|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
0e+00 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 496.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 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 |
5.10e-144 |
|
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: 401.14 E-value: 5.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVGF 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-239 |
2.00e-130 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 367.88 E-value: 2.00e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-237 |
2.59e-126 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 357.96 E-value: 2.59e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG------------VNVADP 68
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgeLVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 69 KTdLNKIREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIA 148
Cdd:COG4598 88 RQ-LQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
....*....
gi 488162483 229 HERAKQFLQ 237
Cdd:COG4598 247 SERLRQFLS 255
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
3.31e-107 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 309.37 E-value: 3.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV------ADPKTDLNK 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQ 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*...
gi 488162483 235 FLQQVMTH 242
Cdd:PRK11264 243 FLEKFLLQ 250
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-240 |
4.71e-103 |
|
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: 299.05 E-value: 4.71e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV------------ADPK 69
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLyhmpgrngplvpADEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 70 tDLNKIREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIAR 149
Cdd:TIGR03005 81 -HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:TIGR03005 160 ALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLAsEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPK 239
|
250
....*....|..
gi 488162483 229 HERAKQFLQQVM 240
Cdd:TIGR03005 240 EERTREFLSKVI 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-242 |
2.87e-102 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 300.07 E-value: 2.87e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKI 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQ 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*...
gi 488162483 235 FLQQVMTH 242
Cdd:COG1135 240 FLPTVLND 247
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
8.00e-94 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 274.61 E-value: 8.00e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKI 75
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 R-EEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFArEVADRVIFVDKGQILEDE 218
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSDE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-236 |
1.18e-93 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 274.97 E-value: 1.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIwvdgvNVADPKTDLNK------- 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-----NIAGHQFDFSQkpsekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 --IREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLA 152
Cdd:COG4161 78 rlLRQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAfFTNPKHERA 232
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASH-FTQPQTEAF 236
|
....
gi 488162483 233 KQFL 236
Cdd:COG4161 237 AHYL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-236 |
2.43e-93 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 273.81 E-value: 2.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIwvdgvNVADPKTDLNK------- 74
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGNHFDFSKtpsdkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 --IREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLA 152
Cdd:PRK11124 78 reLRRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAfFTNPKHERA 232
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAF 236
|
....
gi 488162483 233 KQFL 236
Cdd:PRK11124 237 KNYL 240
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
2.15e-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: 258.67 E-value: 2.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKI 75
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-240 |
1.83e-86 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 260.12 E-value: 1.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKI 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQ 234
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*.
gi 488162483 235 FLQQVM 240
Cdd:PRK11153 240 FIQSTL 245
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
8.73e-86 |
|
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: 253.95 E-value: 8.73e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPK-TDLNKIR 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 -EEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREvADRVIFVDKGQI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
1.52e-85 |
|
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: 254.13 E-value: 1.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREEV 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLaPMKVKGQ-NAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAF-PLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPkHERAKQFL 236
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
4.52e-85 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 252.28 E-value: 4.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK-DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREE 78
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDE 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
3.60e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 245.74 E-value: 3.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK-DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKIREE 78
Cdd:COG3638 2 MLELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENI------------TLAPMkvkgqnAEQAEK-KAMELLERVGLAHKKDAFPSQLSGGQQQRV 145
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtstwrSLLGL------FPPEDReRALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
8.73e-82 |
|
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: 253.29 E-value: 8.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF-----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNK 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQG----FNlyPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIAR 149
Cdd:COG1123 340 LRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|.
