAElkNREQVVGVVFQD---FQLFPHLSIFDNITLA 99
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVkirNPQQ--AIAQGIAMVPEDrkrDGIVPVMGVGKNITLA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 100 pknVLKQpkevYTK-----KAKELA---ESLGISDLLDSYPFQ----LSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:PRK13549 366 ---ALDR----FTGgsridDAAELKtilESIQRLKVKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 168 ELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK13549 439 GAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-194 |
7.50e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKV-SKTFGKkqvIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYL---DQEPFNPAE-LKNREQVV 77
Cdd:PRK09700 267 EVRNVtSRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLngkDISPRSPLDaVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 78 GVVFQDFQLFPHLSIFDNITLAPKnvLKQPKE------VYTKKAKELAES----LGIS-DLLDSYPFQLSGGQKQRVAIA 146
Cdd:PRK09700 344 TESRRDNGFFPNFSIAQNMAISRS--LKDGGYkgamglFHEVDEQRTAENqrelLALKcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1055940219 147 RALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-192 |
2.14e-12 |
|
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: 65.16 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGL---------EKADSGEFYLDQEP-FNPAELknREQVVgvvfqdfq 85
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrltKPAKGKLFYVPQRPyMTLGTL--RDQII-------- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 86 lFPHlSIFDnitlapknvlKQPKEVYTKKAKELAESLGISDLLD---------SYPFQLSGGQKQRVAIARALAMNPRVL 156
Cdd:TIGR00954 537 -YPD-SSED----------MKRRGLSDKDLEQILDNVQLTHILEreggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 1055940219 157 AYDEPTSALDPELRQQVEKLivsLKEEGVTQIIVTH 192
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRL---CREFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-199 |
3.36e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 21 DLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEpFNPAELknrEQ-----VVGVVFqDF------QLFPH 89
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQD-LIVARL---QQdpprnVEGTVY-DFvaegieEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 LSIFDNITlapKNVLKQPKEVYTKKAKELAESLGISDL--LDSYPFQ---------------LSGGQKQRVAIARALAMN 152
Cdd:PRK11147 98 LKRYHDIS---HLVETDPSEKNLNELAKLQEQLDHHNLwqLENRINEvlaqlgldpdaalssLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 153 PRVLAYDEPTSALDPELRQQVEKLivsLKEEGVTQIIVTHDLVFAEN 199
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISHDRSFIRN 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-200 |
3.40e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGlekadsgefyldqepfnpaELKNREQVVGVVFQDFQLFPHLS 91
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG-------------------ELPPRSDASVVIRGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 -IF-----DNITL-APKNVLKQPKEVYTKKAKELAESLGISDLLD--SYPFQLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:PLN03130 689 wIFnatvrDNILFgSPFDPERYERAIDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 163 SALDPELRQQV-EKLIvslKEE--GVTQIIVTHDLVFAENV 200
Cdd:PLN03130 769 SALDAHVGRQVfDKCI---KDElrGKTRVLVTNQLHFLSQV 806
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-204 |
6.31e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGefylDQEPFNPAELKNreqvVGVVFQDFQLFPHLSIFDNITLAPKNVL-- 104
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSG----DATVAGKSILTN----ISDVHQNMGYCPQFDAIDDLLTGREHLYly 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 105 ----KQPKEVYTKKAKELAESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSL 180
Cdd:TIGR01257 2037 arlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170 180
....*....|....*....|....
gi 1055940219 181 KEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:TIGR01257 2117 IREGRAVVLTSHSMEECEALCTRL 2140
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-191 |
8.48e-12 |
|
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: 61.49 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD--SGEFYLDQEPFNpaelKNREQVVGVVFQDFQLFPH 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 LSIfdnitlapknvlkqpkevytkkakelAESLGISDLLDSypfqLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPEL 169
Cdd:cd03232 94 LTV--------------------------REALRFSALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|..
