|
Name |
Accession |
Description |
Interval |
E-value |
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-240 |
0e+00 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 548.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHVS 240
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHVS 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
1.57e-164 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 453.68 E-value: 1.57e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHV 239
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
8.15e-141 |
|
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: 393.05 E-value: 8.15e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
2.26e-121 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 345.63 E-value: 2.26e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG------------LKVNDP 68
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgeLVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 69 KVDERlIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIA 148
Cdd:COG4598 88 RQLQR-IRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPP 228
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
250
....*....|
gi 16128777 229 SQRLQEFLQH 238
Cdd:COG4598 247 SERLRQFLSS 256
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-237 |
1.69e-102 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 297.43 E-value: 1.69e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEE-----ITSGDLIVDGLK-VNDPKVDERL 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTARsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQE 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
...
gi 16128777 235 FLQ 237
Cdd:PRK11264 243 FLE 245
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
9.43e-97 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 285.82 E-value: 9.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQE 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*
gi 16128777 235 FLQHV 239
Cdd:COG1135 240 FLPTV 244
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.70e-96 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 280.01 E-value: 4.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--L 74
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
4.73e-95 |
|
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: 277.45 E-value: 4.73e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--LI 75
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-238 |
5.92e-95 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 278.05 E-value: 5.92e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP-KVDE---RLIRQ 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSqKPSEkaiRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNpQVLIKNPPSQRLQEFLQ 237
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYLS 241
|
.
gi 16128777 238 H 238
Cdd:COG4161 242 H 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-238 |
1.09e-94 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 277.28 E-value: 1.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-----DPKvDERLIR 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpSDK-AIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLiKNPPSQRLQEFL 236
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF-TQPQTEAFKNYL 240
|
..
gi 16128777 237 QH 238
Cdd:PRK11124 241 SH 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
8.02e-92 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 273.90 E-value: 8.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNV----G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAFG-LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 161 DEPTSALDPELRHEvlkvMQD-----LAEEGMTMVIVTH--EIGFAekVASRLIFIDKGRIAEDGNPQVLIKNPPS 229
Cdd:COG3842 160 DEPLSALDAKLREE----MREelrrlQRELGITFIYVTHdqEEALA--LADRIAVMNDGRIEQVGTPEEIYERPAT 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.11e-91 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 270.42 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvderliR 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALG-LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 157 MMLFDEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAED 217
Cdd:COG1116 159 VLLMDEPFGALDALTRER----LQDEllrlwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
3.56e-89 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 262.68 E-value: 3.56e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQE 78
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREiPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-239 |
4.22e-89 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 263.61 E-value: 4.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV------NDPKV--DER 73
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrNGPLVpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 74 ---LIRQEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
Cdd:TIGR03005 81 hlrQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPS 229
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|
gi 16128777 230 QRLQEFLQHV 239
Cdd:TIGR03005 241 ERTREFLSKV 250
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
1.52e-88 |
|
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: 261.45 E-value: 1.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IRQEA 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFgPLRVRGA-NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAF-PLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVlIKNPPSQRLQEFL 236
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE-LLASDDPWVRQFL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
1.35e-87 |
|
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: 259.05 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPT----QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
5.35e-87 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 258.06 E-value: 5.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQE 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHLTALENVMFGPL-------RVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
2.80e-86 |
|
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: 254.75 E-value: 2.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI----GM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 162 EPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03259 156 EPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-237 |
9.00e-85 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 252.97 E-value: 9.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG------------LKVNDpKVDERLIR 76
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVAD-KNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAH-HYPSELSGGQQQRVAIARALAVKP 155
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEF 235
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQF 251
|
..
gi 16128777 236 LQ 237
Cdd:PRK10619 252 LK 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
1.49e-83 |
|
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: 248.16 E-value: 1.49e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlirq 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 eAGMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03293 75 -RGYVFQQDALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 158 MLFDEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAED 217
Cdd:cd03293 153 LLLDEPFSALDALTREQ----LQEElldiwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-227 |
4.42e-83 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 251.53 E-value: 4.42e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 161 DEPTSALDPELRHEV---LKVMQdlAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG3839 158 DEPLSNLDAKLRVEMraeIKRLH--RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
4.85e-83 |
|
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: 247.25 E-value: 4.85e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVS-KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE--LRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQ----QfyLFpHLTALENVMFGPLRvRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG1122 79 LVFQnpddQ--LF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
1.70e-82 |
|
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: 246.33 E-value: 1.70e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFG-PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-DPKVDERLIRQEA 79
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGPLRVR-------GANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
3.60e-82 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 249.29 E-value: 3.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPkVDERLIrqea 79
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTNLP-PRERRV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-236 |
2.09e-81 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 243.74 E-value: 2.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLIR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPhLTALENVMFGPlRVRGA-NKEEAEKLARELLAKVGLAE----RAHHYPSELSGGQQQRVAIARAL 151
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQR 231
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*
gi 16128777 232 LQEFL 236
Cdd:TIGR00972 239 TEDYI 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-239 |
3.30e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 242.66 E-value: 3.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENV-MFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG1131 78 VPQEPALYPDLTVRENLrFFA--RLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIknppSQRLQE-FLQHV 239
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK----ARLLEDvFLELT 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
2.49e-79 |
|
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: 247.12 E-value: 2.49e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERL 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFY--LFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARAL 151
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
4.61e-79 |
|
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: 237.40 E-value: 4.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-IRQEAG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFgPLRVRGA-NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVlIKNPPSQRLQEF 235
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRASDDPLVRQF 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.52e-78 |
|
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: 234.00 E-value: 1.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGplrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-218 |
3.51e-78 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 238.93 E-value: 3.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-236 |
2.00e-76 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 233.06 E-value: 2.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD--LDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGL--AERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDP----ELRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQ 233
Cdd:COG1125 158 LLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
...
gi 16128777 234 EFL 236
Cdd:COG1125 235 DFV 237
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-239 |
1.62e-75 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 233.46 E-value: 1.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG--PTQVL----------------------HNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSG 56
Cdd:COG4175 3 KIEVRNLYKIFGkrPERALklldqgkskdeilektgqtvgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 57 DLIVDG---LKVNDpkvdERLI---RQEAGMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERA 130
Cdd:COG4175 83 EVLIDGediTKLSK----KELRelrRKKMSMVFQHFALLPHRTVLENVAFG-LEIQGVPKAERRERAREALELVGLAGWE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 131 HHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASR 205
Cdd:COG4175 158 DSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRRE----MQDEllelqAKLKKTIVFITHDLDEALRLGDR 233
|
250 260 270
....*....|....*....|....*....|....*
gi 16128777 206 lIFIDK-GRIAEDGNPQVLIKNPPSQRLQEFLQHV 239
Cdd:COG4175 234 -IAIMKdGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
3.23e-75 |
|
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: 227.95 E-value: 3.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQE 78
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHLTALENVMFGPLRVR-------GANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
3.34e-75 |
|
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: 227.45 E-value: 3.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEI-----TSGDLIVDGLKVNDPKVDERLIR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPhLTALENVMFGPlRVRG-ANKEEAEKLARELLAKVGLAE----RAHhyPSELSGGQQQRVAIARAL 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGiKLKEELDERVEEALRKAALWDevkdRLH--ALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
6.04e-75 |
|
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: 226.93 E-value: 6.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDE---- 72
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF--ALDEdara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 73 RLIRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANkeEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-239 |
6.09e-75 |
|
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: 228.30 E-value: 6.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 7 VSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDER----LIRQEAGMV 82
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA--AMSRKelreLRRKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:cd03294 108 FQSFALLPHRTVLENVAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 163 PTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQ 237
Cdd:cd03294 187 AFSALDPLIRRE----MQDEllrlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
..
gi 16128777 238 HV 239
Cdd:cd03294 263 GV 264
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
9.69e-74 |
|
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: 223.11 E-value: 9.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE--LRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQ----QFYlfpHLTALENVMFGPLRvRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:cd03225 79 LVFQnpddQFF---GPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
4.12e-72 |
|
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: 219.30 E-value: 4.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 -QEAGMVFQQFY--LFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGL---AERAHHYPSELSGGQQQRVAIARA 150
Cdd:cd03257 81 rKEIQMVFQDPMssLNPRMTIGEQIAE-PLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
7.84e-71 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 217.21 E-value: 7.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKL-EEI----TSGDLIVDGLKVNDPKVDERLIR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIpgarVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHlTALENVMFGPlRVRG-ANKEEAEKLARELLAKVGL----AERAHHYPSELSGGQQQRVAIARAL 151
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGL-RLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 152 AVKPKMMLFDEPTSALDP-------ELrhevlkvMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|..
gi 16128777 225 KNPPSQRLQEFL 236
Cdd:COG1117 242 TNPKDKRTEDYI 253
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-237 |
2.68e-70 |
|
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: 215.24 E-value: 2.68e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE--QDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGL--AERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQ 237
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-234 |
1.35e-69 |
|
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: 213.90 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFY--LFPHLTaLENVMFGPLRVRGanKEEAEKLARELLAKVGLAER-AHHYPSELSGGQQQRVAIARALAV 153
Cdd:COG1124 79 RRVQMVFQDPYasLHPRHT-VDRILAEPLRIHG--LPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL---IKNPPS 229
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLlagPKHPYT 235
|
....*
gi 16128777 230 QRLQE 234
Cdd:COG1124 236 RELLA 240
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
1.53e-69 |
|
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: 213.25 E-value: 1.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPV----NT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 162 EPTSALDPELRHEV---LKVMQDlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:cd03300 156 EPLGALDLKLRKDMqleLKRLQK--ELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
3.65e-68 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 209.61 E-value: 3.65e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGpTQVLHnIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaG 80
Cdd:COG3840 1 MLRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPV----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFG--P-LRVrgaNKEEAEKLArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGlrPgLKL---TAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
6.49e-67 |
|
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: 206.81 E-value: 6.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNV----GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGA----NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFG-LRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.54e-66 |
|
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: 204.79 E-value: 1.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQE 78
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-237 |
2.55e-66 |
|
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: 206.53 E-value: 2.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-DPKVDERLI 75
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQqfylFPH-----LTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAER-AHHYPSELSGGQQQRVAIAR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN-- 226
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDvd 235
|
250 260
....*....|....*....|
gi 16128777 227 ---------PPSQRLQEFLQ 237
Cdd:TIGR04521 236 elekigldvPEITELARKLK 255
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
3.36e-66 |
|
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: 204.03 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI----AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 162 EPTSALDPELRHEV---LKVMQdlAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03301 156 EPLSNLDAKLRVQMraeLKRLQ--QRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-221 |
1.09e-65 |
|
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: 204.12 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERliRQEAG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--ARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFG--P-LRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
2.05e-65 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 206.47 E-value: 2.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqEAGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR----KVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFG----PLRVRgANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlPRRER-PNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 16128777 237 QHV 239
Cdd:PRK10851 238 GEV 240
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-235 |
5.14e-65 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 205.66 E-value: 5.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqEAGM 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR----DYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 162 EPTSALDPE----LRHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEF 235
Cdd:TIGR03265 160 EPLSALDARvrehLRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADF 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
5.89e-65 |
|
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: 209.76 E-value: 5.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEIT---SGDLIVDGLKVNDpkVDERLI 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE--LSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFY--LFPhLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:COG1123 82 GRRIGMVFQDPMtqLNP-VTVGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-236 |
6.02e-65 |
|
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: 201.62 E-value: 6.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE---DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENV-MFGPLRvrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAELY--GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAF 232
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-237 |
3.04e-64 |
|
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: 200.73 E-value: 3.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERL--IRQ 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL---DTLDEENLweIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQ----QFYlfpHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:TIGR04520 78 KVGMVFQnpdnQFV---GATVEDDVAFGL-ENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIKN------ 226
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQvellke 232
|
250
....*....|....*.
gi 16128777 227 -----PPSQRLQEFLQ 237
Cdd:TIGR04520 233 igldvPFITELAKALK 248
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
1.33e-63 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 202.48 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQeagm 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNT---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEV---LKVMQdlAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK09452 170 ESLSALDYKLRKQMqneLKALQ--RKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
2.97e-63 |
|
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: 196.47 E-value: 2.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQV-LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAF-ALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
3.13e-63 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 197.23 E-value: 3.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIrqeaG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK---PPRRARRRI----G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYL---FPhLTALENVMFGPLRVRGA----NKEEAEKlARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVRDVVLMGRYGRRGLfrrpSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-239 |
7.05e-63 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 200.46 E-value: 7.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE--RLIRQEAGMVFQQF 86
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrEVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 YLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 167 LDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHV 239
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-236 |
9.40e-63 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 199.56 E-value: 9.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDI----CM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
3.30e-62 |
|
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: 192.23 E-value: 3.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVmfgplrvrgankeeaeklarellakvglaerahhypsELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
1.95e-61 |
|
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: 195.27 E-value: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEE---ITSGDLIVDGLKVNDPKVDE- 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 73 RLIR-QEAGMVFQQFY--LFPHLTALENVMFgPLRV-RGANKEEAEKLARELLAKVGL---AERAHHYPSELSGGQQQRV 145
Cdd:COG0444 81 RKIRgREIQMIFQDPMtsLNPVMTVGDQIAE-PLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
...
gi 16128777 225 KNP 227
Cdd:COG0444 240 ENP 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-227 |
4.04e-61 |
|
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: 192.56 E-value: 4.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRqeAG 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-AR--LG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MV--FQQFYLFPHLTALENVMFGPLRVRGAN--------------KEEAEKLARELLAKVGLAERAHHYPSELSGGQQQR 144
Cdd:COG0411 81 IArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
....
gi 16128777 224 IKNP 227
Cdd:COG0411 241 RADP 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
6.27e-61 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 192.00 E-value: 6.27e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlir 76
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 qeaGMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 157 MMLFDEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFIDK--GRIAE 216
Cdd:COG4525 155 FLLMDEPFGALDALTREQ----MQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVE 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-227 |
8.61e-61 |
|
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: 190.73 E-value: 8.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAGM 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI-ARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVM----------FGPLRVRGANKEEAEKlARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:cd03219 80 TFQIPRLFPELTVLENVMvaaqartgsgLLLARARREEREARER-AEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-220 |
1.89e-60 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 194.09 E-value: 1.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVF 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV----GMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 QQFYLFPHLTALENVMFGpLRVRGANKEEAEKL---ARELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11000 82 QSYALYPHLSVAENMSFG-LKLAGAKKEEINQRvnqVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 161 DEPTSALDPEL----RHEVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP 220
Cdd:PRK11000 158 DEPLSNLDAALrvqmRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
2.09e-60 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 188.87 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGM 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE--WRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHlTALENVMFgPLRVRgaNKEEAEKLARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPF-PFQLR--ERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 161 DEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
14-216 |
5.20e-59 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 186.02 E-value: 5.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--LIRQEAGMVFQQFYLFPH 91
Cdd:TIGR02211 18 TRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakLRNKKLGFIYQFHHLLPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:TIGR02211 98 FTALENVAM-PLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128777 172 RHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
Cdd:TIGR02211 177 AKIIFDLMLELnRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-209 |
3.03e-56 |
|
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: 178.19 E-value: 3.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG---LKVNDPKVDErLIRQEAGM 81
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGqetPPLNSKKASK-FRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGPLRVRGaNKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFI 209
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-214 |
4.40e-56 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 178.37 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI- 75
Cdd:NF038007 1 MLNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 -RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:NF038007 81 rRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRI 214
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
3.20e-54 |
|
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: 185.04 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ--IDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFGplrVRGANKEEAEKLARellaKVGLAERAHHYP-----------SELSGGQQQRVAIA 148
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG---DPDATDEEIIEAAR----LAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-226 |
4.74e-54 |
|
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: 173.00 E-value: 4.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAGM 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER-ARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-227 |
5.03e-54 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 176.46 E-value: 5.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--------GPTQVLH---NIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKV 70
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 71 DE-RLIRQEAGMVFQQFY--LFPHLTALENVMFgPLRVRG-ANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRV 145
Cdd:COG4608 88 RElRPLRRRMQMVFQDPYasLNPRMTVGDIIAE-PLRIHGlASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
...