gi 488162483 229 HERAKQFLQQV 239
Cdd:COG1123 498 HPYTRALLAAV 508
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-236 |
3.37e-81 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.93 E-value: 3.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVG 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV----TGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:COG3842 81 MVFQDYALFPHLTVAENVAF-GLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 161 DEPTSALDP----EMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:COG3842 160 DEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-228 |
1.57e-80 |
|
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: 241.08 E-value: 1.57e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNV-HKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVG 80
Cdd:COG1122 1 IELENLsFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQgfnlYP-----HLTVLENITLAPMKvKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:COG1122 79 LVFQ----NPddqlfAPTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-236 |
4.19e-80 |
|
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: 240.66 E-value: 4.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-ESIE----SGEIWVDGVNVADPKTDLNKIR 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPhLTVLENITLAPmKVKG-QNAEQAEKKAMELLERVGL----AHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGiKDKKELDEIVEESLKKAALwdevKDRLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHER 231
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*
gi 488162483 232 AKQFL 236
Cdd:TIGR00972 239 TEDYI 243
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.17e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 239.99 E-value: 1.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnkir 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 eeVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:COG1116 82 --RGVVFQEPALLPWLTVLDNVAL-GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 157 VMLFDEPTSALDP----EMVGEVLKVmkdLAESGMTMMCVTHEMgfaRE---VADRVIFVDK--GQILED 217
Cdd:COG1116 159 VLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDV---DEavfLADRVVVLSArpGRIVEE 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-237 |
1.25e-79 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 239.87 E-value: 1.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 6 NVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVN------------VADpKTDLN 73
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkVAD-KNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 74 KIREEVGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARGLA 152
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERA 232
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
....*
gi 488162483 233 KQFLQ 237
Cdd:PRK10619 249 QQFLK 253
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
1.48e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 238.81 E-value: 1.48e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvaDPKTDLNKIREEVGF 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
2.75e-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: 238.17 E-value: 2.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREEVG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLaPMKVKGQ-NAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPkHERAKQF 235
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
3.68e-79 |
|
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: 237.03 E-value: 3.68e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
7.77e-79 |
|
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: 234.77 E-value: 7.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVGF 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApmkvkgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 162 EPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-236 |
1.04e-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: 233.83 E-value: 1.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHV-INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEV 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD--LDPVELRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKK--DAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:COG1125 79 GYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 158 MLFDEPTSALDPeMVGEVL-KVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQF 235
Cdd:COG1125 158 LLMDEPFGALDP-ITREQLqDELLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADF 236
|
.
gi 488162483 236 L 236
Cdd:COG1125 237 V 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
4.80e-76 |
|
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: 230.15 E-value: 4.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDL-HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKIREEV 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENI---------TLAPMKvkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARG 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrsTWRSLF--GLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
3.37e-74 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 229.19 E-value: 3.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD--PKtdlnkiREE 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlpPK------DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDP----EMVGEVLKVMKDLaesGMTMMCVTHE----MGFarevADRVIFVDKGQILEDETPEAFFTNPKHE 230
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
....*.
gi 488162483 231 RAKQFL 236
Cdd:COG3839 229 FVAGFI 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-217 |
1.41e-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: 220.84 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIR 76
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 E-EVGFVFQ--GFNLYPHLTVLENITlAPMKVKGQN--AEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARG 150
Cdd:cd03257 81 RkEIQMVFQdpMSSLNPRMTIGEQIA-EPLRIHGKLskKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
4.44e-72 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 223.48 E-value: 4.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpKTDLnKIRE-EVG 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNL-PPRErRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 161 DEPTSALDPemvgevlKVMKDL--------AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERA 232
Cdd:COG1118 158 DEPFGALDA-------KVRKELrrwlrrlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
....
gi 488162483 233 KQFL 236
Cdd:COG1118 231 ARFL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
1.50e-71 |
|
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: 218.20 E-value: 1.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIE-----SGEIWVDGVNVADPKTDLNKIR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPhLTVLENITLAPmKVKG-QNAEQAEKKAMELLERVGLAH--KKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGiKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
7.98e-71 |
|
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: 216.78 E-value: 7.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLH-VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVG 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE--QDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPmKVKGQNAEQAEKKAMELLERVGL--AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQ 237
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 488162483 238 Q 238
Cdd:cd03295 238 A 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-207 |
3.26e-70 |
|
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: 214.26 E-value: 3.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnkire 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 eVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:cd03293 75 -RGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 158 MLFDEPTSALDP----EMVGEVLKVmkdLAESGMTMMCVTHEMGFAREVADRVI 207
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
5.14e-70 |
|
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: 214.85 E-value: 5.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF-KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPK-TDLNKIREE 78
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLAPMKVK-------GQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
3.46e-69 |
|
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: 211.56 E-value: 3.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 3 KFKNVHKHFKDLH--VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVG 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQgfnlYP-----HLTVLENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:cd03225 79 LVFQ----NPddqffGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
4.56e-69 |
|
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: 214.92 E-value: 4.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK----DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLES---IESGEIWVDGVNVAD-PKTDL 72
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 73 NKIR-EEVGFVFQG----FNlyPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKK---DAFPSQLSGGQQQR 144
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*.