gi 1055940219 170 RQQVEKLIVSLKEEGVTqIIVT 191
Cdd:cd03232 144 AYNIVRFLKKLADSGQA-ILCT 164
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-192 |
1.09e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.97 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD--SGEFYLDQEPFNPAELKNREQvVG 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAH-LG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 vVFQDFQL---FPHLSIFDNITLAPKNVLKQpkevYTKKAKELAESLGI----SDLLDSYPFQL--------SGGQKQRV 143
Cdd:CHL00131 86 -IFLAFQYpieIPGVSNADFLRLAYNSKRKF----QGLPELDPLEFLEIinekLKLVGMDPSFLsrnvnegfSGGEKKRN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 144 AIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-196 |
1.29e-11 |
|
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: 63.04 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 20 LDLVIPDGKTLAIVGPSGGGKTTLLR-VLAGLEKadsgefyldqepfnpaeLKNREQVVGVVfqdfQLFPHLSIFDNITL 98
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-----------------VEGHVHMKGSV----AYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 99 ApKNVL--KQPKEVYTKKAKELAESLGISDLLDS--------YPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE 168
Cdd:TIGR00957 716 R-ENILfgKALNEKYYQQVLEACALLPDLEILPSgdrteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190
....*....|....*....|....*....|
gi 1055940219 169 LRQQVEKLIVSLKE--EGVTQIIVTHDLVF 196
Cdd:TIGR00957 795 VGKHIFEHVIGPEGvlKNKTRILVTHGISY 824
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-166 |
1.51e-11 |
|
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: 61.12 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 6 KVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD---SGEFYLDQEPFNPAELKNREQVVGVVFQ 82
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 83 DFQlFPHLSIFDNITLApknvlkqpkevytkkakelAESLGisdllDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPT 162
Cdd:cd03233 92 DVH-FPTLTVRETLDFA-------------------LRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
....
gi 1055940219 163 SALD 166
Cdd:cd03233 147 RGLD 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-166 |
1.85e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 13 KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLA----GLEKADSGEFYLDQEPfnPAELKN--REQVVGVVFQDFQl 86
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT--PEEIKKhyRGDVVYNAETDVH- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 87 FPHLSIFDNITLAPKnvLKQP--------KEVYTKKAKEL-AESLGISDLLDS-----YPFQLSGGQKQRVAIARALAMN 152
Cdd:TIGR00956 150 FPHLTVGETLDFAAR--CKTPqnrpdgvsREEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGG 227
|
170
....*....|....
gi 1055940219 153 PRVLAYDEPTSALD 166
Cdd:TIGR00956 228 AKIQCWDNATRGLD 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-205 |
2.46e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKN--REQVV---------GVVfqdfqlfPHLSIFDN 95
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaiRAGIMlcpedrkaeGII-------PVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 I-------TLAPKNVLKQPKEvyTKKAKELAESLGISDLLDSYPF-QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:PRK11288 352 InisarrhHLRAGCLINNRWE--AENADRFIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 168 ELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK11288 430 GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-175 |
4.45e-11 |
|
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: 61.46 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 10 TFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADsGEFYLDQEPFNPAELKNREQVVGVVFQdfQLFPH 89
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ--KVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 90 LSIFDnitlapKNVlkQPKEVYT-KKAKELAESLGISDLLDSYP----FQL-------SGGQKQRVAIARALAMNPRVLA 157
Cdd:TIGR01271 1305 SGTFR------KNL--DPYEQWSdEEIWKVAEEVGLKSVIEQFPdkldFVLvdggyvlSNGHKQLMCLARSILSKAKILL 1376
|
170
....*....|....*...
gi 1055940219 158 YDEPTSALDPELRQQVEK 175
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIRK 1394
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
3-166 |
5.99e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 3 ELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE-------FYLDQEPFnpaelknrEQ 75
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEgdirisgFPKKQETF--------AR 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 76 VVGVVFQDFQLFPHLS-----IFDNITLAPKNVLKQPKEVYTKKAKELAESLGISDLLDSYP--FQLSGGQKQRVAIARA 148
Cdd:PLN03140 954 ISGYCEQNDIHSPQVTvreslIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVE 1033
|
170
....*....|....*...
gi 1055940219 149 LAMNPRVLAYDEPTSALD 166
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLD 1051
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-194 |
6.09e-11 |
|
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: 59.35 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 15 QVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHlSIFD 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 NItlapknvlkQPKEVYTKKakELAESLGISDLLDSypfqLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVE 174
Cdd:cd03369 101 NL---------DPFDEYSDE--EIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180
....*....|....*....|..