gi 16128777 225 KNP 227
Cdd:COG4608 247 ARP 249
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-240 |
5.48e-54 |
|
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: 176.53 E-value: 5.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 32 IIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALENVMFgPLRVRGANKE 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHI----NMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 112 EAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMV 190
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128777 191 IVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHVS 240
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEIN 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
1.16e-53 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 176.19 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqea 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 160 FDEPTSALDPELRH----EVLKVMQDLaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP 220
Cdd:PRK11650 158 FDEPLSNLDAKLRVqmrlEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-236 |
1.67e-53 |
|
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: 172.13 E-value: 1.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQvLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI----SY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-226 |
3.44e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 180.36 E-value: 3.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD--LTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFpHLTALENVMFGPLrvrGANKEEAEKLARellaKVGLAERAHHYP-----------SELSGGQQQRVAIAR 149
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRP---DATDEEVEEAAK----AAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
3.82e-53 |
|
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: 171.32 E-value: 3.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVF--QQFYLFPHLTALENVMFGpLRVRGANKEEAEKLAR--ELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG0410 80 IGYvpEGRRIFPSLTVEENLLLG-AYARRDRAEVRADLERvyELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
8.51e-53 |
|
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: 167.81 E-value: 8.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQqfylfphltalenvmfgplrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128777 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-234 |
9.59e-53 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 180.30 E-value: 9.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE--RL 74
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIaedgnpqvlIKNPPSQRLQE 234
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI---------VRNPPAQEKVN 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-218 |
1.56e-52 |
|
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: 169.21 E-value: 1.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 21 DLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALENVMF 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV----SMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 101 G---PLRVRGANKEEAEKLarelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK 177
Cdd:cd03298 94 GlspGLKLTAEDRQAIEVA----LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128777 178 VMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-215 |
1.60e-52 |
|
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: 168.87 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkvdeRLIRQEAGMV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-------EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYL---FPhLTALENVMFGPLRVRGA---NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLYGHKGLfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.83e-52 |
|
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: 169.54 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-----GPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV--DGLKVNDPKVD 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 72 ERLI----RQEAGMVFQQFYLFPHLTALENVMfGPLRVRGANKEEAEKLARELLAKVGLAERAHH-YPSELSGGQQQRVA 146
Cdd:COG4778 84 PREIlalrRRTIGYVSQFLRVIPRVSALDVVA-EPLLERGVDREEARARARELLARLNLPERLWDlPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
2.22e-52 |
|
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: 167.17 E-value: 2.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT--QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRD--LDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVmfgplrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGR 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
2-236 |
2.63e-52 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 173.26 E-value: 2.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEI--TSGDLIVDGLKVNDPKVDERLIrqea 79
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAagLTGRIAIADRDLTHAPPHKRGL---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:TIGR03258 82 ALLFQNYALFPHLKVEDNVAFG-LRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEE--GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:TIGR03258 161 LDEPLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFL 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
2.86e-52 |
|
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: 167.23 E-value: 2.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvderlirqeagmv 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 fqqfylfphltalenvmfgplrvrgaNKEEAEKLA--RELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:cd03214 68 --------------------------PKELARKIAyvPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-218 |
4.81e-52 |
|
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: 167.86 E-value: 4.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIA---QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-------LKVNDPKVDERLirqeaGMVFQQF 86
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRKI-----GLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 YLFPHLTALENVMFGplrVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:cd03297 85 ALFPHLNVRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 167 LDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-217 |
5.99e-52 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 169.09 E-value: 5.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAgmvfq 84
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDA----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 85 qfYLFPHLTALENVMFGplrVRGANKEEAeklaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK11247 91 --RLLPWKKVIDNVGLG---LKGQWRDAA----LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 165 SALDPELRHEvlkvMQDLAE-----EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:PRK11247 162 GALDALTRIE----MQDLIEslwqqHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-233 |
1.80e-51 |
|
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: 170.67 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFkNVSKHFGPTQVlhNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLI----- 75
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD---SARGIflpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPHLTALENVMFGplRVRGANKEEAEKLAR--ELLakvGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:COG4148 76 RRRIGYVFQEARLFPHLSVRGNLLYG--RKRAPRAERRISFDEvvELL---GIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRL 232
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
.
gi 16128777 233 Q 233
Cdd:COG4148 231 A 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-194 |
3.86e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 173.28 E-value: 3.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERL-Irq 77
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfRSPRDAQAAgI-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 eaGMVFQQFYLFPHLTALENVMFGPLRVRGA--NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:COG1129 82 --AIIHQELNLVPNLSVAENIFLGREPRRGGliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128777 156 KMMLFDEPTSALDpelRHEV---LKVMQDLAEEGMTMVIVTH 194
Cdd:COG1129 160 RVLILDEPTASLT---EREVerlFRIIRRLKAQGVAIIYISH 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
4.59e-50 |
|
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: 162.65 E-value: 4.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlIRQEAG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED---YRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEklARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW-AALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
5.83e-50 |
|
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: 160.51 E-value: 5.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvDERLIRQEAGMVFQQFYLFPHLTALE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD--ERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 97 NVMFGpLRVRGANKEEAEKLARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:pfam00005 79 NLRLG-LLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
7.14e-50 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 163.41 E-value: 7.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLI 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVFQQFYLFPhLTALENVMFGpLRVRGA-NKEEAEKLARELLAKVGL----AERAHHYPSELSGGQQQRVAIARA 150
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIkDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQ 230
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHK 241
|
....*.
gi 16128777 231 RLQEFL 236
Cdd:PRK14239 242 ETEDYI 247
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-216 |
1.99e-49 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 162.56 E-value: 1.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlirqEAG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 161 DEPTSALDPELRHEvlkvMQDL-----AEEGMTMVIVTHEIGFAEKVASRLIFI--DKGRIAE 216
Cdd:PRK11248 153 DEPFGALDAFTREQ----MQTLllklwQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
14-206 |
2.23e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 161.52 E-value: 2.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--LIRQEAGMVFQQFYLFPH 91
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaeLRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK11629 102 FTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128777 172 RHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRL 206
Cdd:PRK11629 181 ADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-240 |
2.86e-49 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 165.78 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeag 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLArELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVN-EMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 161 DEPTSALDPELRHEV-LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQHV 239
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
.
gi 16128777 240 S 240
Cdd:PRK11607 254 N 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-226 |
5.33e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 162.52 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQ--QFYLFPH 91
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 lTALENVMFGPlRVRGANKEEAEKLARELLAKVGLA--ERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:PRK13637 100 -TIEKDIAFGP-INLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 170 ELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PRK13637 178 KGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-221 |
6.62e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 161.72 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQ----QFYlf 89
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD--VRRQVGMVFQnpdnQFV-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 pHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:PRK13635 96 -GATVQDDVAFG-LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 170 ELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKvASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK13635 174 RGRREVLETVRQLKEQKGITVLsITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-210 |
1.48e-48 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 158.80 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCIN-KLEEI--TSGDLIVDGLKVNDPKVDERLIrq 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALPAEQRRI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 eaGMVFQQFYLFPHLTALENVMFG-PLRVRGANKEEAeklARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:COG4136 79 --GILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRAR---VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 157 MMLFDEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEkVASRLIFID 210
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEEDAP-AAGRVLDLG 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-238 |
2.18e-48 |
|
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: 167.25 E-value: 2.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD--LDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFG-PlrvrGANKEEaeklARELLAKVGLAERAHHYP-----------SELSGGQQQRVAI 147
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLArP----DATDEE----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEvlkVMQDLAE--EGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQA---LLADLLEalAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLA 558
|
250
....*....|...
gi 16128777 226 NPPsqRLQEFLQH 238
Cdd:COG4987 559 QNG--RYRQLYQR 569
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-224 |
2.57e-48 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 158.98 E-value: 2.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 21 DLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALENVMF 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV----SMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 101 G--P-LRVRGANKEEAEKLARellaKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK 177
Cdd:PRK10771 95 GlnPgLKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128777 178 VMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK10771 171 LVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
2.92e-48 |
|
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: 158.30 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGM 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---DVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENV-MFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:cd03265 78 VFQDLSVDDELTGWENLyIHA--RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 161 DEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
5.26e-48 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 159.02 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRcinKLEEITSGDLIVDG---LKVNDPKVDERLI-- 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSAGShieLLGRTVQREGRLArd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 ----RQEAGMVFQQFYLFPHLTALENVMFGPLR--------VRGANKEEAEKlARELLAKVGLAERAHHYPSELSGGQQQ 143
Cdd:PRK09984 81 irksRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-223 |
5.85e-48 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 158.74 E-value: 5.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErLIRQEAg 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-LARRRA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 mVFQQFYL--FPhLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAH-HYPsELSGGQQQRVAIARALA----- 152
Cdd:COG4559 79 -VLPQHSSlaFP-FTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHLAGrSYQ-TLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 153 --VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP-QVL 223
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPeEVL 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-226 |
6.41e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 159.48 E-value: 6.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQ------VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERL 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL---DTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 --IRQEAGMVFQQfylfP--HLTAL---ENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAI 147
Cdd:PRK13633 81 wdIRNKAGMVFQN----PdnQIVATiveEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHeigFAEKV--ASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITH---YMEEAveADRIIVMDSGKVVMEGTPKEIF 232
|
..
gi 16128777 225 KN 226
Cdd:PRK13633 233 KE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
6.52e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 158.47 E-value: 6.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLIR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRG--ANKEEAEKLARELLAKVGLAE----RAHHYPSELSGGQQQRVAIARA 150
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGlvKSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQ 230
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
....*.
gi 16128777 231 RLQEFL 236
Cdd:PRK14267 243 LTEKYV 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
8.47e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 159.42 E-value: 8.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKV 70
Cdd:PRK13634 3 ITFQKVEHRYQYktpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 71 derlIRQEAGMVFQ--QFYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERA-HHYPSELSGGQQQRVAI 147
Cdd:PRK13634 83 ----LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
.
gi 16128777 227 P 227
Cdd:PRK13634 237 P 237
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.04e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 159.48 E-value: 1.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT-----QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI----------------- 59
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 60 -VDGLKVNDPKVDE----RLIRQEAGMVFQ--QFYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAER-AH 131
Cdd:PRK13651 83 vLEKLVIQKTRFKKikkiKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 132 HYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....*
gi 16128777 212 GRIAEDGNPQVLIKN 226
Cdd:PRK13651 241 GKIIKDGDTYDILSD 255
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-218 |
1.06e-47 |
|
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: 157.24 E-value: 1.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDeRLIrqeagmVFQQFYLFPHLTALE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-RMV------VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 97 NVMFGPLRV-RGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP----EL 171
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128777 172 RHEVLKVMQdlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:TIGR01184 154 QEELMQIWE---EHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-223 |
1.50e-47 |
|
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: 159.09 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPkvdeRLIRQEAGMVFQQFY 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVvREP----RKVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 88 LFPHLTALEN-VMFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR01188 77 VDEDLTGRENlEMMG--RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.71e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 158.32 E-value: 1.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVS-KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA 79
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQ--FYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK13639 81 GIVFQNpdDQLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
5.15e-47 |
|
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: 154.68 E-value: 5.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI----GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGpLRVRGANKEEAEklarELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLL-ARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-221 |
8.49e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 156.44 E-value: 8.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKV--DERL 74
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQqfylFPHL-----TALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERA-HHYPSELSGGQQQRVAIA 148
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
1.19e-46 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 155.24 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-----LI 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELakrlaIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 RQEAGMVfqqfylfPHLTALENVMFGplRV---RGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:COG4604 81 RQENHIN-------SRLTVRELVAFG--RFpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 153 VKPKMMLFDEPTSALDpeLRHEV--LKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:COG4604 152 QDTDYVLLDEPLNNLD--MKHSVqmMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
2.09e-46 |
|
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: 161.85 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFpHLTALENVMFGplrVRGANKEEAEklarELLAKVGLAERAHHYP-----------SELSGGQQQRVAIAR 149
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG---RPDASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-227 |
4.00e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 153.92 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEI-----TSGDLIVDGLKVNdpKVDERLIR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGPLRVRGA-NKEEAEKLARELLAKVGLAE----RAHHYPSELSGGQQQRVAIARAL 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
5.20e-46 |
|
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: 151.81 E-value: 5.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQ-----F 86
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDpddqlF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 YLfphlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:TIGR01166 83 AA----DVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|...
gi 16128777 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFA 199
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-223 |
6.30e-46 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 153.39 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKV---NDPKVD---ERL 74
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGELSPDSGEVrlnGRPLADwspAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAgMVFQQFYL-FPhLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAH-HYPsELSGGQQQRVAIARALA 152
Cdd:PRK13548 75 ARRRA-VLPQHSSLsFP-FTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 153 ------VKPKMMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP-QVL 223
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPaEVL 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-227 |
7.73e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 154.22 E-value: 7.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-- 74
Cdd:PRK13641 3 IKFENVDYIYSPgtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQ--QFYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAER-AHHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
8.06e-46 |
|
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: 151.89 E-value: 8.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlIRQEA 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA---ARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-239 |
1.08e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 156.73 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPTQVLHNIDLN---------IAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL---KVNDPKVD 71
Cdd:PRK10070 22 FKYIEQGLSKEQILEKTGLSlgvkdaslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 72 ErLIRQEAGMVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:PRK10070 102 E-VRRKKIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQ 230
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
|
....*....
gi 16128777 231 RLQEFLQHV 239
Cdd:PRK10070 260 YVRTFFRGV 268
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.46e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 152.84 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP--TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQE 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE--IRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQ----QFYlfpHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK13632 85 IGIIFQnpdnQFI---GATVEDDIAFG-LENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
5.07e-45 |
|
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: 149.65 E-value: 5.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIA-WLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
2.41e-44 |
|
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: 149.08 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSG-DLIVDGLKVNDPKVDErlIRQEA 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE--LRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMV--FQQFYLFPHLTALENVM---FGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG1119 81 GLVspALQLRFPRDETVLDVVLsgfFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTH---EI--GFaekvaSRLIFIDKGRIAEDG 218
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAG 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-227 |
4.00e-44 |
|
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: 155.23 E-value: 4.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVNDPKVDE-RLIRQEAGMVFQQFY 87
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlRPLRRRMQVVFQDPF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 88 --LFPHLTALENVMFGpLRV--RGANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:COG4172 373 gsLSPRMTVGQIIAEG-LRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 163 PTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
5.15e-44 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 148.78 E-value: 5.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEI-----TSGDLIVDGLKVNDPKVDERLIR 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHlTALENVMFGPlRVRGANKEEAEKLAREL------------LAKVGLAerahhypseLSGGQQQR 144
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGA-RINGYKGDMDELVERSLrqaalwdevkdkLKQSGLS---------LSGGQQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFID---------KGRIA 215
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLV 238
|
250 260
....*....|....*....|.