gi 488162483 224 FTNPKH 229
Cdd:COG0444 239 FENPRH 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
1.28e-67 |
|
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: 208.44 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpkTDLNKIR 76
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-------QDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EE---------VGFVFQGFNLYPHLTVLENITLaPMKVKGqnAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAI 147
Cdd:COG4181 81 EDararlrarhVGFVFQSFQLLPTLTALENVML-PLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEA 222
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-237 |
3.38e-67 |
|
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: 207.73 E-value: 3.38e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadPKTDLNKIR 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQ----GFNlyPHLTVLEniTLA-PMKVKGQNaeQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARG 150
Cdd:COG1124 79 RRVQMVFQdpyaSLH--PRHTVDR--ILAePLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 488162483 230 ERAKQFLQ 237
Cdd:COG1124 233 PYTRELLA 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-239 |
4.15e-67 |
|
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: 208.27 E-value: 4.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIR-EEVGFVFQGFNLYPHLTV 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP----E 170
Cdd:cd03294 120 LENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 171 MVGEVLKVMkdlAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:cd03294 199 MQDELLRLQ---AELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-236 |
4.16e-66 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 205.27 E-value: 4.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-ESIE----SGEIWVDGVNVADPKTDLNKIR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHlTVLENITLAP----MKVKGQNAEQAEKKamelLERVGL----AHKKDAFPSQLSGGQQQRVAIA 148
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGLrlhgIKSKSELDEIVEES----LRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPemvGEVLKV---MKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDP---ISTAKIeelILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
250
....*....|.
gi 488162483 226 NPKHERAKQFL 236
Cdd:COG1117 243 NPKDKRTEDYI 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-236 |
2.38e-65 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 202.29 E-value: 2.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVinGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVG 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLA--P-MKVkgqNAEQaEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGlrPgLKL---TAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 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 |
3.73e-65 |
|
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: 202.18 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVK----GQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFG-LRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 158 MLFDEPTSALDPemvgevlKVMKDLA--------ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:cd03296 158 LLLDEPFGALDA-------KVRKELRrwlrrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
....*..
gi 488162483 230 ERAKQFL 236
Cdd:cd03296 231 PFVYSFL 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-232 |
4.67e-64 |
|
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: 207.45 E-value: 4.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL---ESIESGEIWVDGVNVADPKTDLnkI 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGF--NLYPhLTVLENITLAPMkVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:COG1123 82 GRRIGMVFQDPmtQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERA 232
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-239 |
4.80e-64 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 204.18 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLesIE--SGEIWVDGVNVAD-PKTDLNKIR-EEVGFVFQGFNLYPHL 92
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRL--IEptAGEVLIDGEDITKlSKKELRELRrKKMSMVFQHFALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP--- 169
Cdd:COG4175 121 TVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlir 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 170 -EMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:COG4175 200 rEMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
8.78e-63 |
|
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: 196.23 E-value: 8.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvaDPKTDLNKIREEVG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE---DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMkVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAE-LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.15e-62 |
|
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: 195.16 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK-DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREE 78
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-225 |
7.11e-62 |
|
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: 194.49 E-value: 7.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlNKIREEVG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR--RELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITL--AP-MKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-226 |
1.00e-61 |
|
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: 194.57 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdLNKIREEV 79
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQgfNlyPH-----LTV-------LENITLAPmkvkgqnaEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAI 147
Cdd:TIGR04520 80 GMVFQ--N--PDnqfvgATVeddvafgLENLGVPR--------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFFTN 226
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-228 |
2.85e-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: 192.27 E-value: 2.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLnKIREEVGFVFQ 84
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLAPMKVKGQNA---------EQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
4.17e-61 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 191.68 E-value: 4.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 162 EPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
9.58e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 190.03 E-value: 9.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVGF 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQgfnlYPHL---TVLENITLaPMKVKGQNAEqaEKKAMELLERVGLAH---KKDAfpSQLSGGQQQRVAIARGLAMEP 155
Cdd:COG4619 79 VPQ----EPALwggTVRDNLPF-PFQLRERKFD--RERALELLERLGLPPdilDKPV--ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
2.20e-60 |
|
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: 191.13 E-value: 2.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNV----HKHFK-DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKI 75
Cdd:TIGR04521 1 IKLKNVsyiyQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQgfnlYPH-----LTVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIAR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
3.74e-60 |
|
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: 188.77 E-value: 3.74e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF-KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREEV 79