gi 1055940219 175 KLIvslKEE--GVTQIIVTHDL 194
Cdd:cd03369 166 KTI---REEftNSTILTIAHRL 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-204 |
1.98e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKAD--------SGEFYLDQEPF---NPAELKNREQVV------G 78
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLaaiDAPRLARLRAVLpqaaqpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 79 VVFQDFQL-----FPHLSIFDNITLAPKNVLKQpkevytkkAKELAeslGISDLLDSYPFQLSGGQKQRVAIARALAM-- 151
Cdd:PRK13547 96 FAFSAREIvllgrYPHARRAGALTHRDGEIAWQ--------ALALA---GATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 152 -------NPRVLAYDEPTSALDPELRQQVEKLIVSLKEE---GVTQIIvtHDLVFAENVSDQL 204
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIV--HDPNLAARHADRI 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-211 |
6.39e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 56.46 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 26 DGKTLaIVGPSGGGKTTLLR----VLAGLEKADSGEFYLDQEPFNPAElknreqVVGVVFQDFQLFP--------HLSIF 93
Cdd:cd03240 22 SPLTL-IVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGE------VRAQVKLAFENANgkkytitrSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 DNItlapknvlkqpkeVYTKK---AKELAESLGisdlldsypfQLSGGQKQ------RVAIARALAMNPRVLAYDEPTSA 164
Cdd:cd03240 95 ENV-------------IFCHQgesNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1055940219 165 LDPE-LRQQVEKLIVSLKEEGVTQIIV-THDLVFaENVSDQLLKVTPNQ 211
Cdd:cd03240 152 LDEEnIEESLAEIIEERKSQKNFQLIViTHDEEL-VDAADHIYRVEKDG 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-196 |
9.56e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 9.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAG-LEKADSGEFYLDQEPFNPAELKNREQVvgvvfqdfqlfphlsifdnitlapknvlk 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 106 qpkevytkkakelaeslgisdLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVS------ 179
Cdd:smart00382 53 ---------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllll 111
|
170
....*....|....*..
gi 1055940219 180 LKEEGVTQIIVTHDLVF 196
Cdd:smart00382 112 KSEKNLTVILTTNDEKD 128
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-194 |
1.22e-09 |
|
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: 57.26 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFphlSIFDN 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLF---SGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 ITLAPKNVLKQpKEVYTkkAKELAESLG-ISDLLDSYPFQ-------LSGGQKQRVAIARALAMNPRVLAYDEPTSALDP 167
Cdd:TIGR00957 1378 MNLDPFSQYSD-EEVWW--ALELAHLKTfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180
....*....|....*....|....*..
gi 1055940219 168 ELRQQVEKLIVSlKEEGVTQIIVTHDL 194
Cdd:TIGR00957 1455 ETDNLIQSTIRT-QFEDCTVLTIAHRL 1480
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-204 |
1.33e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGG--KTTLLRVLAGLEK-----------ADSGEFYLDQEPFNPA 68
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*twcANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 69 ELKNREQVVGVvfqdfqlfphlsifDNITLAPKNVLKQPKEVYTKkAKELAESLGISDLLDSYPFQLSGGQKQRVAIARA 148
Cdd:NF000106 94 R*GRRESFSGR--------------ENLYMIGR*LDLSRKDARAR-ADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 149 LAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQL 204
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHEL 214
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-211 |
2.48e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.25 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKTTLlrVLAGLEKadSGEFYLDQEPFNPAELKnreqvvgVVFQDfQLfphlsifdni 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYA--SGKARLISFLPKFSRNK-------LIFID-QL---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 97 tlapKNVLKqpkevytkkakelaesLGISDL-LDSYPFQLSGGQKQRVAIARALAMNPR--VLAYDEPTSALDPELRQQV 173
Cdd:cd03238 69 ----QFLID----------------VGLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 1055940219 174 EKLIVSLKEEGVTQIIVTHDLVFAENvSDQLLKVTPNQ 211
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
6-205 |
2.89e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 6 KVSKtfGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAglEKADSGEFYLDQEPFNPAEL-KNREQVVGVVFQ-D 83
Cdd:TIGR00956 770 KIKK--EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGRPLdSSFQRSIGYVQQqD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 84 FQLfPHLSIFDNITLAPKnvLKQPKEVYTKKAKELAESlgISDLLD--SYPFQLSG--------GQKQRVAIARALAMNP 153
Cdd:TIGR00956 846 LHL-PTSTVRESLRFSAY--LRQPKSVSKSEKMEYVEE--VIKLLEmeSYADAVVGvpgeglnvEQRKRLTIGVELVAKP 920
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 154 RVLAY-DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD---LVFAEnvSDQLL 205
Cdd:TIGR00956 921 KLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLL 974
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
3.69e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpAELKNREQVVGVV 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQLFPHLSIFDNITLapknvlkqpkEVYTKKAK----ELAESLGISDLLDsYPFQ-LSGGQKQRVAIARALAMNPRV 155