gi 16128777 216 EDGNPQVLIKNPPSQRLQEFL 236
Cdd:PRK14243 239 EFDRTEKIFNSPQQQATRDYV 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-194 |
6.09e-44 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 154.03 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKvderlirqE 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVriRSPR--------D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 A-----GMVFQQFYLFPHLTALENVMFG--PLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:COG3845 77 AialgiGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
1.04e-43 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 146.94 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSK-HFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLIRQE 78
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
1.96e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 147.12 E-value: 1.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPK----VDERLIRQEAGMVFQQFYLFPH 91
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFgPLRVRG-ANKEEAEKLARELLAKVGLAERAHHY----PSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PRK14246 105 LSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 167 LDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.09e-43 |
|
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: 153.30 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDGLKVNdpKVDE 72
Cdd:COG4172 6 LLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL--GLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 73 RLIRQ----EAGMVFQQfylfPhLTAL------ENVMFGPLRV-RGANKEEAEKLARELLAKVGLAE---RAHHYPSELS 138
Cdd:COG4172 84 RELRRirgnRIAMIFQE----P-MTSLnplhtiGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 139 GGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250
....*....|
gi 16128777 218 GNPQVLIKNP 227
Cdd:COG4172 239 GPTAELFAAP 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
5.97e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 146.79 E-value: 5.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-------ER 73
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 74 lirqeaGmvfqqfyLFPHLTALENVM-FGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:COG4152 81 ------G-------LYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGN 219
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGS 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-215 |
7.28e-43 |
|
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: 144.23 E-value: 7.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 21 DLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGMVFQQFYLFPHLTALENVMF 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPV----SMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 101 G---PLRVRGANKEEAEKLAREllakVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK 177
Cdd:TIGR01277 94 GlhpGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128777 178 VMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:TIGR01277 170 LVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-214 |
1.07e-42 |
|
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: 143.55 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVS-KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndPKVDERLIRQEAGMVF 83
Cdd:cd03226 3 ENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-----KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 Q--QFYLFphltalENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03226 78 QdvDYQLF------TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 |
1.15e-42 |
|
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: 144.30 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEA 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS--LRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFGplrVRGANKEEAEKLARELLA-------------KVGlaERAhhypSELSGGQQQRVA 146
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYG---RPGATREEVEEAARAANAhefimelpegydtVIG--ERG----VKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-227 |
1.27e-42 |
|
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: 147.57 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 6 NVSKHFGPTQVlhNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP--KVDERLIRQEAGMVF 83
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkGIFLPPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 QQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERahhYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 164 TSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-240 |
3.63e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 145.76 E-value: 3.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 8 SKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL------------- 74
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 -IRQEAGMVFQ--QFYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLA----ERAhhyPSELSGGQQQRVAI 147
Cdd:PRK13631 113 eLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDdsylERS---PFGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNp 227
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTD- 266
|
250
....*....|...
gi 16128777 228 psqrlQEFLQHVS 240
Cdd:PRK13631 267 -----QHIINSTS 274
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
6.18e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 143.72 E-value: 6.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQ---VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQ 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD--IRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQ----QFYlfpHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:PRK13650 82 KIGMVFQnpdnQFV---GATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIgfaEKVA--SRLIFIDKGRIAEDGNPQVL 223
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDL---DEVAlsDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
1.29e-41 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 141.45 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQ----VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER--L 74
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARakL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDkGRIAED 217
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-227 |
1.51e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.02 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKL---EEITSGDLIVDGLKVNDPKVDErlIR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWD--IR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQ----QFYlfpHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:PRK13640 84 EKVGIVFQnpdnQFV---GATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
2.03e-41 |
|
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: 141.21 E-value: 2.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT-QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFpHLTALENVMFGPLrvrGANKEEAEKLAR------ELLA-------KVGlaERAhhypSELSGGQQQRVAI 147
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRP---DATDEEVIEAAKaaqihdKIMRfpdgydtIVG--ERG----LKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTH---EIGFAEKVasrlIFIDKGRIAEDGNPQVLI 224
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHrlsTIVNADKI----IVLKDGRIVERGTHEELL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-220 |
2.18e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 142.95 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL- 74
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 -IRQEAGMVFQ--QFYLFPHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARA 150
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP 220
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-218 |
2.70e-41 |
|
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: 140.74 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAGMV 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER-ARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGpLRVRGANKEEAEKLARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-LAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 163 PTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
6.91e-41 |
|
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: 139.93 E-value: 6.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--HDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFGPLRVRGANKEEAEKLA------RELLAKVG--LAERAhhypSELSGGQQQRVAIARAL 151
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAgahdfiSELPEGYDtiVGEQG----AGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
1.95e-40 |
|
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: 137.80 E-value: 1.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderLIRQEAGM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLA-QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
2.34e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 139.74 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP-KVDErlIRQE 78
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQG--IRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYL-FPHLTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFGPENL-CLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRL 232
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
1.29e-39 |
|
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: 136.18 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR--QLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFGPLRVRGANKEEAEKLArellakvGLAERAHHYP-----------SELSGGQQQRVAIA 148
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLGAPLADDERILRAAELA-------GVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDG 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
1.42e-39 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 136.75 E-value: 1.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----------------------GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 59 IVDGlkvndpkvdeR---LIrqEAGMVFQqfylfPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAH---- 131
Cdd:COG1134 84 EVNG----------RvsaLL--ELGAGFH-----PELTGRENIYLN-GRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 132 HYPSelsgGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
Cdd:COG1134 146 TYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
250
....*....|....
gi 16128777 212 GRIAEDGNPQVLIK 225
Cdd:COG1134 222 GRLVMDGDPEEVIA 235
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-225 |
2.04e-39 |
|
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: 144.24 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVderlIRQ 77
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPAD----LRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFpHLTALENVMFGplrVRGANKEEAEKLARellaKVGLAERAHHYPS-----------ELSGGQQQRVA 146
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG---APYADDEEILRAAE----LAGVTEFVRRHPDgldmqigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIK 225
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLE 688
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
2.17e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 137.17 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQ----QFYlfpHLTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK13647 83 LVFQdpddQVF---SSTVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-227 |
3.33e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.17 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDP-KVDERLIRQEAGMVFQQFY--LFPH 91
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQKLLRQKIQIVFQNPYgsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTaLENVMFGPLRVRG--ANKEEAEKlARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK11308 109 KK-VGQILEEPLLINTslSAAERREK-ALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
4.75e-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: 132.94 E-value: 4.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERL-Irqe 78
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfaSPRDARRAgI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 aGMVFQqfylfphltalenvmfgplrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMM 158
Cdd:cd03216 78 -AMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
6.61e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 135.55 E-value: 6.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITS-----GDLIVDGLKVNDPKVDERLIR 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPhLTALENVMFGPLRVRGANKEEAEKLARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALA 152
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDK-----GRIAEDGNPQVLIKN 226
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNS 246
|
250
....*....|
gi 16128777 227 PPSQRLQEFL 236
Cdd:PRK14258 247 PHDSRTREYV 256
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-227 |
7.78e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 135.35 E-value: 7.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF---------GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKV 70
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 71 DERLIRqeagMVFQQFY--LFPHLTA---LEnvmfGPLRVRGA-NKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQ 143
Cdd:COG4167 85 RCKHIR----MIFQDPNtsLNPRLNIgqiLE----EPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQV 222
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
....*
gi 16128777 223 LIKNP 227
Cdd:COG4167 237 VFANP 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
1.15e-38 |
|
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: 133.65 E-value: 1.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIR 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVM-FGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEyFA--GLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
2.32e-38 |
|
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: 133.12 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT-QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:cd03254 3 IEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD--ISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHlTALENVMFGPLRvrgANKEEAEKLARELLAK---VGLAERAHHYPSE----LSGGQQQRVAIARALAV 153
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPN---ATDEEVIEAAKEAGAHdfiMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHE---IGFAEKVasrlIFIDKGRIAEDGNPQVLIK 225
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRlstIKNADKI----LVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-225 |
3.27e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 134.52 E-value: 3.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE--RL 74
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQqfylFPHLTALEN-----VMFGPlRVRGANKEEAEKLARELLAKVGLAERA-HHYPSELSGGQQQRVAIA 148
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
3.94e-38 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 132.70 E-value: 3.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdERLIRQEAG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-AKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-226 |
8.12e-38 |
|
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: 131.89 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFgPT----QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77
Cdd:cd03249 1 IEFKNVSFRY-PSrpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD--LNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPhLTALENVMFGplrVRGANKEEAEKLARELLA-------------KVGlaERAhhypSELSGGQQQR 144
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRYG---KPDATDEEVEEAAKKANIhdfimslpdgydtLVG--ERG----SQLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
..
gi 16128777 225 KN 226
Cdd:cd03249 226 AQ 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-227 |
2.35e-37 |
|
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: 130.74 E-value: 2.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 6 NVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirQEAGMVF-- 83
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKR---ARLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 QQFYLFPHLTALENVMfGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:cd03218 82 QEASIFRKLTVEENIL-AVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 |
4.78e-37 |
|
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: 136.09 E-value: 4.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEI--TSGDLI-------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 60 -------------VDGLKVNDPkVDERLIRQEAGMVFQQFYLFPHLTALENVMfGPLRVRGANKEEAEKLARELLAKVGL 126
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDK-LRRRIRKRIAIMLQRTFALYGDDTVLDNVL-EALEEIGYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 127 AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE---LRHEVLKvmQDLAEEGMTMVIVTHEIGFAEKVA 203
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQtakLVHNALE--EAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|.
gi 16128777 204 SRLIFIDKGRIAEDGNPQVLI 224
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVV 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-217 |
5.61e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.58 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHF---------GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERL 74
Cdd:PRK10419 7 SGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 IRQEAGMVFQQFY--LFPHLTALEnVMFGPLR-VRGANKEEAEKLARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARA 150
Cdd:PRK10419 87 FRRDIQMVFQDSIsaVNPRKTVRE-IIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-218 |
1.00e-36 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 128.05 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCIN--KLEEITSGDLivdglKVNDPKVDERLIRQEAGMVFQQFYLFPH 91
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEV-----LINGRPLDKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFGpLRVRGankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:cd03213 97 LTVRETLMFA-AKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128777 172 RHEVLKVMQDLAEEGMTMVIVTH----EIgfaEKVASRLIFIDKGRIAEDG 218
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHqpssEI---FELFDKLLLLSQGRVIYFG 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
2.81e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.66 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP-----TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-- 73
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 74 LIrqeaGMVFQQFYL--FPHLTALENVMFGPLR------VRGANKEEAEkLARELLAKV--GLAERAHHYPSELSGGQQQ 143
Cdd:COG1101 81 YI----GRVFQDPMMgtAPSMTIEENLALAYRRgkrrglRRGLTKKRRE-LFRELLATLglGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-240 |
5.38e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 128.29 E-value: 5.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 6 NVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSG-----DLIVDGLKVNDPKvDERLIRQEAG 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPhLTALENVMFGPLRVRGANKEEAEKLARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFL 236
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
....
gi 16128777 237 QHVS 240
Cdd:PRK14271 263 AGLS 266
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
7.09e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 129.57 E-value: 7.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQEAGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA---RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALEN-VMFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK13536 119 VPQFDNLDLEFTVRENlLVFG--RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-218 |
1.04e-35 |
|
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: 132.92 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT--QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEA 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS--LRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHlTALENVMFGplRVRGANKEEAEKLARELLAK-------VGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYG--RTEQADRAEIERALAAAYAQdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDG 218
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLSTIEK-ADRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-226 |
1.12e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 127.82 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDE-RLIRQEAGMVFQ--QFYLF 89
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEvKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 PHlTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAER-AHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK13645 105 QE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 169 PELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-224 |
3.40e-35 |
|
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: 132.17 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL--AIADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHlTALENVMFG-PlrvrGANKEEAEKLARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARAL 151
Cdd:TIGR01846 534 GVVLQENVLFSR-SIRDNIALCnP----GAPFEHVIHAAKLAGAHDFISELPQGYNTEvgekganLSGGQRQRIAIARAL 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREIC-RGRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-236 |
3.46e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 126.03 E-value: 3.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVD-ERL--IRQ 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG--ENIPAMSrSRLytVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPHLTALENVMFgPLRvrgankeEAEKLAREL--------LAKVGLAERAHHYPSELSGGQQQRVAIAR 149
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAY-PLR-------EHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNpP 228
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN-P 235
|
....*...
gi 16128777 229 SQRLQEFL 236
Cdd:PRK11831 236 DPRVRQFL 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
5.53e-35 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 128.42 E-value: 5.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFG--PLRVRGANKEEAEKLA-RELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 158 MLFDEPTSALDpeLRHEV--LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK09536 161 LLLDEPTASLD--INHQVrtLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
8.56e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 124.37 E-value: 8.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR---- 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 --QEAGmVFQQfylfphLTALENVMfGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:COG1137 83 lpQEAS-IFRK------LTVEDNIL-AVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.71e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.30 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKvDERLIRQEAGM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENVM-FGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLvFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
2.03e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.64 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKVndpkvderlirqeaGMV 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI--------------GYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVM--FGPLRVRGANKEEAEKL-----------------------------ARELLAKVGLAERAH 131
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgDAELRALEAELEELEAKlaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 132 HYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE----LRHEvlkvmqdLAEEGMTMVIVTHEIGFAEKVASRL 206
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLEsiewLEEF-------LKNYPGTVLVVSHDRYFLDRVATRI 219
|
....*...