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHemgfAREVAD----RVIFVDKGQI 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH----AKELVDttrhRVIALERGKL 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
1.98e-59 |
|
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: 185.29 E-value: 1.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvaDPKTDLNKIREEVGF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENItlapmkvkgqnaeqaekkamellervglahkkdafpsQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-239 |
3.36e-59 |
|
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: 190.83 E-value: 3.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKI-REEVGFVFQGFNLYPHLTV 94
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKqSPVELREVrRKKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP----E 170
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPlirdS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 171 MVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:TIGR01186 168 MQDELKKLQATL---QKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-209 |
2.44e-58 |
|
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: 183.59 E-value: 2.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKI--REEVGFV 82
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrREKLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:TIGR03608 82 FQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFArEVADRVIFV 209
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-228 |
2.70e-58 |
|
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: 188.32 E-value: 2.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDI----TRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 162 EPTSALDPEmVGEVLKV-MKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:TIGR03265 160 EPLSALDAR-VREHLRTeIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPA 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
5.26e-58 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 187.60 E-value: 5.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENI----TLAPMKvKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIafglTVLPRR-ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 488162483 237 QQV 239
Cdd:PRK10851 238 GEV 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-236 |
9.71e-58 |
|
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: 183.31 E-value: 9.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINgVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-223 |
1.18e-57 |
|
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: 182.63 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLnKIREEVGFVFQ 84
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERvgLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:cd03224 83 GRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 165 SALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
1.31e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 182.98 E-value: 1.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPktdlnkiREEVG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-------RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPH--LTVLENITL---APMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:COG1121 79 YVPQRAEVDWDfpITVRDVVLMgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDeTPEAFFTNPKHERAKQF 235
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG-PPEEVLTPENLSRAYGG 237
|
....*..
gi 488162483 236 LQQVMTH 242
Cdd:COG1121 238 PVALLAH 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-228 |
3.51e-57 |
|
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: 182.55 E-value: 3.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnKI-REEV 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH--RIaRLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLAPMKVKGQNA--------------EQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRV 145
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFF 224
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
....
gi 488162483 225 TNPK 228
Cdd:COG0411 242 ADPR 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
6.66e-57 |
|
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: 180.14 E-value: 6.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 162 EPTSALDP----EMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03301 156 EPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-214 |
1.72e-53 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 171.83 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK----DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlNKI- 75
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYS-QKIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 --REEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:NF038007 80 lrRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGfAREVADRVIFVDKGQI 214
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-240 |
2.46e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 175.68 E-value: 2.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGFVFQ 84
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK11432 86 SYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 165 SALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPkherAKQFLQQVM 240
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP----ASRFMASFM 237
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
5.39e-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: 168.58 E-value: 5.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 3 KFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--KLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQgfnlyphltvlenitlapmkvkgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-228 |
7.41e-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: 170.55 E-value: 7.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnKI-REEV 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--RIaRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAM-ELLERvgLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVyELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-229 |
1.31e-52 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 172.99 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHF-----------KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDL 72
Cdd:COG4608 11 RDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSGREL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 73 NKIREEVGFVFQgfNLY----PHLTVlENITLAPMKVKGQ-NAEQAEKKAMELLERVGL--AHKkDAFPSQLSGGQQQRV 145
Cdd:COG4608 91 RPLRRRMQMVFQ--DPYaslnPRMTV-GDIIAEPLRIHGLaSKAERRERVAELLELVGLrpEHA-DRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFF 224
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
....*
gi 488162483 225 TNPKH 229
Cdd:COG4608 247 ARPLH 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-236 |
3.86e-52 |
|
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: 176.80 E-value: 3.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKS----TLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIR-EEVGFVFQ---- 84
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSERELRRIRgNRIAMIFQepmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNlyPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGL---AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:COG4172 104 SLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIAD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