Cdd:PRK13540 80 GHRSGINPYLTLRENCLY----------DIHFSPGAvgitELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 1055940219 156 LAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
12-211 |
6.91e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 12 GKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLR---VLAGLEkadsgefyldqepfNPAELKNREQVVGVVFQDFQLFP 88
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGA--------------QSATRRRSGVKAGCIVAAVSAEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 89 HLSIFdnitlapknvlkqpkevytkkakelaeslgisdlldsypfQLSGGQKQRVAIARALA---MNPRVL-AYDEPTSA 164
Cdd:cd03227 72 IFTRL----------------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEIDRG 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1055940219 165 LDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENvSDQLLKVTPNQ 211
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIVITHLPELAEL-ADKLIHIKKVI 157
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-178 |
7.20e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.34 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 32 IVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNpaelKNREQVVGVVFQDFQLFPHLSIFDNitlapknvLKQPKEVY 111
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN----NIAKPYCTYIGHNLGLKLEMTVFEN--------LKFWSEIY 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 112 TKKAKELA--ESLGISDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIV 178
Cdd:PRK13541 99 NSAETLYAaiHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV 167
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-192 |
8.01e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVV 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 81 FQDFQL---FPHLS--IFDNITLAPKNVLKQPKEV----YTKKAKELAESLGI-SDLLD-SYPFQLSGGQKQRVAIARAL 149
Cdd:PRK09580 81 FMAFQYpveIPGVSnqFFLQTALNAVRSYRGQEPLdrfdFQDLMEEKIALLKMpEDLLTrSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1055940219 150 AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTH 192
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-194 |
8.33e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 14 KQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYldqepfnpAElknreqvvgvvfQDFQLFPHLSIF 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------AE------------RSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 DNITLApKNVLKQPKEvytkKAKELAESLGISDL---LDSYP-----------FQLSGGQKQRVAIARALAMNPRVLAYD 159
Cdd:PTZ00243 733 MNATVR-GNILFFDEE----DAARLADAVRVSQLeadLAQLGggleteigekgVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 EPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECFLGALAGKTRVLATHQV 842
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-177 |
1.74e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 7 VSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADsGEFYLDQEPFNPAELKNREQVVGVVFQDFQL 86
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 87 FphlsifdnitlapKNVLKQPKEVYTKKAKE----LAESLGISDLLDSYPFQL-----------SGGQKQRVAIARALAM 151
Cdd:cd03289 89 F-------------SGTFRKNLDPYGKWSDEeiwkVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLS 155
|
170 180
....*....|....*....|....*.
gi 1055940219 152 NPRVLAYDEPTSALDPELRQQVEKLI 177
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTL 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-193 |
2.16e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 18 KELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGlekadsgefylDQEPfnpaelknreqVVGVVFQDFQLfpHLSIF---- 93
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISG-----------ELQP-----------SSGTVFRSAKV--RMAVFsqhh 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 -DNITLAPKNVLKQPK---EVYTKKAKELAESLGISDLLDSYP-FQLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPE 168
Cdd:PLN03073 582 vDGLDLSSNPLLYMMRcfpGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180
....*....|....*....|....*..
gi 1055940219 169 lrqQVEKLI--VSLKEEGVtqIIVTHD 193
Cdd:PLN03073 662 ---AVEALIqgLVLFQGGV--LMVSHD 683
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-207 |
4.56e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQepfnpaelknreqvvGV- 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK---------------GIk 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 80 --VFQDFQL---------FPHLSifdniTLAPKNVLKQpkevytkkakelaeslgISDLLDSYPFQ----------LSGG 138
Cdd:PRK10636 377 lgYFAQHQLeflradespLQHLA-----RLAPQELEQK-----------------LRDYLGGFGFQgdkvteetrrFSGG 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055940219 139 QKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLkeEGVTqIIVTHDLVFAENVSDQLLKV 207
Cdd:PRK10636 435 EKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGAL-VVVSHDRHLLRSTTDDLYLV 500
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-194 |
6.61e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDFQLFPHLSIFDn 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 96 itLAPknvLKQPKEVYTKKAKELAEslgISDLLDSYPFQL-----------SGGQKQRVAIARALAMNPRVLAYDEPTSA 164
Cdd:PLN03232 1330 --IDP---FSEHNDADLWEALERAH---IKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190
....*....|....*....|....*....|..