gi 16128777 207 IFIDKGRI 214
Cdd:COG0488 220 LELDRGKL 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
2.52e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.19 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQ--FYLFPhLTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-227 |
3.87e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.07 E-value: 3.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFgPT----QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
Cdd:TIGR00958 479 IEFQDVSFSY-PNrpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPHlTALENVMFGplrVRGANKEEAEKLARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARA 150
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQ---LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
6.99e-34 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.54 E-value: 6.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT--QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
Cdd:TIGR03797 452 IEVDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG--LDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHlTALENVMFG-PLRVrgankEEAEKLAREllakVGLAE--RA-----HHYPSE----LSGGQQQRVAI 147
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENIAGGaPLTL-----DEAWEAARM----AGLAEdiRAmpmgmHTVISEgggtLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQA---IVSESLERLKVTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELM 672
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
8.28e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.60 E-value: 8.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEA 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE--VRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQ----QFYlfpHLTALENVMFGPLRVrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:PRK13652 81 GLVFQnpddQIF---SPTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-215 |
1.25e-33 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 120.84 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI-NKLEE--ITSGDLIVDGLKVNDPKVderliRQEAGMVFQQFYLFPH 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGggTTSGQILFNGQPRKPDQF-----QKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFGP---LRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:cd03234 96 LTVRETLTYTAilrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIG---FaeKVASRLIFIDKGRIA 215
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.49e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.78 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQE 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK--LRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQ----QFYlfpHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:PRK13648 85 IGIVFQnpdnQFV---GSIVKYDVAFG-LENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-200 |
1.89e-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: 126.25 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD--ADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHlTALENVMFGPLRVRGANKEEAEKLA--RELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAglDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAE 200
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA 521
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-219 |
3.67e-33 |
|
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: 126.09 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT-QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:COG5265 358 VRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD--VTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFpHLTALENVMFGplRVrGANKEEAEKLARelLA---------------KVGlaERAhhypSELSGGQQQRV 145
Cdd:COG5265 436 IVPQDTVLF-NDTIAYNIAYG--RP-DASEEEVEAAAR--AAqihdfieslpdgydtRVG--ERG----LKLSGGEKQRV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI------VTHeigfaekvASRLIFIDKGRIAEDGN 219
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIahrlstIVD--------ADEILVLEAGRIVERGT 575
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-227 |
4.03e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.12 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG----------PTQVLHNID---LNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG---LK 64
Cdd:PRK15079 8 LLEVADLKVHFDikdgkqwfwqPPKTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 65 VNDpkVDERLIRQEAGMVFQQ--FYLFPHLTALEnVMFGPLRVRGAN--KEEAEKLARELLAKVGLAERA-HHYPSELSG 139
Cdd:PRK15079 88 MKD--DEWRAVRSDIQMIFQDplASLNPRMTIGE-IIAEPLRTYHPKlsRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 140 GQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
|
....*....
gi 16128777 219 NPQVLIKNP 227
Cdd:PRK15079 245 TYDEVYHNP 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-194 |
5.24e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.11 E-value: 5.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 11 FGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLirqeaGMVFQQFYL-- 88
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------GARV-----AYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 89 -FPhLTALENVMFGPLRVRGANKE---EAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:NF040873 69 sLP-LTVRDLVAMGRWARRGLWRRltrDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 16128777 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
5.87e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 119.73 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKvDERLIRQEAg 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS-SRQLARRLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 mVFQQFYLFPH-LTALENVMFG--P-LRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK11231 80 -LLPQHHLTPEgITVRELVAYGrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
5.91e-33 |
|
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: 117.32 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHlTALENVmfgplrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
4.82e-32 |
|
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: 116.48 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF----------------------GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 60 VDGlkvndpKVDERLirqEAGMVFQqfylfPHLTALENVMFGpLRVRGANKEEAEKLARELLAKVGLaERAHHYP-SELS 138
Cdd:cd03220 81 VRG------RVSSLL---GLGGGFN-----PELTGRENIYLN-GRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLPvKTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 139 GGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-227 |
5.28e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 123.04 E-value: 5.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 19 NIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDERL--IRQEAGMVFQQFY--LFPHLTA 94
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI-DTLSPGKLqaLRRDIQFIFQDPYasLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 95 LENVMfGPLRVRG-ANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:PRK10261 421 GDSIM-EPLRVHGlLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 173 HEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK10261 500 GQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
8.18e-32 |
|
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: 121.70 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ-VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFpHLTALENVMFGplrvrgaNKEEAEKLARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIAR 149
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTH 194
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.59e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.55 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-DGLKVndpkvderlirqea 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKI-------------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQ-QFYLFPHLTALENvmfgplrVRGANKEEAEKLARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDE-------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 158 MLFDEPTSALDPELRhEVLKVMqdLAE-EGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE-DGN 219
Cdd:COG0488 454 LLLDEPTNHLDIETL-EALEEA--LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVREyPGG 513
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-225 |
1.91e-31 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 121.31 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDG-LKVNDPKVDERLIRQEAGMVFQQFYLFPHLT 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 94 ALENVMFGPlRVR-GANKEEAEKLAR--ELLAKVGLAERAH------HYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:TIGR00955 116 VREHLMFQA-HLRmPRRVTKKEKRERvdEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTH----EIGFaekVASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpssELFE---LFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-221 |
2.51e-31 |
|
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: 120.29 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF-----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV----DGLKVNDPKVD 71
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 72 ER-LIRQEAGMVFQQFYLFPHLTALENVM----------FGPLRVRGANKEEA--EKLARELLAKvglaerahhYPSELS 138
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNLTeaiglelpdeLARMKAVITLKMVGfdEEKAEEILDK---------YPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 139 GGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....
gi 16128777 218 GNPQ 221
Cdd:TIGR03269 510 GDPE 513
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
3.30e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 120.31 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVskHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD--YSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPHlTALENVMFGplrvrganKEEA--EKLArELLAKVGLAERAHHYPS----------ELSGGQQQRV 145
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLA--------APNAsdEALI-EVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIK 225
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA 562
|
250
....*....|....
gi 16128777 226 NPPsqRLQEFLQHV 239
Cdd:PRK11160 563 QQG--RYYQLKQRL 574
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-239 |
4.48e-31 |
|
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: 114.03 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdeRLIRQEAGM 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT------RKDLHKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VFQQFYLFPHLTALENvmfgpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR03740 75 LIESPPLYENLTAREN-----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGnpqvliKNPPSQRLQEFLQHV 239
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG------KINKSENLEKLFVEV 221
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-227 |
2.48e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 114.84 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFG----PTQVLHNIDLNIAQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDG--LKVNDPKV 70
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGqdLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 71 DERLIRQEAGMVFQQ--FYLFPHLTALENVMfGPLRV-RGANKEEAEKLARELLAKVGL---AERAHHYPSELSGGQQQR 144
Cdd:PRK11022 83 RRNLVGAEVAMIFQDpmTSLNPCYTVGFQIM-EAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
....
gi 16128777 224 IKNP 227
Cdd:PRK11022 242 FRAP 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-214 |
3.60e-30 |
|
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: 111.79 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF---GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQE 78
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHlTALENVMFGplrVRGANKEEAEKLARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIARAL 151
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRI 214
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-202 |
2.28e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI--YRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHlTALENVMFgPLRVRGANKEEAeKLARElLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIF-PWQIRNQQPDPA-IFLDD-LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTH---EIGFAEKV 202
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHdkdEINHADKV 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-194 |
2.44e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.90 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIR-QEAGMVF--QQFYLfPHL 92
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG----------------RIARpAGARVLFlpQRPYL-PLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TaLENVMFGPLRVRGANKEEAeklaRELLAKVGLAERAHHY------PSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:COG4178 441 T-LREALLYPATAEAFSDAEL----REALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180
....*....|....*....|....*...
gi 16128777 167 LDPELRHEVLKVMQDlAEEGMTMVIVTH 194
Cdd:COG4178 516 LDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-224 |
3.19e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 11 FGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFP 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE--VARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 91 HLTALENVMFG-----PLRVRGaNKEEAEKLARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK10253 95 DITVQELVARGryphqPLFTRW-RKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 166 ALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-224 |
3.25e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.73 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdeRLIRQEA 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL--ASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENVMFGplRVRGANKEEAEKLAR-----ELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYA--RTEQYSREQIEEAARmayamDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-223 |
4.19e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.02 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV---DGLKVNDPKVDE----RLIRQ 77
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEaerrRLLRT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFY--LFPHLTALENV----MFGPLRVRGANKEEAEklarELLAKVGL-AERAHHYPSELSGGQQQRVAIARA 150
Cdd:PRK11701 90 EWGFVHQHPRdgLRMQVSAGGNIgerlMAVGARHYGDIRATAG----DWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG-NPQVL 223
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGlTDQVL 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-227 |
4.22e-29 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 109.69 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpKVDERLIRQeaG 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIARM--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MV--FQQFYLFPHLTALENVMF------------GPLRVRGANKEEAEKLAREL--LAKVGLAERAHHYPSELSGGQQQR 144
Cdd:PRK11300 82 VVrtFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
....
gi 16128777 224 IKNP 227
Cdd:PRK11300 242 RNNP 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
7.61e-29 |
|
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: 107.01 E-value: 7.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP--TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvdERLIRQEA 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL---EKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFpHLTALENvmfgplrvrgankeeaeklarellakvgLAERahhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNN----------------------------LGRR-------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDG 218
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-237 |
3.07e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 111.72 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKST----LLRCINkleeiTSGDLIVDGLKVNDPKVDERL-IRQEAGMVFQQF 86
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLpVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 Y--LFPHLTALENVMFGpLRV--RGANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:PRK15134 372 NssLNPRLNVLQIIEEG-LRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRLQEFLQ 237
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
3.36e-28 |
|
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: 112.14 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFG-PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHlTALENVMFGplrvrgaNKEEAEKlaRELLAKVGLAE--------------RAHHYPSELSGGQQQRVA 146
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLG-------AKENVSQ--DEIWAACEIAEikddienmplgyqtELSEEGSSISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 147 IARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIK 225
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
6-223 |
5.30e-28 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 106.84 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 6 NVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL--------IVDGLKVNDPKvDERLIRQ 77
Cdd:TIGR02323 8 GLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaELELYQLSEAE-RRRLMRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFY--LFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVK 154
Cdd:TIGR02323 87 EWGFVHQNPRdgLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 155 PKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG-NPQVL 223
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGlTDQVL 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-220 |
6.38e-28 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 106.30 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLKVNDPKVDERlirQEAG 80
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDER---ARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MvfqqFYLFPH-------------LTALENVMFGPLRVRgankeEAEKLARELLAKVGLAER-AHHYPSE-LSGGQQQRV 145
Cdd:COG0396 79 I----FLAFQYpveipgvsvsnflRTALNARRGEELSAR-----EFLKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPE-LRHeVLKVMQDLAEEGMTMVIVTH------EIgfaekVASRLIFIDKGRIAEDG 218
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDaLRI-VAEGVNKLRSPDRGILIITHyqrildYI-----KPDFVHVLVDGRIVKSG 223
|
..
gi 16128777 219 NP 220
Cdd:COG0396 224 GK 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-223 |
8.14e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 8.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQ-FYLFPHLTAL 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN--LRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFGpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEV 175
Cdd:PRK13642 101 DDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128777 176 LKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVL 223
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-194 |
1.82e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 104.19 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER---LIRQ 77
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchyLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAgmvfqqfyLFPHLTALENVMFGPlRVRGANKEEAEklarELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK13539 82 NA--------MKPALTVAENLEFWA-AFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-214 |
1.98e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 103.28 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVF-----QQFYLFP 90
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI---RAGIAYvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 91 HLTALENVMFGPLrvrgankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPE 170
Cdd:cd03215 92 DLSVAENIALSSL---------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128777 171 LRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
2.25e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.10 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA- 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAAQLGi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHLTALENVMFGPLRVR---GANK---EEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-232 |
2.72e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.59 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAGMVFQ 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR-ARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 85 QFYLFPHLTALENVMfGPLRVR-GANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:PRK10895 86 EASIFRRLSVYDNLM-AVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNPPSQRL 232
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
6.43e-27 |
|
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: 103.34 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPHlTALENVmfGPLrvrgaNKEEAEKLaRELLAKVGLAERAHHYP-----------SELSGGQQQRVAIA 148
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNL--DPF-----GEYSDEEL-WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 149 RALAVKPKMMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIgfaEKVAS--RLIFIDKGRIAEDGNP 220
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRL---DTIIDsdRILVLDKGRVVEFDSP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-215 |
8.70e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.41 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVF----- 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAI---RAGIAYvpedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 QQFYLFPHLTALENVMFGPLRVRGA----NKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:COG1129 337 KGEGLVLDLSIRENITLASLDRLSRggllDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-226 |
1.01e-26 |
|
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: 108.18 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPT--QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEAGMV 82
Cdd:TIGR01257 932 KNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYA-QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 163 PTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPqVLIKN 226
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP-LFLKN 1149
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
4.35e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.81 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF-GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTAlENvmfgpLRVRGANKEEAEKL-------ARELLAK--VGLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:PRK13657 413 VVFQDAGLFNRSIE-DN-----IRVGRPDATDEEMRaaaeraqAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 152 AVKPKMMLFDEPTSALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELV 557
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-227 |
6.34e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.79 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF---------GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK 69
Cdd:PRK15112 4 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 70 VDERLIRqeagMVFQ--QFYLFPHlTALENVMFGPLRVRGA-NKEEAEKLARELLAKVGL-AERAHHYPSELSGGQQQRV 145
Cdd:PRK15112 84 YRSQRIR----MIFQdpSTSLNPR-QRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
...