4.32e-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: 166.84 E-value: 4.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnKIREEVGFVFQ 84
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK--ELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 gfnlyphltvlenitlapmkvkgqnaeqaekkameLLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 165 SALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQIL 215
Cdd:cd03214 126 SHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
4.66e-52 |
|
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: 179.26 E-value: 4.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLH--VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEV 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ--IDPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYpHLTVLENITLApmkvkgqNAEQAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIA 148
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEA 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-214 |
1.53e-51 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 171.37 E-value: 1.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM----NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 162 EPTSALDP----EMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK11000 159 EPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
2.23e-51 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 167.40 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-----ESIESGEIWVDGVNVAdpKTDLNKIR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHLTVLENITLAP-MKVKGQNAEQAEKKAMELLERVGL----AHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHER 231
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHEL 240
|
....*
gi 488162483 232 AKQFL 236
Cdd:PRK14247 241 TEKYV 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
3.11e-51 |
|
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: 164.48 E-value: 3.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPktDLNKIREEV 79
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYpHLTVLENItlapmkvkgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQ 213
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
1.13e-50 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 165.79 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-----ESIESGEIWVDGVNVADPKTDLNKIR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHLTVLENITLApmkVKGQNAEQAEKkamELLERVGLAHKKDA-----------FPSQLSGGQQQRV 145
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG---VKLNGLVKSKK---ELDERVEWALKKAAlwdevkdrlndYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|....*
gi 488162483 226 NPKHERAKQFLQQVM 240
Cdd:PRK14267 238 NPEHELTEKYVTGAL 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-228 |
1.67e-50 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.59 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGF 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 162 EPTSALD----PEMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:PRK09452 170 ESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-226 |
7.69e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 164.45 E-value: 7.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVGFVFQgfnlYPHL---- 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQ----YPEYqlfe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 -TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK--KDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP 169
Cdd:PRK13637 99 eTIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 170 EMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK13637 178 KGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.16e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 161.40 E-value: 1.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD-LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEV 79
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQgfNLYPHL---TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:PRK13639 81 GIVFQ--NPDDQLfapTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-215 |
1.21e-48 |
|
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: 159.38 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 7 VHKHFKDLHvingvnLEIK---KGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADP--KTDLNKIREEVGF 81
Cdd:cd03297 6 IEKRLPDFT------LKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkKINLPPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITLApMKVKGQNAEQaeKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFG-LKRKRNREDR--ISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQIL 215
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-206 |
1.50e-48 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 166.35 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdPKTDLNKIREEVG 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQ--NAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRV 206
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
3.39e-48 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 155.88 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvADPKTDLNKIREEVGFVFQGFNLYPHLTVLE 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQ--DLTDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 97 NITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKD----AFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTS 165
Cdd:pfam00005 79 NLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-214 |
7.30e-48 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 157.27 E-value: 7.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 22 LEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV--ADPKtdlnkiREEVGFVFQGFNLYPHLTVLENIT 99
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaAPPA------DRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 100 LAPMKVKGQNAEQaeKKAME-LLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKV 178
Cdd:cd03298 93 LGLSPGLKLTAED--RQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 488162483 179 MKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
8.55e-48 |
|
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: 156.92 E-value: 8.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 3 KFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpktdlnKIREEVGFV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-------KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQGFNL---YPhLTVLENITLA--PMKVKGQNAEQAEK-KAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGlyGHKGLFRRLSKADKaKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKG 212
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-202 |
2.09e-47 |
|
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: 155.71 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLnkiREEVG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY---RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLApMKVKGQNAEQAEkkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFW-AALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTH---EMGFAREV 202
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-237 |
2.26e-47 |
|
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: 164.09 E-value: 2.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 4 FKNVHKHFKdlhVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESiESGEIWVDGVNVAD-PKTDLNKIREEVGFV 82