gi 1055940219 165 LDPELRQQVEKLIvslKEE--GVTQIIVTHDL 194
Cdd:PLN03232 1402 VDVRTDSLIQRTI---REEfkSCTMLVIAHRL 1430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-207 |
6.37e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 6.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 132 PFQLSGGQKQ------RVAIARALA--------MNPRVLayDEPTSALDPELRQQVEKLIVSLKEEGVTQII-VTHD--L 194
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPPLIL--DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVvVSHDdeL 856
|
90
....*....|...
gi 1055940219 195 VFAenvSDQLLKV 207
Cdd:PRK02224 857 VGA---ADDLVRV 866
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-205 |
8.46e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 2 IELKKVSKTFGKKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAglekadsgEFYLDQEPFNPAELKNREQVVGVVF 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--------MHAIDGIPKNCQILHVEQEVVGDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 82 QDFQLFPHLSIFDNITLAPK-NVLKQPKEVYTKKA------------------KELAESLGISDLLDSYPF--------- 133
Cdd:PLN03073 250 TALQCVLNTDIERTQLLEEEaQLVAQQRELEFETEtgkgkgankdgvdkdavsQRLEEIYKRLELIDAYTAearaasila 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 134 --------------QLSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEegvTQIIVTHDLVFAEN 199
Cdd:PLN03073 330 glsftpemqvkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK---TFIVVSHAREFLNT 406
|
....*.
gi 1055940219 200 VSDQLL 205
Cdd:PLN03073 407 VVTDIL 412
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
134-191 |
9.58e-06 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 44.94 E-value: 9.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 134 QLSGGQKQRVAIARALAMN-----PRVLaYDEPTSALDPELRQQVEKLIVSLKEEgvTQIIVT 191
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
135-193 |
2.92e-05 |
|
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: 43.40 E-value: 2.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 135 LSGGQKQRVAIARALAMNPRVLAY--DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD 193
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-205 |
6.55e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 6.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055940219 135 LSGGQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVSDQLL 205
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 462
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-194 |
7.84e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 31 AIVGPSGGGKTTLLRVLA-GLEKADSGEFYLDQEPFNPAELKNReqvVGVVFQ-------------DFQLFPHLS----- 91
Cdd:COG0419 27 LIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLINVGSEEAS---VELEFEhggkryrierrqgEFAEFLEAKpserk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 92 -IFDNITLAPK-----NVLKQPKEVYTKKAKELAESLGI-----SDLLDSYPF-QLSGGQKQRVAIARALAMnprVLayD 159
Cdd:COG0419 104 eALKRLLGLEIyeelkERLKELEEALESALEELAELQKLkqeilAQLSGLDPIeTLSGGERLRLALADLLSL---IL--D 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1055940219 160 epTSALDPELRQQVEKLIVSLKeegvtqiIVTHDL 194
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
123-206 |
1.51e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 123 GISDLLDSypfqLSGGQKQ------RVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLI-VSLKEEGVTQ--IIVTH- 192
Cdd:PRK01156 794 GMVEGIDS----LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeYSLKDSSDIPqvIMISHh 869
|
90
....*....|....*
gi 1055940219 193 -DLVFAENVSDQLLK 206
Cdd:PRK01156 870 rELLSVADVAYEVKK 884
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-201 |
1.74e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 17 IKELDLVIPDGKTlAIVGPSGGGKTTLLRVLAGLEKADSGEFYLDQEPFNPAELKNREQVVGVVFQDF--QLFPHLsIFD 94
Cdd:COG3593 14 IKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGSLlsRLLRLL-LKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 95 NITLAPKNVLKQPKEVYTKKAKELAESL--------------------GISDLLDSYPFQLSGGQK----------QRV- 143
Cdd:COG3593 92 EDKEELEEALEELNEELKEALKALNELLseylkelldgldlelelsldELEDLLKSLSLRIEDGKElpldrlgsgfQRLi 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055940219 144 --AIARALAM-----NPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVS 201
Cdd:COG3593 172 llALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVP 236
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-211 |
2.36e-04 |
|
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: 40.72 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 1 MIELKKVSKTFG---KKQVI--KELDlvipDGKTLAIVGPSGGGKTTLLRV----LAGlEKADSGEFYLDQEPFNPAELK 71
Cdd:cd03279 1 MKPLKLELKNFGpfrEEQVIdfTGLD----NNGLFLICGPTGAGKSTILDAityaLYG-KTPRYGRQENLRSVFAPGEDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 72 NReqvvgVVFqDFQL---------FPHLSI--FDNITLAPKNvlkqpkevytkkakelaeslGISDLLDSYPFQLSGGQK 140
Cdd:cd03279 76 AE-----VSF-TFQLggkkyrverSRGLDYdqFTRIVLLPQG--------------------EFDRFLARPVSTLSGGET 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 141 QRVAIARALAMNpRVLAY-----------DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENVsDQLLKVTP 209
Cdd:cd03279 130 FLASLSLALALS-EVLQNrggarlealfiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERI-PQRLEVIK 207
|
..