gi 16128777 225 KNP 227
Cdd:PRK15112 239 ASP 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-227 |
6.37e-26 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 101.79 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFPHLTAL 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFGPLRVRGA----NKEEAEKLaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:PRK10575 104 ELVAIGRYPWHGAlgrfGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK10575 183 QVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
6.43e-26 |
|
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: 98.29 E-value: 6.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvndpkvderlirqeagm 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 vfqqfylfphltalENVMFGplrvrgankeeaeklarellakvglaerahhYPSELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:cd03221 61 --------------STVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128777 162 EPTSALDPELRhEVLKVMqdLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:cd03221 96 EPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-227 |
6.73e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 6.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKS-TLLRCINKLE----EITSGDLIVDGLKVndPKVDERLIRQEAG----MVFQQ 85
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPsppvVYPSGDIRFHGESL--LHASEQTLRGVRGnkiaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 86 --FYLFPhLTALENVMFGPLRV-RGANKEEAEKLARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKMML 159
Cdd:PRK15134 101 pmVSLNP-LHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-214 |
6.75e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.42 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFkNVSKHFGPTQVLHNIDLNiAQGeVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-------LKVNDPkVDER 73
Cdd:PRK11144 1 MLEL-NFKQQLGDLCLTVNLTLP-AQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLP-PEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 74 LIrqeaGMVFQQFYLFPHLTALENVMFGplrVRGANKEEAEKLArELLAKVGLAERahhYPSELSGGQQQRVAIARALAV 153
Cdd:PRK11144 77 RI----GYVFQDARLFPHYKVRGNLRYG---MAKSMVAQFDKIV-ALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 154 KPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-213 |
1.88e-25 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 103.72 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITS--GDLIVDG--LKVNDPKVDERL-- 74
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevCRFKDIRDSEALgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 --IRQEAGMVfqqfylfPHLTALENVMFGPLRVRGA--NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARA 150
Cdd:NF040905 81 viIHQELALI-------PYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 151 LAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-212 |
2.69e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 98.88 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 7 VSKHFGPTQ------VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDgLKVNDPKVDERLIRqeag 80
Cdd:COG2401 30 VLEAFGVELrvveryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFGREASLID---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 mvfqqfylfpHLTALENVmfgplrvrgankeeaeKLARELLAKVGLAErAHHY---PSELSGGQQQRVAIARALAVKPKM 157
Cdd:COG2401 105 ----------AIGRKGDF----------------KDAVELLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVA-SRLIFIDKG 212
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
2.81e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.09 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCinkLEEIT-----SGDLIVDG--LKVNDPKVDER 73
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV---LSGVYphgtyEGEIIFEGeeLQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 74 lirqeAGMV--FQQFYLFPHLTALENVMFGPLRVRGA--NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
Cdd:PRK13549 82 -----AGIAiiHQELALVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 150 ALAVKPKMMLFDEPTSAL-DPELRHeVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:PRK13549 157 ALNKQARLLILDEPTASLtESETAV-LLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-223 |
2.89e-25 |
|
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: 98.37 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLE--EITSGDLIVDGLKVNDPKVDERlIRQEAGMVFQQFYLFPHL 92
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEER-ARLGIFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TaleNVMFgplrVRGANkeeaeklarellakVGlaerahhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:cd03217 93 K---NADF----LRYVN--------------EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128777 173 HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFI-DKGRIAEDGNPQVL 223
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVHVlYDGRIVKSGDKELA 192
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
4.09e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 97.93 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVS-----KHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkLEEI--TSGDLIVDGlkvndpKVderl 74
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELekLSGSVSVPG------SI---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 75 irqeaGMVFQQFYLFPhLTALENVMFG-PLrvrgaNKEEAEKLAR--------ELLAK-----VGlaERAhhypSELSGG 140
Cdd:cd03250 69 -----AYVSQEPWIQN-GTIRENILFGkPF-----DEERYEKVIKacalepdlEILPDgdlteIG--EKG----INLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 141 QQQRVAIARALAVKPKMMLFDEPTSALDPEL-RHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGR 213
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-218 |
6.39e-25 |
|
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: 102.43 E-value: 6.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPH 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK--QWDRETFGKHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 lTALENVM-FGplrvRGANKE---EAEKLA--RELLAKV------GLAERAhhypSELSGGQQQRVAIARALAVKPKMML 159
Cdd:TIGR01842 407 -TVAENIArFG----ENADPEkiiEAAKLAgvHELILRLpdgydtVIGPGG----ATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDG 218
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLG-CVDKILVLQDGRIARFG 535
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-223 |
1.06e-24 |
|
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: 101.75 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIrqeaGMVFQQFYLFPHlT 93
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadLSQWDREELGRHI----GYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 94 ALENV-MFGplrvrGANKE---EAEKLAR--ELLAK--------VGLAERAhhypseLSGGQQQRVAIARALAVKPKMML 159
Cdd:COG4618 422 IAENIaRFG-----DADPEkvvAAAKLAGvhEMILRlpdgydtrIGEGGAR------LSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNP-QVL 223
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRdEVL 554
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-194 |
1.11e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG-- 80
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGPLRVRGA--NKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-218 |
1.75e-24 |
|
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: 97.02 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvnDPKVDERLIRQEAGMVF-QQFYLFPHLTA 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 95 LENVMFGPlRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHE 174
Cdd:cd03267 113 IDSFYLLA-AIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128777 175 VLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:cd03267 192 IRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-220 |
1.78e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.16 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQ-----FYlf 89
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDpeqqiFY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 phlTALENVMFGPLRVRGANKEEAEKLARELLAKVGlAERAHHYPSE-LSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK13638 93 ---TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP 220
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-227 |
2.35e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 100.94 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFPHLTAl 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS--WRSRLAVVSQTPFLFSDTVA- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFG-PlrvrGANKEEAEKLARelLAKV--GLAERAHHYPSE-------LSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK10789 407 NNIALGrP----DATQQEIEHVAR--LASVhdDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 166 ALDPELRHEVLkvmQDLAE--EGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK10789 481 AVDGRTEHQIL---HNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-211 |
3.45e-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: 94.53 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvndpkvderlirqeag 80
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 mvfqqfylfpHLTALENVMFGPLR---VRGankeeaekLARELLAkvglaerahhYP--SELSGGQQQRVAIARALAVKP 155
Cdd:cd03223 59 ----------GMPEGEDLLFLPQRpylPLG--------TLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 156 KMMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFaEKVASRLIFIDK 211
Cdd:cd03223 111 KFVFLDEATSALDEESED---RLYQLLKELGITVISVGHRPSL-WKFHDRVLDLDG 162
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
5.80e-24 |
|
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: 99.51 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGLKVNDPKVDERlirQE 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDT---ER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVF--QQFYLFPHLTALENVMFG-PLRVRGANKEEAEKLAR--ELLAKVGLAERAHHYP-SELSGGQQQRVAIARALA 152
Cdd:TIGR02633 78 AGIVIihQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRakNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-194 |
1.97e-23 |
|
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: 93.58 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvdERLIRQEagmvfQQFYLF-- 89
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDEPHE-----NILYLGhl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 ----PHLTALENvmfgpLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:TIGR01189 82 pglkPELSALEN-----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 16128777 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-227 |
2.13e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 96.13 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKleeITSGDLIV--DGLKVND-------PKVDERLIRQEAGMV 82
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---ITKDNWHVtaDRFRWNGidllklsPRERRKIIGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQ--QFYLFPHLTA---LENVMFGPlRVRG---ANKEEAEKLARELLAKVGLaeRAHH-----YPSELSGGQQQRVAIAR 149
Cdd:COG4170 95 FQepSSCLDPSAKIgdqLIEAIPSW-TFKGkwwQRFKWRKKRAIELLHRVGI--KDHKdimnsYPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-227 |
3.99e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.56 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 21 DLN--IAQGEVVVIIGPSGSGKSTLLRCINKL---EEITSGDLIVDGLKV-NDPKVDERLIR-QEAGMVFQQ--FYLFPH 91
Cdd:PRK09473 34 DLNfsLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREIlNLPEKELNKLRaEQISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAE---RAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK09473 114 MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
5.56e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 5.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF----GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDE-- 72
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmlLRRRSRQVIEls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 73 -------RLIR-QEAGMVFQQ--FYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERA---HHYPSELSG 139
Cdd:PRK10261 92 eqsaaqmRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 140 GQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|.
gi 16128777 219 NPQVLIKNPPSQRLQEFLQHV 239
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAV 272
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-195 |
6.81e-23 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 96.87 E-value: 6.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKVNDPKVDERLIRQeAGMVFQQFYLFPHLTAL 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMF-GPLRV-RGANKEEAEKLARELLAKVGLAE-----RAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PLN03211 159 ETLVFcSLLRLpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180
....*....|....*....|....*..
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-216 |
1.04e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.19 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFG-PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED--YRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTalenvmfGPlrvrgANKEEAEKLARELLAKVGLAERAHHYPSE-----LSGGQQQRVAIARALAVKP 155
Cdd:PRK10522 401 AVFTDFHLFDQLL-------GP-----EGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 156 KMMLFDEPTSALDPELR----HEVLKVMQdlaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
Cdd:PRK10522 469 DILLLDEWAADQDPHFRrefyQVLLPLLQ---EMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-194 |
3.07e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.25 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 18 HNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERlirqeagmvFQQFYLF-------- 89
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR--RQRDE---------YHQDLLYlghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 PHLTALENVMFGpLRVRGANKEEAeklARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:PRK13538 87 TELTALENLRFY-QRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180
....*....|....*....|....*
gi 16128777 170 ELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:PRK13538 163 QGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-219 |
6.44e-22 |
|
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: 93.85 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPT-QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD-LIVDGLKVndpkvderlirqeaGMV 82
Cdd:TIGR03719 8 NRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEaRPQPGIKV--------------GYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGPLRVRGANKE-------------EAEKLARE---------------LLAKVGLAERAHHYP 134
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGVAEIKDALDRfneisakyaepdaDFDKLAAEqaelqeiidaadawdLDSQLEIAMDALRCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 135 ------SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIF 208
Cdd:TIGR03719 154 pwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILE 230
|
250
....*....|..
gi 16128777 209 IDKGR-IAEDGN 219
Cdd:TIGR03719 231 LDRGRgIPWEGN 242
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-220 |
8.47e-22 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 90.66 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKleEIT----------SGDLIVDG--LKVNDPKvdeRLIRQEAGMVF 83
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGepLAAIDAP---RLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 QQFYLFPhLTALENVMFGPL---RVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA-------- 152
Cdd:PRK13547 91 AAQPAFA-FSAREIVLLGRYphaRRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 153 -VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP 220
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-227 |
1.03e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 90.14 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 18 HNIDLNIAQGEVVVIIGPSGSGKStlLRCINKLE------EITSGDLIVDGLKVNDPKVDERLIRqeagmvfqqfylfph 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCALRGRKIA--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 lTALEN--VMFGPLR---------VRGANKEEAEKLARELLAKVGLAERA---HHYPSELSGGQQQRVAIARALAVKPKM 157
Cdd:PRK10418 83 -TIMQNprSAFNPLHtmhtharetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-227 |
1.15e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 92.99 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 14 TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLrciNKLEEITS--GDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpH 91
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFLPyqGSLKINGIELRE--LDPESWRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 92 LTALENVMFGplrvrgaNKEEAEKLARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK11174 437 GTLRDNVLLG-------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 161 DEPTSALDpelRHEVLKVMQDL--AEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIKNP 227
Cdd:PRK11174 510 DEPTASLD---AHSEQLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
1.26e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 89.01 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP--TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG--IDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPhltalenvmfGPLR--VRGANKEEAEKLARELLAKVGlaerahhyPSELSGGQQQRVAIARALAVKPKM 157
Cdd:cd03369 85 TIIPQDPTLFS----------GTIRsnLDPFDEYSDEEIYGALRVSEG--------GLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 158 MLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfaeKVA--SRLIFIDKGRIAEDGNP 220
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLR---TIIdyDKILVMDAGEVKEYDHP 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-218 |
1.58e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.42 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdeRLIRQEAG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA------RLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 -----MVFQQFYLFPHLTALENVMFGPlrvrgANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
Cdd:PRK15439 85 qlgiyLVPQEPLLFPNLSVKENILFGL-----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-196 |
6.57e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDerlirQE 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSS-----QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGM--VFQQFYLFPHLTALENVMFGPLRVRGANKEEAEKLARE---LLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
Cdd:PRK10762 79 AGIgiIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128777 154 KPKMMLFDEPTSAL-DPELRhEVLKVMQDLAEEGMTMVIVTHEI 196
Cdd:PRK10762 159 ESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHRL 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-223 |
1.21e-20 |
|
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: 90.24 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ-----VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIR 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREA--YR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTalenvmfgplrvrGANKEEAEKLARELLAKVGLAERAHHY-----PSELSGGQQQRVAIARAL 151
Cdd:COG4615 406 QLFSAVFSDFHLFDRLL-------------GLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 152 AVKPKMMLFDEPTSALDPELR----HEVLkvmQDLAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGNPQVL 223
Cdd:COG4615 473 LEDRPILVFDEWAADQDPEFRrvfyTELL---PELKARGKTVIAISHDDRYFD-LADRVLKMDYGKLVELTGPAAL 544
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
1.22e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.61 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFgPTQV----------------------LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL 58
Cdd:COG4586 1 IIEVENLSKTY-RVYEkepglkgalkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 59 IVDGLkvnDPKVDERLIRQEAGMVF---QQfyLFPHLTALENvmfgpLRVRGA----NKEEAEKLARELLAKVGLAE--- 128
Cdd:COG4586 80 RVLGY---VPFKRRKEFARRIGVVFgqrSQ--LWWDLPAIDS-----FRLLKAiyriPDAEYKKRLDELVELLDLGElld 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 129 ---RahhypsELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVAS 204
Cdd:COG4586 150 tpvR------QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCD 223
|
250
....*....|....*
gi 16128777 205 RLIFIDKGRIAEDGN 219
Cdd:COG4586 224 RVIVIDHGRIIYDGS 238
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-206 |
1.61e-20 |
|
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: 86.01 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerlIRQEAGMVFQQFYLFPHLTAL 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS---IARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFgplrVRGANKEEAeklARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDpelRHEV 175
Cdd:cd03231 92 ENLRF----WHADHSDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD---KAGV 161
|
170 180 190
....*....|....*....|....*....|....*
gi 16128777 176 LKVMQDLA---EEGMTMVIVTH-EIGFAEKVASRL 206
Cdd:cd03231 162 ARFAEAMAghcARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-218 |
2.13e-20 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 88.25 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTllrciNKLEEITSG-DLIVDGLKVNDPKVDERLIRQEAG 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHV*GpDAGRRPWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQ-QFYLFPHLTALENV-MFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:NF000106 89 *HRPvR*GRRESFSGRENLyMIG--R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-216 |
4.05e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNV-SKHFGPTQvlhNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGM 81
Cdd:PRK09700 267 EVRNVtSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI---SPRSPLDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 VF-----QQFYLFPHLTALENVMFGPL----RVRGA----NKEEAEKLA---RELLA-KVGLAERAhhyPSELSGGQQQR 144
Cdd:PRK09700 341 AYitesrRDNGFFPNFSIAQNMAISRSlkdgGYKGAmglfHEVDEQRTAenqRELLAlKCHSVNQN---ITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-197 |
4.80e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkvdeRLIRQEAGMVFQQF----YLFPHL 92
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------QALQKNLVAYVPQSeevdWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 taLENVM----FGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:PRK15056 97 --VEDVVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180
....*....|....*....|....*....