Cdd:COG4172 292 FRRTVGHVK---AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGlSRRALRPLRRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQ---GfNLYPHLTVLENITlAPMKV--KGQNAEQAEKKAMELLERVGL----AHKkdaFPSQLSGGQQQRVAIARGLAM 153
Cdd:COG4172 368 FQdpfG-SLSPRMTVGQIIA-EGLRVhgPGLSAAERRARVAEALEEVGLdpaaRHR---YPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERA 232
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYT 522
|
....*
gi 488162483 233 KQFLQ 237
Cdd:COG4172 523 RALLA 527
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-221 |
3.44e-47 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 165.28 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTD-LNKIREE-VGFVFQGFNLYP 90
Cdd:PRK10535 20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQLRREhFGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK10535 100 HLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 171 MVGEVLKVMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPE 221
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
3.87e-47 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 159.62 E-value: 3.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK-DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKtDLNkire 77
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPA-DRD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 eVGFVFQGFNLYPHLTVLENITLApMKVKGQNAEQAEK---KAMELLERVGLAHKKdafPSQLSGGQQQRVAIARGLAME 154
Cdd:PRK11650 78 -IAMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEErvaEAARILELEPLLDRK---PRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 155 PRVMLFDEPTSALDP----EMVGEVLKVMKDLaesGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK11650 153 PAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
4.88e-47 |
|
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: 155.67 E-value: 4.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF-------KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV--NQLesIESGEIWVD----GVNV-- 65
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVRhdggWVDLaq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 66 ADPKTDLNKIREEVGFVFQGFNLYPHLTVLEnITLAPMKVKGQNAEQAEKKAMELLERVGLAHKK-DAFPSQLSGGQQQR 144
Cdd:COG4778 82 ASPREILALRRRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
5.29e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 157.58 E-value: 5.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadPKTDLNKI---RE 77
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL--DPEDRRRIgylPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGfvfqgfnLYPHLTVLENIT-LApmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:COG4152 79 ERG-------LYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRK 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-221 |
9.50e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 163.03 E-value: 9.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHkhF---KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREE 78
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD--LTLESLRRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYpHLTVLENITLApmkvkgqNAEQAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAI 147
Cdd:COG1132 416 IGVVPQDTFLF-SGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPE 221
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHE 559
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-236 |
1.01e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 155.70 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-----ESIESGEIWVDGVNVADPKTDLNKI 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGFNLYPhLTVLENIT----LAPMKVKGQNAEQAEK--KAMELLERVglahkKDAFPSQ---LSGGQQQRVA 146
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVyglrLKGIKDKQVLDEAVEKslKGASIWDEV-----KDRLHDSalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 147 IARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
250
....*....|
gi 488162483 227 PKHERAKQFL 236
Cdd:PRK14239 238 PKHKETEDYI 247
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-215 |
1.14e-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: 154.20 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDL--HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpkTDLNKIREEV 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTVLENITLAPMkVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYAR-LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAeSGMTMMCVTHEMGFAREVADRVIFVDKGQIL 215
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
2.22e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 155.02 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF----KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnkiR 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 eevGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488162483 157 VMLFDEPTSALDP----EMVGEVLKVMkdlAESGMTMMCVTH 194
Cdd:COG4525 155 FLLMDEPFGALDAltreQMQELLLDVW---QRTGKGVFLITH 193
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-221 |
2.51e-46 |
|
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: 156.01 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 9 KHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA-DPKtdlnKIREEVGFVFQGFN 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVrEPR----KVRRSIGIVPQYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 LYPHLTVLENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSAL 167
Cdd:TIGR01188 77 VDEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 168 DPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPE 221
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-238 |
2.75e-46 |
|
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: 161.47 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPktDLNKIREEV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL--DEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGfnlyPHL---TVLENITLApmkvkgqnAEQA-EKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQR 144
Cdd:COG4987 412 AVVPQR----PHLfdtTLRENLRLA--------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGfAREVADRVIFVDKGQILEDETPEAff 224
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEE-- 555
|
250
....*....|....
gi 488162483 225 TNPKHERAKQFLQQ 238
Cdd:COG4987 556 LLAQNGRYRQLYQR 569
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-239 |
4.91e-46 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 155.73 E-value: 4.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 34 GPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQA 113
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 114 EKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCV 192
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488162483 193 THEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
4.98e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 155.24 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK-----DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI------------------ 58
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 59 WVDGVNVADPKT----DLNKIREEVGFVFQgFNLYPHL--TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAH---K 129
Cdd:PRK13651 83 VLEKLVIQKTRFkkikKIKEIRRRVGVVFQ-FAEYQLFeqTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDEsylQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 130 KDAFpsQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFV 209
Cdd:PRK13651 161 RSPF--ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*...