gi 1055940219 210 NQ 211
Cdd:cd03279 208 TP 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-207 |
2.88e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 24 IPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF---------YLDQEpfNPA-ELKNREQVVGVVFQDFQLFPHLSIF 93
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlaWVNQE--TPAlPQPALEYVIDGDREYRQLEAQLHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 94 ----DNITLAPKNVLKQPKEVYT--KKAKELAESLGIS-DLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTSALD 166
Cdd:PRK10636 102 nernDGHAIATIHGKLDAIDAWTirSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1055940219 167 PELRQQVEKLivsLKEEGVTQIIVTHDLVFAENVSDQLLKV 207
Cdd:PRK10636 182 LDAVIWLEKW---LKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-202 |
3.74e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 135 LSGGQKQRVAIARALAMNPRVLAY--DEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHD---LVFAENVSD 202
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIID 549
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
138-193 |
5.28e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 5.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055940219 138 GQKQRVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLivsLKEEGVTQIIVTHD 193
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMIIISHD 211
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
17-57 |
7.92e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 7.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1055940219 17 IKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGE 57
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGA 225
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
135-194 |
9.16e-04 |
|
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: 39.13 E-value: 9.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 135 LSGGQKQRVAIARALAMNPR-----VLayDEPTSALDPElrqQVEKLIV---SLKEEGVTQIIVTHDL 194
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktlyIL--DEPTTGLHFH---DVKKLLEvlqRLVDKGNTVVVIEHNL 232
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
132-196 |
9.53e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 9.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 132 PFQLSGGQKQ---RVAIARALAMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVF 196
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
13-48 |
2.06e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 38.63 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1055940219 13 KKQVIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLA 48
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
121-209 |
4.20e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 121 SLGISDLLDSYP-FQLSGGQKQRVAIARAL---AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVF 196
Cdd:PRK00635 795 SLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV 874
|
90
....*....|...
gi 1055940219 197 AEnVSDQLLKVTP 209
Cdd:PRK00635 875 VK-VADYVLELGP 886
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-194 |
5.36e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 5.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055940219 135 LSGGQKQRVAIARAL---AMNPRVLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDL 194
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
135-208 |
5.71e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 36.13 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 135 LSGGQKQRVAIARALAMN-----P-RVLayDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENvSDQLLKVT 208
Cdd:cd03239 95 LSGGEKSLSALALIFALQeikpsPfYVL--DEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFEN-ADKLIGVL 171
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
27-57 |
6.12e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 6.12e-03
10 20 30
....*....|....*....|....*....|.
gi 1055940219 27 GKTLAIVGPSGGGKTTLLRVLAGLEKADSGE 57
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLPELVLATGE 115
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-209 |
6.44e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 6.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055940219 135 LSGGQKQRVAIARALAMNPR---VLAYDEPTSALDPELRQQVEKLIVSLKEEGVTQIIVTHDLVFAENvSDQLLKVTP 209
Cdd:PRK00635 1700 LSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
11-48 |
7.92e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 35.58 E-value: 7.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1055940219 11 FGKKQVIKELDLVI--PDGKTLAIVGPSGGGKTTLLRVLA 48
Cdd:cd00009 1 VGQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIA 40
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
16-58 |
8.87e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 36.19 E-value: 8.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1055940219 16 VIKELDLVIPDGKTLAIVGPSGGGKTTLLRVLAGLEKADSGEF 58
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDF 44
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
91-166 |
9.30e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 36.31 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055940219 91 SIFDNITLA------PKNVLKQPKEvyTKKAKELAESLGI-SDLLDSYPFQLSGGQKQRVAIARALAMNPRVLAYDEPTS 163
Cdd:NF040905 356 DIKRNITLAnlgkvsRRGVIDENEE--IKVAEEYRKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
...
gi 1055940219 164 ALD 166
Cdd:NF040905 434 GID 436
|
|
| |