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIG 197
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-223 |
1.39e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.51 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVNDPKVDErLIRQEA----------GM-VFQq 85
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAE-LARHRAylsqqqsppfAMpVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 86 fYLFPHLTAlenvmfgplrvrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARA-LAVKP------KMM 158
Cdd:COG4138 89 -YLALHQPA------------GASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPtinpegQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 159 LFDEPTSALDpeLRHEV--LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNP-QVL 223
Cdd:COG4138 156 LLDEPMNSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETaEVM 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-239 |
1.62e-19 |
|
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: 84.00 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 23 NIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN----------DPKVDERLIRQEAGMVFQQFYlfphl 92
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikadyEGTVRDLLSSITKDFYTHPYF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 talENVMFGPLRVRGAnkeeaekLARELLakvglaerahhypsELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:cd03237 96 ---KTEIAKPLQIEQI-------LDREVP--------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 173 HEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDkGRIAEDGnpqvlIKNPPSQRLQ---EFLQHV 239
Cdd:cd03237 152 LMASKVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNG-----VANPPQSLRSgmnRFLKNL 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-226 |
2.23e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.95 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 8 SKHFGPTqvLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkLEEITSGDlivdglkvnDPKVDerlIRQEAGMVFQQFY 87
Cdd:PLN03232 626 SKTSKPT--LSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAE---------TSSVV---IRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 88 LFpHLTALENVMFG----PLRVRGANKEEAEKLARELLAKVGLAERAHHyPSELSGGQQQRVAIARALAVKPKMMLFDEP 163
Cdd:PLN03232 690 IF-NATVRENILFGsdfeSERYWRAIDVTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIKN 226
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-212 |
1.08e-18 |
|
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: 84.68 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 27 GEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvdeRLIRQEAGMVFQQFYLFPHLTALENVMFGP---- 102
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG----------KSILTNISDVHQNMGYCPQFDAIDDLLTGRehly 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 103 --LRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQ 180
Cdd:TIGR01257 2035 lyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190
....*....|....*....|....*....|..
gi 16128777 181 DLAEEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-196 |
1.74e-18 |
|
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: 83.68 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 26 QGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVD-GLKVNDPKVDErLIRQEAGMVfqqfyLFPHLTALEN------- 97
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALK-------ILSGELKPNlGDYDEEPSWDE-VLKRFRGTE-----LQDYFKKLANgeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 98 ----VMFGPLRVRGANKEEAEK-----LARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALD 168
Cdd:COG1245 165 kpqyVDLIPKVFKGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180
....*....|....*....|....*...
gi 16128777 169 PELRHEVLKVMQDLAEEGMTMVIVTHEI 196
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-225 |
2.35e-18 |
|
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: 83.84 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ--VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEA 79
Cdd:TIGR00957 1285 VEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD--LRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPhltalenvmfGPLRVR----GANKEEAEKLARELLAKVG----LAERAHHYPSE----LSGGQQQRVAI 147
Cdd:TIGR00957 1363 TIIPQDPVLFS----------GSLRMNldpfSQYSDEEVWWALELAHLKTfvsaLPDKLDHECAEggenLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 148 ARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIK 225
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-182 |
2.41e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvndpkvdERLIRQEAG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLtALENVMFgpLRVRGANKEEAEKLArelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PRK09544 71 YVPQKLYLDTTL-PLTVNRF--LRLRPGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128777 161 DEPTSALD-----------PELRHE----VLKVMQDL 182
Cdd:PRK09544 145 DEPTQGVDvngqvalydliDQLRREldcaVLMVSHDL 181
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-227 |
4.33e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 81.77 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSkhfGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKleeITSGDLIV--DGLKVND-------PKVDE 72
Cdd:PRK15093 11 IEFKTSD---GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG---VTKDNWRVtaDRMRFDDidllrlsPRERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 73 RLIRQEAGMVFQ--QFYLFPHLTALENVM--------FGPLRVRGANKEeaeKLARELLAKVGLAERA---HHYPSELSG 139
Cdd:PRK15093 85 KLVGHNVSMIFQepQSCLDPSERVGRQLMqnipgwtyKGRWWQRFGWRK---RRAIELLHRVGIKDHKdamRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 140 GQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
....*....
gi 16128777 219 NPQVLIKNP 227
Cdd:PRK15093 242 PSKELVTTP 250
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-195 |
1.28e-17 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 77.67 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEE--ITSGDLIVDGLKVNDPkvderlIRQEAGMVFQQFYLFPHL 92
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN------FQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TALENVMFGPLrVRGankeeaeklarellakvglaerahhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:cd03232 95 TVREALRFSAL-LRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|...
gi 16128777 173 HEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIHQ 167
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-234 |
1.44e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.32 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 8 SKHFGPTqvLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkLEEI--TSGDLIVdglkvndpkvderlIRQEAGMVFQQ 85
Cdd:PLN03130 626 SKAERPT--LSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELppRSDASVV--------------IRGTVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 86 FYLFpHLTALENVMFG-PLRVRGANKE-EAEKLAREL-------LAKVGlaERAhhypSELSGGQQQRVAIARALAVKPK 156
Cdd:PLN03130 688 SWIF-NATVRDNILFGsPFDPERYERAiDVTALQHDLdllpggdLTEIG--ERG----VNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 157 MMLFDEPTSALDPELRHEVL-KVMQDlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIKNPPS-QRLQE 234
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFdKCIKD-ELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGPLfQKLME 838
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-225 |
1.82e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 20 IDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVderLIRqeAGMVF-----QQFYLFPHL 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRD---AIR--AGIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TALENV------MFGPLRVRGANKEEAEkLARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTS 165
Cdd:PRK11288 347 SVADNInisarrHHLRAGCLINNRWEAE-NADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA-----EDGNPQVLIK 225
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALS 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-214 |
4.85e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.61 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 11 FGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINK---LEE---ITSGDLIVDGLKVNDPkvderliRQEAGMVF- 83
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLIVARLQQDPP-------RNVEGTVYd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 --------QQFYLFPHLTALENVMFGPlrvrgaNKEEAEKLAR------------------ELLAKVGLAerAHHYPSEL 137
Cdd:PRK11147 86 fvaegieeQAEYLKRYHDISHLVETDP------SEKNLNELAKlqeqldhhnlwqlenrinEVLAQLGLD--PDAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 138 SGGQQQRVAIARALAVKPKMMLFDEPTSALDP---ELRHEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIetiEWLEGFLKTFQG------SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-191 |
4.92e-17 |
|
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: 76.53 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPT----QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI-NKLEEI--TSGDLIVDGLkvnDPKVDERLIR 76
Cdd:cd03233 6 WRNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNvsVEGDIHYNGI---PYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGankeeaeklarellakvglaeraHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFA-LRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVI 191
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFV 174
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-212 |
8.44e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.38 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCinkLEE------ITSGDLIVDGlkvndPKVDERLIRQeAGMVFQQFYL 88
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAErvttgvITGGDRLVNG-----RPLDSSFQRS-IGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 89 FPHLTALENVMFG-----PLRVRGANKEEAEKLARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKMMLF-D 161
Cdd:TIGR00956 848 LPTSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128777 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE---IGFAEkvASRLIFIDKG 212
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILFEE--FDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
1.43e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.31 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGptqvlhNIDLN-----IAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDgLKVN------DPK 69
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqyiKPD 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 70 VDERLirqeagmvfqQFYLFPHLTALENVMFGPlrvrgankeeaeklarELLAKVGLAERAHHYPSELSGGQQQRVAIAR 149
Cdd:PRK13409 413 YDGTV----------EDLLRSITDDLGSSYYKS----------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAA 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLI 207
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-214 |
1.60e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 12 GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVF-----QQF 86
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR---RLGVAYipedrLGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 YLFPHLTALENVMFG-----PLRVRGA-NKEEAEKLARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKMML 159
Cdd:COG3845 346 GLVPDMSVAENLILGryrrpPFSRGGFlDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-196 |
2.18e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 77.46 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAG--MV 82
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL---ENGisMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGPLRVRG----ANK--EEAEKLARELLAKVGLAERAhhypSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGRYPTKGmfvdQDKmyRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128777 157 MMLFDEPTSAL-DPELRHeVLKVMQDLAEEGMTMVIVTHEI 196
Cdd:PRK10982 155 IVIMDEPTSSLtEKEVNH-LFTIIRKLKERGCGIVYISHKM 194
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-219 |
2.55e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.47 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPT-QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-DGLKVndpkvderlirqeaGMV 82
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV--------------GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 83 FQQFYLFPHLTALENVMFGPLRVRGANKE-------------EAEKLARE---------------LLAKVGLAERAHHYP 134
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGVAEVKAALDRfneiyaayaepdaDFDALAAEqgelqeiidaadawdLDSQLEIAMDALRCP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 135 ------SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIF 208
Cdd:PRK11819 156 pwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILE 232
|
250
....*....|..
gi 16128777 209 IDKGR-IAEDGN 219
Cdd:PRK11819 233 LDRGRgIPWEGN 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-196 |
3.49e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP---TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV-DGLKVNDpkVDERLIRQ 77
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKD--INLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQFYLFPH---------------LTALENVMF--GPLRVRGANKEEA--EKLAREL------LAKVGLAERAHH 132
Cdd:PTZ00265 461 KIGVVSQDPLLFSNsiknnikyslyslkdLEALSNYYNedGNDSQENKNKRNScrAKCAGDLndmsntTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 133 Y-----------------------------------PSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK 177
Cdd:PTZ00265 541 YqtikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|
gi 16128777 178 VMQDL-AEEGMTMVIVTHEI 196
Cdd:PTZ00265 621 TINNLkGNENRITIIIAHRL 640
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-236 |
4.53e-16 |
|
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: 76.91 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 13 PTqvLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvderlirqEAGMVFQQFYLfPHL 92
Cdd:TIGR00957 652 PT--LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------------SVAYVPQQAWI-QND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TALENVMFGplrvrganKEEAEKLARELLAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKMMLFD 161
Cdd:TIGR00957 714 SLRENILFG--------KALNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 162 EPTSALDPEL-RHEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIKNPPSqrLQEFL 236
Cdd:TIGR00957 786 DPLSAVDAHVgKHIFEHV---IGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGA--FAEFL 859
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
1.10e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.44 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI---------NKL----EEITSGDLIVDglkvndp 68
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgRRRGSGETIWD------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 69 kvderlIRQEAGMVFQQFylfpHL-----TALENVM----FGPLRVRGANKEEAEKLARELLAKVGLAERAHHYP-SELS 138
Cdd:PRK10938 334 ------IKKHIGYVSSSL----HLdyrvsTSVRNVIlsgfFDSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLS 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 139 GGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEigfAEK----VASRLIFIDKGR 213
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHH---AEDapacITHRLEFVPDGD 480
|
.
gi 16128777 214 I 214
Cdd:PRK10938 481 I 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
1.19e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLKVNDPKVDErliRQE 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE---RAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGmVFQQFYLFPHLTALENVMFgpLRV------RGANKEEAEKLA-----RELLAKVGLAER-AHHYPSE-LSGGQQQRV 145
Cdd:CHL00131 84 LG-IFLAFQYPIEIPGVSNADF--LRLaynskrKFQGLPELDPLEfleiiNEKLKLVGMDPSfLSRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 146 AIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFI-DKGRIAEDGN 219
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVmQNGKIIKTGD 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-207 |
1.31e-15 |
|
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: 75.59 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 24 IAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDgLKVN-DPKVderlIRQEAGMVFQQFylfphltaLENVMFGP 102
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISyKPQY----ISPDYDGTVEEF--------LRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 103 LrvrGANKEEAEkLARELlakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDL 182
Cdd:COG1245 430 F---GSSYYKTE-IIKPL----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*.
gi 16128777 183 AEE-GMTMVIVTHEIGFAEKVASRLI 207
Cdd:COG1245 502 AENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-240 |
2.19e-15 |
|
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: 73.35 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHF--GPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVNdpKVDERLIRQEA 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWN--SVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPhltalenvmfGPLRVR-----GANKEEAEKLAREllakVGLAERAHHYPSEL-----------SGGQQQ 143
Cdd:cd03289 80 GVIPQKVFIFS----------GTFRKNldpygKWSDEEIWKVAEE----VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 144 RVAIARALAVKPKMMLFDEPTSALDPeLRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGNPQVL 223
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKL 223
|
250 260
....*....|....*....|....*
gi 16128777 224 IKN--------PPSQRLQEFLQHVS 240
Cdd:cd03289 224 LNEkshfkqaiSPSDRLKLFPRRNS 248
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
3.38e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 3.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQ-VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS--SLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVfQQFYLFPHLTALENVMFGplrvrganKEEAEKLARELLAKVGLAERAHHYP-----------SELSGGQQQRVAIAR 149
Cdd:PRK10790 419 MV-QQDPVVLADTFLANVTLG--------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 150 ALAVKPKMMLFDEPTSALDPELRHEVLKVMQdLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLI 224
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-234 |
3.80e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.39 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAgm 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 vfqqfY--------LFPHLTALENV-MFGplRVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
Cdd:NF033858 80 -----YmpqglgknLYPTLSVFENLdFFG--RLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 153 VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEE--GMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGNPQVLIKNPPSQ 230
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLARTGAD 231
|
....
gi 16128777 231 RLQE 234
Cdd:NF033858 232 TLEA 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-196 |
6.82e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.66 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 13 PTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkvndpkvdERLIrqeaGMVFQQFYLFpHL 92
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERSI----AYVPQQAWIM-NA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TALENVMFgplrvrgANKEEAEKLAR-----ELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDE 162
Cdd:PTZ00243 736 TVRGNILF-------FDEEDAARLADavrvsQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128777 163 PTSALDPELRHevlKVMQDL---AEEGMTMVIVTHEI 196
Cdd:PTZ00243 809 PLSALDAHVGE---RVVEECflgALAGKTRVLATHQV 842
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-194 |
7.93e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 26 QGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQfylfpHLTALEN-------- 97
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVK-------ILSGELIPNLGDYEEEPSWDEVLKRFRGTELQN-----YFKKLYNgeikvvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 98 ---VMFGPLRVRGANKEEAEK-----LARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:PRK13409 166 pqyVDLIPKVFKGKVRELLKKvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*
gi 16128777 170 ELRHEVLKVMQDLAeEGMTMVIVTH 194
Cdd:PRK13409 246 RQRLNVARLIRELA-EGKYVLVVEH 269
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-198 |
1.66e-14 |
|
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: 70.05 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGMVF--QQFYLFpHLTA 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 95 LENVMFG-PL-RVRGANKEEAEKLAREL-LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPEL 171
Cdd:cd03290 96 EENITFGsPFnKQRYKAVTDACSLQPDIdLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180
....*....|....*....|....*....
gi 16128777 172 RHEVLK--VMQDLAEEGMTMVIVTHEIGF 198
Cdd:cd03290 176 SDHLMQegILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-225 |
1.98e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.08 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGP-TQVLHnIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKvdERLIRQEAG 80
Cdd:NF033858 267 IEARGLTMRFGDfTAVDH-VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAG--DIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMfgpLRVR--GANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMM 158
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLE---LHARlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 159 LFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA 486
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-229 |
4.78e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLF------ 89
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE--LRRQFSMIPQDPVLFdgtvrq 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 90 ---PHL--------TALENVmfgPLRVRGANKEEaeklarellakvGLAERAHHYPSELSGGQQQRVAIARALAVK-PKM 157
Cdd:PTZ00243 1403 nvdPFLeassaevwAALELV---GLRERVASESE------------GIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGF 1467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 158 MLFDEPTSALDPELRHEV-LKVMQdlAEEGMTMVIVTHEIgfaEKVAS--RLIFIDKGRIAEDGNPQVLIKNPPS 229
Cdd:PTZ00243 1468 ILMDEATANIDPALDRQIqATVMS--AFSAYTVITIAHRL---HTVAQydKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-196 |
5.05e-14 |
|
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: 69.32 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 27 GEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVNDPKVDERLIRQEAGMVFQQFylfphLTAL----------- 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALK-------ILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNY-----FTKLlegdvkvivkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFGPLRVRGA------NKEEAEKLaRELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:cd03236 94 QYVDLIPKAVKGKvgellkKKDERGKL-DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 16128777 170 ELRHEVLKVMQDLAEEGMTMVIVTHEI 196
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-229 |
5.08e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPT--QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFYLFPhltalenvmfGPLRV------RGANKEEAEKLARELLAKV------GLAERAHHYPSELSGGQQQRVAI 147
Cdd:PLN03130 1316 GIIPQAPVLFS----------GTVRFnldpfnEHNDADLWESLERAHLKDVirrnslGLDAEVSEAGENFSVGQRQLLSL 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 148 ARALAVKPKMMLFDEPTSALDpeLRHEVLkVMQDLAEE--GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIK 225
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVD--VRTDAL-IQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
....