gi 488162483 210 DKGQILED 217
Cdd:PRK13651 239 KDGKIIKD 246
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-217 |
5.80e-46 |
|
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: 151.99 E-value: 5.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIreevGF 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRI----GA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENitlapMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03268 77 LIEAPGFYPNLTAREN-----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-226 |
8.08e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 154.09 E-value: 8.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD------LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtDLNK 74
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQG-FNLYPHLTVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:PRK13633 83 IRNKAGMVFQNpDNQIVATIVEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-236 |
1.87e-45 |
|
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: 151.52 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlNKIREEVGFVFQ 84
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAGIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLApmkvkgqnaeqaekkamelLERVGLAHKK------DAFP----------SQLSGGQQQRVAIA 148
Cdd:TIGR03410 83 GREIFPRLTVEENLLTG-------------------LAALPRRSRKipdeiyELFPvlkemlgrrgGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFftnp 227
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL---- 219
|
....*....
gi 488162483 228 KHERAKQFL 236
Cdd:TIGR03410 220 DEDKVRRYL 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-214 |
3.06e-45 |
|
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: 150.40 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 21 NLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDLNKIREEVGFVFQGFNLYPHLTVLENITL 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH----TGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 101 APMKVKGQNAEQAEKkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMK 180
Cdd:TIGR01277 94 GLHPGLKLNAEQQEK-VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 488162483 181 DLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:TIGR01277 173 QLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
4.88e-45 |
|
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: 150.21 E-value: 4.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA-DPKtdlnKIREEVG 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrEPR----EVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHA-RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPE 221
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
2.27e-44 |
|
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: 148.11 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGeVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvaDPKTDLNKIREEVGF 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLEniTLAPMKV-KGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIAWlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-217 |
3.73e-44 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 148.19 E-value: 3.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVinGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNvadpKTDLNKIREEVG 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITL--AP-MKVkgqNAEQAEKKAmELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLglNPgLKL---NAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
3.87e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 149.37 E-value: 3.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLH--VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREE 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQG-FNLYPHLTV-------LENITLAPMKVKGQNAEQAEKKAME-LLERVglahkkdafPSQLSGGQQQRVAIAR 149
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVeddiafgLENKKVPPKKMKDIIDDLAKKVGMEdYLDKE---------PQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGM-TMMCVTHEMgfaREV--ADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEILNN 232
|
250
....*....|.
gi 488162483 227 pkheraKQFLQ 237
Cdd:PRK13632 233 ------KEILE 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-214 |
4.12e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 149.06 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDgvnvadpKTDLNKIREEVGFVFQ 84
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-------TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLApmkVKGQNAEQAEkkamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK11247 89 DARLLPWKKVIDNVGLG---LKGQWRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 165 SALDPEMVGEvlkvMKDLAES-----GMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK11247 162 GALDALTRIE----MQDLIESlwqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-227 |
4.62e-44 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 151.41 E-value: 4.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFkNVHKHFKDLHVinGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLN----KIR 76
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpphRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 eeVGFVFQGFNLYPHLTVLENITLApMK--VKGQNAEQAEkkamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:COG4148 79 --IGYVFQEARLFPHLSVRGNLLYG-RKraPRAERRISFD----EVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRdELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
4.62e-44 |
|
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: 147.43 E-value: 4.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKIREEVG 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 fvfqgfnLYPHLTVLEN-ITLApmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03269 81 -------LYPKMKVIDQlVYLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-222 |
1.19e-43 |
|
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: 154.53 E-value: 1.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVH-KHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVG 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGfnlyPHL---TVLENITLApmkvkgqnAEQAEKKAM-ELLERVGLAHKKDAFP-----------SQLSGGQQQRV 145
Cdd:COG4988 415 WVPQN----PYLfagTIRENLRLG--------RPDASDEELeAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEA 222
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-242 |
1.78e-43 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 147.18 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIR--- 76
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRavl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 ---EEVGFVFqgfnlyphlTVLENITL--APMkvkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:COG4559 81 pqhSSLAFPF---------TVEEVVALgrAPH---GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 A-------MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFF 224
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
250
....*....|....*...