gi 16128777 226 NPPS 229
Cdd:PLN03130 1462 NEGS 1465
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-217 |
1.22e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 19 NIDLNIAQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDGLKVnDPKVDERLIRQEAGMV---FQQFYLFPHLTA 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVpedRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 95 LENVMFGPLR---VRGANKEEAE-KLARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDP 169
Cdd:TIGR02633 357 GKNITLSVLKsfcFKMRIDAAAElQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128777 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-221 |
1.94e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 24 IAQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVNDPKVDErLIRQEA----------GM-VFQqfYLFPHL 92
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAE-LARHRAylsqqqtppfAMpVFQ--YLTLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TAlenvmfgplrvrGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARA-LAVKP------KMMLFDEPTS 165
Cdd:PRK03695 95 PD------------KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGNPQ 221
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-170 |
1.98e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 5 KNVSKHFGPtqvlhnIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERliRQEAGMVFQ 84
Cdd:PRK13543 21 RNEEPVFGP------LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDR--SRFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 85 QFYLFPHLTALENVMFgplrVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPT 164
Cdd:PRK13543 90 LPGLKADLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
....*.
gi 16128777 165 SALDPE 170
Cdd:PRK13543 166 ANLDLE 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-213 |
2.44e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.90 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 55 SGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFpHLTALENVMFGPLR-----VRGANK-----EEAEKLARELLAKV 124
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKD--LRNLFSIVSQEPMLF-NMSIYENIKFGKEDatredVKRACKfaaidEFIESLPNKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 125 GlaerahHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVA 203
Cdd:PTZ00265 1353 G------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSD 1426
|
170
....*....|
gi 16128777 204 SRLIFIDKGR 213
Cdd:PTZ00265 1427 KIVVFNNPDR 1436
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-212 |
4.08e-13 |
|
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: 65.42 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLR-CINKLEEitsgDLIVDGLKVNDpkvderliRQEAGMVFQqfylfphLTAL 95
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLYASGK----ARLISFLPKFS--------RNKLIFIDQ-------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 ENVMFGPLRvrgankeeaekLARELlakvglaerahhypSELSGGQQQRVAIARALAVKPK--MMLFDEPTSALDPELRH 173
Cdd:cd03238 72 IDVGLGYLT-----------LGQKL--------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128777 174 EVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKG 212
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-207 |
5.83e-13 |
|
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: 67.65 E-value: 5.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDErlIRQeagm 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQ--SRD---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 vfqqfylfpHLTALENVMfgplrvrganKEEAEKLARELLAKVGLAERAH------------HYPSELSGGQQQRVAIAR 149
Cdd:TIGR03719 396 ---------ALDPNKTVW----------EEISGGLDIIKLGKREIPSRAYvgrfnfkgsdqqKKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 150 ALAVKPKMMLFDEPTSALDPelrhEVLKVMQDLAEE--GMTMVIvTHEIGFAEKVASRLI 207
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNfaGCAVVI-SHDRWFLDRIATHIL 511
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-219 |
7.60e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.99 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLIRQEAGMVFQqfylfphLTALE 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQ-------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 97 NVMFGPLrVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVL 176
Cdd:PRK13546 105 NIEFKML-CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128777 177 KVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGN 219
Cdd:PRK13546 184 DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-193 |
1.49e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.67 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI-NKLEEI---TSGDLIVDGLKVNDPKvdeRLIRQEAGMVFQQFYLFP 90
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFhigVEGVITYDGITPEEIK---KHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 91 HLTALENVMF-----GP-LRVRGANKEE-AEKLARELLAKVGLAeraHHYPSE--------LSGGQQQRVAIARALAVKP 155
Cdd:TIGR00956 152 HLTVGETLDFaarckTPqNRPDGVSREEyAKHIADVYMATYGLS---HTRNTKvgndfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128777 156 KMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT 193
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVA 266
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-219 |
1.86e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.07 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTLlrcinkleeitsGDLIVDGLKVNDPKVDerlIRQEAGMVFQQFYLFPHLTALE 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTL------------SNLIAGVTMPNKGTVD---IKGSAALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 97 NVMFGPLrVRGANKEEAEKLARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVL 176
Cdd:PRK13545 105 NIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128777 177 KVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGN 219
Cdd:PRK13545 184 DKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-215 |
3.59e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 19 NIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirqEAGMVF-----QQFYLFPHLT 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL---ARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 94 ALENV---MFG--PLRVRGAnKEEA--EKLARELLAKVGLAERAhhyPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:PRK15439 358 LAWNVcalTHNrrGFWIKPA-RENAvlERYRRALNIKFNHAEQA---ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128777 167 LDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-169 |
8.56e-12 |
|
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: 64.55 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEiTSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPhltal 95
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWN--SVTLQTWRKAFGVIPQKVFIFS----- 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 96 envmfGPLRVR-----GANKEEAEKLAREllakVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKMML 159
Cdd:TIGR01271 1306 -----GTFRKNldpyeQWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILL 1376
|
170
....*....|
gi 16128777 160 FDEPTSALDP 169
Cdd:TIGR01271 1377 LDEPSAHLDP 1386
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-217 |
1.15e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 137 LSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
.
gi 16128777 217 D 217
Cdd:PRK13549 486 D 486
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-229 |
1.69e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGP--TQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
Cdd:PLN03232 1234 SIKFEDVHLRYRPglPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFYLFPHltaleNVMFGPLRVRGANKEEA-EKLARELLAKV------GLAERAHHYPSELSGGQQQRVAIARAL 151
Cdd:PLN03232 1312 LSIIPQSPVLFSG-----TVRFNIDPFSEHNDADLwEALERAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 152 AVKPKMMLFDEPTSALDpeLRHEVLkVMQDLAEE--GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLIKNPPS 229
Cdd:PLN03232 1387 LRRSKILVLDEATASVD--VRTDSL-IQRTIREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-214 |
2.46e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.60 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRcinkleeITSGDLIVDGLKVN-DPkvDERL--IRQ 77
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMK-------ILGGDLEPSAGNVSlDP--NERLgkLRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EagmvfqQFyLFPHLTALENVMFGPLRVRGANKEE-------------------------------AEKLARELLAKVGL 126
Cdd:PRK15064 72 D------QF-AFEEFTVLDTVIMGHTELWEVKQERdriyalpemseedgmkvadlevkfaemdgytAEARAGELLLGVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 127 AERAHHYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPelrHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASR 205
Cdd:PRK15064 145 PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI---NTIRWLEDVLNERNSTMIIISHDRHFLNSVCTH 221
|
....*....
gi 16128777 206 LIFIDKGRI 214
Cdd:PRK15064 222 MADLDYGEL 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-224 |
6.26e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSkhfGPTqvLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLI------ 75
Cdd:PRK10762 258 LKVDNLS---GPG--VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAngivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 76 ---RQEAGMVFQqfylfphLTALENVMFGPLR----VRGANKEEAEKLArellakVGLAERAHHY--PS------ELSGG 140
Cdd:PRK10762 333 sedRKRDGLVLG-------MSVKENMSLTALRyfsrAGGSLKHADEQQA------VSDFIRLFNIktPSmeqaigLLSGG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 141 QQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI-----A 215
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftR 479
|
....*....
gi 16128777 216 EDGNPQVLI 224
Cdd:PRK10762 480 EQATQEKLM 488
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-207 |
1.03e-10 |
|
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: 58.74 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 24 IAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpkvderlirqeagmvfqqfylfphltalenvMFGPL 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP---------------------------------VYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 104 RVrgankeeaeklarellakvglaerahhypsELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLA 183
Cdd:cd03222 69 YI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*
gi 16128777 184 EEGM-TMVIVTHEIGFAEKVASRLI 207
Cdd:cd03222 119 EEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
1.15e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 MVFQQFYLFPHLTALENVMFGpLRVRGANKEEAEklarelLAKVGLAERAHHYPSEL-SGGQQQRVAIARALAVKPKMML 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYD-IHFSPGAVGITE------LCRLFSLEHLIDYPCGLlSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 16128777 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-208 |
4.32e-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: 56.61 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 26 QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdglkVNDPKVDERLIRQEAGMVFqqfylfphltalenvmfgplrv 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLIIV---------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 106 rgankeeaeklarellakvglaeraHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLK------VM 179
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180
....*....|....*....|....*....
gi 16128777 180 QDLAEEGMTMVIVTHEIGFAEKVASRLIF 208
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-172 |
9.04e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 9.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVNDPKVDerlirqeagm 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVD---------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 82 vfqQFY--LFPHLTALENVMFGPLRVRGANKEEAeklARELLA-----------KVGlaerahhypsELSGGQQQRVAIA 148
Cdd:PRK11819 394 ---QSRdaLDPNKTVWEEISGGLDIIKVGNREIP---SRAYVGrfnfkggdqqkKVG----------VLSGGERNRLHLA 457
|
170 180
....*....|....*....|....*
gi 16128777 149 RALAVKPKMMLFDEPTSALDPE-LR 172
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVEtLR 482
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-168 |
2.07e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 56.40 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPtqVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdglkvndpkvderlIRQEAGMVF 83
Cdd:cd03291 42 FSNLCLVGAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-----------------IKHSGRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 --QQFYLFPHlTALENVMFG----PLRVRGANKeeAEKLARELLAkvgLAERAHHYPSE----LSGGQQQRVAIARALAV 153
Cdd:cd03291 103 ssQFSWIMPG-TIKENIIFGvsydEYRYKSVVK--ACQLEEDITK---FPEKDNTVLGEggitLSGGQRARISLARAVYK 176
|
170
....*....|....*
gi 16128777 154 KPKMMLFDEPTSALD 168
Cdd:cd03291 177 DADLYLLDSPFGYLD 191
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-194 |
2.33e-09 |
|
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: 57.07 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNiDLN--IAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLirqe 78
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIE-SLSfeVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA--------KGKL---- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 agmvfqqFYL--FPHLT--ALENVMFGPLRV-----RGANKEEAEKLARE-----LLAKVGLAERAHHYPSELSGGQQQR 144
Cdd:TIGR00954 518 -------FYVpqRPYMTlgTLRDQIIYPDSSedmkrRGLSDKDLEQILDNvqlthILEREGGWSAVQDWMDVLSGGEKQR 590
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTH 194
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVDVEG---YMYRLCREFGITLFSVSH 637
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-196 |
2.48e-09 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.40 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 9 KHFGPTQVLHNIDLNiaqGEVVVIIGPSGSGKSTLLRCI-------------------NKLEEITSGDLIV--------- 60
Cdd:COG0419 8 ENFRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIryalygkarsrsklrsdliNVGSEEASVELEFehggkryri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 61 -------DGLKVNDPKVDERLIRQEAGM-VFQQFYLfpHLTALENvmfgPLRVRGANKEEAEKLARELLAKV-GLAErah 131
Cdd:COG0419 85 errqgefAEFLEAKPSERKEALKRLLGLeIYEELKE--RLKELEE----ALESALEELAELQKLKQEILAQLsGLDP--- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128777 132 hyPSELSGGQQQRVAIARALAvkpkmMLFDepTSALDPELRHEVLKVMQDLAeegmtmvIVTHEI 196
Cdd:COG0419 156 --IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
3.00e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLE--EITSGDLIVDGLKVNDPKVDERlirqe 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AG----MVFQ----------QFYLFPHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYpsELSGGQQQR 144
Cdd:PRK09580 76 AGegifMAFQypveipgvsnQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNV--GFSGGEKKR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-215 |
3.48e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 3.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 137 LSGGQQQRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-195 |
1.20e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL-IVDGLKVNdpkvderlirqea 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLG------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 gmVFQQFYLfPHLTALENvmfgPLR--VRGANKEEAEKLaRELLAKVGL-AERAHHYPSELSGGQQQRVAIARALAVKPK 156
Cdd:PRK10636 379 --YFAQHQL-EFLRADES----PLQhlARLAPQELEQKL-RDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128777 157 MMLFDEPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHE 195
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHD 486
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-207 |
1.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLR-------------C-INKLEEITSGDLIVDGLKVND 67
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipknCqILHVEQEVVGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 68 PKVDE-RLIRQEAGMVFQQFYL-FPHLTAL----------ENVMFGPL-----RVRGANKEEAEKLARELLAKVGL-AER 129
Cdd:PLN03073 258 TDIERtQLLEEEAQLVAQQRELeFETETGKgkgankdgvdKDAVSQRLeeiykRLELIDAYTAEARAASILAGLSFtPEM 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 130 AHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-214 |
1.90e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 2 IEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIVDGLKV---------------- 65
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVkwsenanigyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 66 ----ND------------PKVDERLIRQEAG-MVFQQfylfphltalenvmfgplrvrgankEEAEKlarelLAKVglae 128
Cdd:PRK15064 393 ydfeNDltlfdwmsqwrqEGDDEQAVRGTLGrLLFSQ-------------------------DDIKK-----SVKV---- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 129 rahhypseLSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElRHEVLKVMQDLAEEgmTMVIVTHEIGFAEKVASRLIF 208
Cdd:PRK15064 439 --------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME-SIESLNMALEKYEG--TLIFVSHDREFVSSLATRIIE 507
|
....*.
gi 16128777 209 IDKGRI 214
Cdd:PRK15064 508 ITPDGV 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-168 |
2.74e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 4 FKNVSKHFGPtqVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVNDPKvderlIRQEAGMVF 83
Cdd:TIGR01271 431 FSNFSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLM------------MIMGELEPSEGK-----IKHSGRISF 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 84 --QQFYLFPHlTALENVMFG----PLRVRGANK-----EEAEKLAREllAKVGLAERAhhypSELSGGQQQRVAIARALA 152
Cdd:TIGR01271 492 spQTSWIMPG-TIKDNIIFGlsydEYRYTSVIKacqleEDIALFPEK--DKTVLGEGG----ITLSGGQRARISLARAVY 564
|
170
....*....|....*.
gi 16128777 153 VKPKMMLFDEPTSALD 168
Cdd:TIGR01271 565 KDADLYLLDSPFTHLD 580
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-195 |
5.65e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.87 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL----------LRCINKLE----------EITSGDLIvDGLKVNdPKVDERLIR 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSayarqflgqmDKPDVDSI-EGLSPA-IAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEagmvfqqfylfPHLTAlenvmfgplrvrGANKEEAEKLaRELLAKVGLAER---------AHHYPSE----LSGGQQQ 143
Cdd:cd03270 89 RN-----------PRSTV------------GTVTEIYDYL-RLLFARVGIRERlgflvdvglGYLTLSRsaptLSGGEAQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128777 144 RVAIARALAVKPKMML--FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:cd03270 145 RIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-203 |
6.75e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLI-VDGLKVNDpkvderlIRQEA 79
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARAL-------AGELPlLSGERQSQ-------FSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMVFQQFylfPHLTALE-----NVMFGP------LRVRGANKEEAEKLAR--ELLAKVG---LAERAHHYpseLSGGQQQ 143
Cdd:PRK10938 69 RLSFEQL---QKLVSDEwqrnnTDMLSPgeddtgRTTAEIIQDEVKDPARceQLAQQFGitaLLDRRFKY---LSTGETR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 144 RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVT---HEI-GFAEKVA 203
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLnrfDEIpDFVQFAG 206
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-236 |
6.77e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 137 LSGGQQQRVAIARALAVKPK--MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE---IGFAEKVasrlifIDK 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRI------IDI 550
|
90 100
....*....|....*....|....*
gi 16128777 212 GRIAEDGNPQVLIKNPPsqrlQEFL 236
Cdd:PRK00635 551 GPGAGIFGGEVLFNGSP----REFL 571
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-195 |
2.24e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLkvndPKVDERLIRQeAGMVFQQFYLFPHL 92
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGF----PKKQETFARI-SGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 93 TALENVMFGP-LRV-RGANKEEAEKLARELL----------AKVGLAErahhyPSELSGGQQQRVAIARALAVKPKMMLF 160
Cdd:PLN03140 969 TVRESLIYSAfLRLpKEVSKEEKMMFVDEVMelveldnlkdAIVGLPG-----VTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|....*
gi 16128777 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-195 |
3.10e-07 |
|
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: 49.92 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL--------LRCINKLEEITSGDL-IVDGL----KVNDpkVDERLI----RQEA 79
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypaLARRLHLKKEQPGNHdRIEGLehidKVIV--IDQSPIgrtpRSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 GMvfqqfY--LFPHLTAL-----ENVMFGP--LRVRGANK----------EEAE-------KLAREL--LAKVGLAERAH 131
Cdd:cd03271 89 AT-----YtgVFDEIRELfcevcKGKRYNRetLEVRYKGKsiadvldmtvEEALeffenipKIARKLqtLCDVGLGYIKL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128777 132 HYPS-ELSGGQQQRVAIARALAVK---PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:cd03271 164 GQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-195 |
4.37e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 29 VVVIIGPSGSGKSTLLRCINKleeITSGDLIvdgLKVNDPKVDERLIRQEA--GMVFQQFYLFP--------HLTALENV 98
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKY---ALTGELP---PNSKGGAHDPKLIREGEvrAQVKLAFENANgkkytitrSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 99 MFGPlrvrganKEEAEKLARELLAKvglaerahhypseLSGGQQQ------RVAIARALAVKPKMMLFDEPTSALDPELR 172
Cdd:cd03240 98 IFCH-------QGESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180
....*....|....*....|....*..
gi 16128777 173 ----HEVLKVMQdlAEEGMTMVIVTHE 195
Cdd:cd03240 158 eeslAEIIEERK--SQKNFQLIVITHD 182
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-172 |
1.05e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQ------------GEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderLIRQEAGMVFQ 84
Cdd:PRK13541 4 LHQLQFNIEQknlfdlsitflpSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN------IAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 85 QFYLFPHLTALENVmfgplrvrgankeeaeKLARELLAKVGLAERAHHY----------PSELSGGQQQRVAIARALAVK 154
Cdd:PRK13541 78 NLGLKLEMTVFENL----------------KFWSEIYNSAETLYAAIHYfklhdlldekCYSLSSGMQKIVAIARLIACQ 141
|
170
....*....|....*...
gi 16128777 155 PKMMLFDEPTSALDPELR 172
Cdd:PRK13541 142 SDLWLLDEVETNLSKENR 159
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-211 |
1.07e-06 |
|
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: 47.35 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 21 DLNIAQGEVVVIIGPSGSGKSTLLRCINkleeitsgdLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHltalenvmf 100
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKAGCIVAAVSAELIFTRL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 101 gplrvrgankeeaeklarellakvglaerahhypsELSGGQQQRVAIARALA---VKPK-MMLFDEPTSALDPELRHEVL 176
Cdd:cd03227 77 -----------------------------------QLSGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|....*
gi 16128777 177 KVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDK 211
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAEL-ADKLIHIKK 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-216 |
2.79e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 3 EFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkLEEI--TSGDLIVdGLKVNDPKVDERliRQEag 80
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLqaDSGRIHC-GTKLEVAYFDQH--RAE-- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 81 mvfqqfyLFPHLTALENVMFGplrvrganKEEAEKLARELLAKVGLAE------RAHHYPSELSGGQQQRVAIARaLAVK 154
Cdd:PRK11147 394 -------LDPEKTVMDNLAEG--------KQEVMVNGRPRHVLGYLQDflfhpkRAMTPVKALSGGERNRLLLAR-LFLK 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 155 P-KMMLFDEPTSALDPELRhEVLKVMqdLAEEGMTMVIVTHEIGFAEK-VASRLIFIDKGRIAE 216
Cdd:PRK11147 458 PsNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVDNtVTECWIFEGNGKIGR 518
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-224 |
3.17e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.83 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 16 VLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQ---------QF 86
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 87 YLFPHLTALENVMFGPLRVrgankEEAEKLARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKMMLFDEPTSA 166
Cdd:cd03288 114 NLDPECKCTDDRLWEALEI-----AQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128777 167 LDPELRHEVLK-VMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGNPQVLI 224
Cdd:cd03288 187 IDMATENILQKvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-168 |
5.20e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHF--GPTqVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCInkleeitSGDL-IVDGLKVNDPKVdeRLirq 77
Cdd:PLN03073 508 IISFSDASFGYpgGPL-LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SGELqPSSGTVFRSAKV--RM--- 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 eagMVFQQFylfpHLTALENVMFGPLRVRGANKEEAEKLARELLAKVGLAERAHHYPS-ELSGGQQQRVAIARALAVKPK 156
Cdd:PLN03073 575 ---AVFSQH----HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPH 647
|
170
....*....|..
gi 16128777 157 MMLFDEPTSALD 168
Cdd:PLN03073 648 ILLLDEPSNHLD 659
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-195 |
5.20e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 15 QVLHNIDLNIAQGEVVVIIGPSGSGKSTLLRCI-------NkleeiTSGDLIVDGLKVNDPKVDeRLI----------RQ 77
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrN-----ISGTVFKDGKEVDVSTVS-DAIdaglayvtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 78 EAGMVFQQfylfphlTALENVMFGPLR------VRGANKE--EAEKLAREL-------LAKVGlaerahhypsELSGGQQ 142
Cdd:NF040905 348 GYGLNLID-------DIKRNITLANLGkvsrrgVIDENEEikVAEEYRKKMniktpsvFQKVG----------NLSGGNQ 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 143 QRVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSE 463
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-194 |
5.36e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 5.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 135 SELSGGQQQRVAIARAL---AVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
8.47e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 8.47e-06
10 20
....*....|....*....|....*..
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL 43
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-213 |
9.32e-06 |
|
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: 44.95 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLN-IAQGEVVVIIGPSGSGKSTLLrcinklEEIT---SGDLIVDGlKVNDPKVDERLIR 76
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVIDFTgLDNNGLFLICGPTGAGKSTIL------DAITyalYGKTPRYG-RQENLRSVFAPGE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 77 QEAGMVFQqFYLFPHLTALEnvmfgplRVRGANKEEAEKLAreLLAKVGLAERAHHYPSELSGGQQQRVAIARALAV--- 153
Cdd:cd03279 74 DTAEVSFT-FQLGGKKYRVE-------RSRGLDYDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLALALsev 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128777 154 ------KPKMMLF-DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIfIDKGR 213
Cdd:cd03279 144 lqnrggARLEALFiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLE-VIKTP 209
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-194 |
1.08e-05 |
|
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: 46.16 E-value: 1.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128777 137 LSGGQQQRVAIARALAVK---PKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-239 |
3.91e-05 |
|
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: 43.84 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 17 LHNIDLNIAQGeVVVIIGPSGSGKSTLLRCINKL------EEITSGDLIVDGLKVNDP------------KVDERLIRQE 78
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLlgpsssRKFDEEDFYLGDDPDLPEieieltfgsllsRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 79 AGMVFQQFY------LFPHLTALENV-------MFGPLRVR-GANKEEAEKLARELlaKVGLAERAHHYPSELSGGQQQR 144
Cdd:COG3593 93 DKEELEEALeelneeLKEALKALNELlseylkeLLDGLDLElELSLDELEDLLKSL--SLRIEDGKELPLDRLGSGFQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 145 VAIA--RALA-----VKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKV-ASRLIFIDKGriaE 216
Cdd:COG3593 171 ILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRD---S 247
|
250 260
....*....|....*....|...
gi 16128777 217 DGNPQVLIKNPPSQRLQEFLQHV 239
Cdd:COG3593 248 GGTTSTKLIDLDDEDLRKLLRYL 270
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
134-194 |
4.09e-05 |
|
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: 43.92 E-value: 4.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128777 134 PSELSGGQQQ---RVAIARALAVKPKMMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
113-194 |
6.98e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 113 AEKLarELLAKVGLAerahhY-----PS-ELSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMQDLA 183
Cdd:COG0178 804 ARKL--QTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLV 876
|
90
....*....|.
gi 16128777 184 EEGMTMVIVTH 194
Cdd:COG0178 877 DKGNTVVVIEH 887
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-43 |
1.52e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.52e-04
10 20
....*....|....*....|....*..
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL 43
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-228 |
2.24e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 135 SELSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAeKVASRLIFIDK 211
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALL-KQADYLIEMGP 1776
|
90
....*....|....*..
gi 16128777 212 GRIAEDGnpQVLIKNPP 228
Cdd:PRK00635 1777 GSGKTGG--KILFSGPP 1791
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
17-59 |
2.24e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.84 E-value: 2.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16128777 17 LHNIDLNIaqGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLI 59
Cdd:COG4637 13 LRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARGGLQ 53
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-43 |
2.92e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 2.92e-04
10 20
....*....|....*....|....*..
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL 43
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-44 |
2.97e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 2.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 16128777 1 MIEFKNVSKHfgptqVLHNIDLNIAQGEVVVIIGPSGSGKSTLL 44
Cdd:TIGR00630 613 FLTLKGAREN-----NLKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-216 |
3.59e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 1 MIEFKNVSKHFGPTQVLHNIDLNIAQGEVVVIIGPSGSGKSTLLrcinkleEITSGDLIVDGLKVNDPKV-DERLIRQEA 79
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLL-------ALLKNEISADGGSYTFPGNwQLAWVNQET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 80 gmvfqqfylfPHL--TALENVMFGPLRVRGANKEEAE---------------KL-----------ARELLAKVGLAERAH 131
Cdd:PRK10636 74 ----------PALpqPALEYVIDGDREYRQLEAQLHDanerndghaiatihgKLdaidawtirsrAASLLHGLGFSNEQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 132 HYP-SELSGGQQQRVAIARALAVKPKMMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFID 210
Cdd:PRK10636 144 ERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
....*.
gi 16128777 211 KGRIAE 216
Cdd:PRK10636 221 QQSLFE 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1-44 |
6.64e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 6.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 16128777 1 MIEFKNVSKHfgptqVLHNIDLNIAQGEVVVIIGPSGSGKSTLL 44
Cdd:PRK00349 614 FLKLKGAREN-----NLKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
7.92e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 7.92e-04
10 20
....*....|....*....|....*..
gi 16128777 17 LHNIDLNIAQGEVVVIIGPSGSGKSTL 43
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
113-194 |
1.06e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 113 AEKLarELLAKVGLAerahhY-----PS-ELSGGQQQRVAIARALAVKPK---MMLFDEPTSALDPELRHEVLKVMQDLA 183
Cdd:PRK00349 808 ARKL--QTLVDVGLG-----YiklgqPAtTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLV 880
|
90
....*....|.
gi 16128777 184 EEGMTMVIVTH 194
Cdd:PRK00349 881 DKGNTVVVIEH 891
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-193 |
1.11e-03 |
|
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: 39.17 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128777 136 ELSGGQQQRVAIARALAVK-----PkMMLFDEPTSALDPELRHEVLKVMQDLAEEgmTMVIVT 193
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDAQYRTAVANMIKELSDG--AQFITT 217
|
|
| VirD4 |
COG3505 |
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, ... |
30-122 |
2.34e-03 |
|
Type IV secretory pathway, VirD4 component, TraG/TraD family ATPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442728 [Multi-domain] Cd Length: 402 Bit Score: 38.43 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 30 VVIIGPSGSGKSTLLrCINKLEEITSGDLIVdglkVNDPKVD--ERLI--RQEAGmvfQQFYLFpHLTALENVM-FGPLR 104
Cdd:COG3505 2 VLVIGPTGSGKTVGL-VIPNLTQLARGESVV----VTDPKGDlaELTAgfRRRAG---YDVYVF-DPFDPERSHrWNPLD 72
|
90
....*....|....*...
gi 16128777 105 vRGANKEEAEKLARELLA 122
Cdd:COG3505 73 -EIRDPADAQELAEALIP 89
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
18-48 |
2.51e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|.
gi 16128777 18 HNIDLNiAQGEVVVIIGPSGSGKSTLLRCIN 48
Cdd:COG3950 17 LEIDFD-NPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
27-45 |
2.55e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 37.12 E-value: 2.55e-03
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
24-52 |
3.32e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 3.32e-03
10 20 30
....*....|....*....|....*....|.
gi 16128777 24 IAQGE-VVVIIGPSGSGKSTLLRC-INKLEE 52
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRlLERLPD 69
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-50 |
4.95e-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: 36.99 E-value: 4.95e-03
10 20
....*....|....*....|....*
gi 16128777 26 QGEVVVIIGPSGSGKSTLlrcINKL 50
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNAL 105
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
29-49 |
5.01e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.36 E-value: 5.01e-03
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
26-133 |
5.27e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 36.71 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 26 QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-------ERLIRQEAGMVFQQFyLFPHLTALENV 98
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFLRGKCDENLPYSPllealtrEGLLRQLLDELESSL-LEAWRAALLEA 101
|
90 100 110
....*....|....*....|....*....|....*
gi 16128777 99 MFGPLRVRGankEEAEKLARELLAKVGLAERAHHY 133
Cdd:pfam13191 102 LAPVPELPG---DLAERLLDLLLRLLDLLARGERP 133
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
9-47 |
5.41e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 5.41e-03
10 20 30
....*....|....*....|....*....|....*....
gi 16128777 9 KHFGPtqvLHNIDLNIAQGeVVVIIGPSGSGKSTLLRCI 47
Cdd:pfam13476 4 ENFRS---FRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-44 |
5.58e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.50 E-value: 5.58e-03
10 20
....*....|....*....|....*..
gi 16128777 18 HNIDLNIAQGEVVVIIGPSGSGKSTLL 44
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-47 |
6.46e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.98 E-value: 6.46e-03
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-181 |
8.52e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 34.52 E-value: 8.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128777 135 SELSGGQQQR---VAIARALA----------VKPKMMLFDEPTSALDPELRHEVLKVMQD 181
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PrkA |
COG2766 |
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]; |
11-57 |
9.41e-03 |
|
Predicted Ser/Thr protein kinase [Signal transduction mechanisms];
Pssm-ID: 442049 [Multi-domain] Cd Length: 675 Bit Score: 36.74 E-value: 9.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128777 11 FGPTQVLHNI--DL-NIAQG-----EVVVIIGPSGSGKSTLLRCI-NKLEEITSGD 57
Cdd:COG2766 84 FGLEETLERIvdYLrSAARGlgerkRILLLHGPVGSGKSTLARCLkRGLEEYSRTD 139
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| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
29-73 |
9.74e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 33.85 E-value: 9.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 16128777 29 VVVIIGPSGSGKSTLLRcinKLEEITSGD--------LIVDGLKVNDPKVDER 73
Cdd:cd02019 1 IIAITGGSGSGKSTVAK---KLAEQLGGRsvvvldeiVILEGLYASYKSRDAR 50
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