gi 488162483 225 TNPKHERAKQFLQQVMTH 242
Cdd:COG4559 229 TDELLERVYGADLRVLAH 246
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-228 |
3.60e-43 |
|
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: 145.76 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 6 NVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDL---NKIREEVGFV 82
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI----TKLpmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQGFNLYPHLTVLENItLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:cd03218 81 PQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEmgfARE---VADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-227 |
5.21e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 148.07 E-value: 5.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 9 KHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWV------------DGVNVADPKT--DLNK 74
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhELITNPYSKKikNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQgFNLYPHL--TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLahkKDAF----PSQLSGGQQQRVAIA 148
Cdd:PRK13631 114 LRRRVSMVFQ-FPEYQLFkdTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGL---DDSYlersPFGLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-206 |
6.23e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 151.72 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKtdlNKIREE 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPR---DAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLA--PMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRV 206
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-239 |
7.13e-43 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 149.41 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIR-EEVGFVFQGFNLYPHLTV 94
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP----E 170
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlirtE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 171 MVGEVLKVMkdlAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK10070 203 MQDELVKLQ---AKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-223 |
1.15e-42 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 145.54 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL---ESIESGEIWVDGVNVADP---KTDLNK 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQGFNLYPHLTVLENITLAPMkvkGQN----------AEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQR 144
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGAL---GSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAF 223
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-227 |
4.19e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 144.78 E-value: 4.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVdGVNVADPKT---DLNKIREEVGFVFQgfnlYPHL---- 92
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKknkKLKPLRKKVGIVFQ----FPEHqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 -TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK13634 101 eTVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 171 MVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13634 180 GRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-207 |
4.96e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 142.24 E-value: 4.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTL-----------IRTvnqlesieSGEIWVDGVNVadpk 69
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlaaiagtlspaFSA--------SGEVLLNGRRL---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 70 TDLNKIREEVGFVFQGFNLYPHLTVLENITLA-PMKVKGQNAEQAekkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIA 148
Cdd:COG4136 69 TALPAEQRRIGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRAR---VEQALEEAGLAGFADRDPATLSGGQRARVALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLK-VMKDLAESGMTMMCVTHEMGfAREVADRVI 207
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTHDEE-DAPAAGRVL 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
7.15e-42 |
|
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: 140.26 E-value: 7.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKtdlNKIREEV 79
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR---DARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQgfnlyphltvlenitlapmkvkgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03216 78 AMVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-199 |
1.30e-41 |
|
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: 140.25 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVGFVFQGFN---LYPhl 92
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqlFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLAPMKVKGQNAEqAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMV 172
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAE-VERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*..
gi 488162483 173 GEVLKVMKDLAESGMTMMCVTHEMGFA 199
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-216 |
2.58e-41 |
|
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: 141.06 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNkireevgFVFQGFNLYPHLTVLE 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-------VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 97 NITLAPMKVKGQnAEQAEKKAM--ELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGE 174
Cdd:TIGR01184 74 NIALAVDRVLPD-LSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488162483 175 VL-KVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDK------GQILE 216
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILE 201
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
14-229 |
4.18e-41 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 143.18 E-value: 4.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 14 LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADP-KTDLNKIREEVGFVFQgfNLY--- 89
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQKLLRQKIQIVFQ--NPYgsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 -PHLTVlENITLAPMKVKGQ-NAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:PRK11308 106 nPRKKV-GQILEEPLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 167 LDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-239 |
4.40e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 144.21 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpktdLNKIREEVG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAmELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVN-EMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 161 DEPTSALDPEMVGEV-LKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK11607 174 DEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-225 |
5.86e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 140.68 E-value: 5.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIR--- 76
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRavl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 ---EEVGFVFqgfnlyphlTVLENITL--APMkvkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:PRK13548 82 pqhSSLSFPF---------TVEEVVAMgrAPH---GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 A------MEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
.
gi 488162483 225 T 225
Cdd:PRK13548 230 T 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.07e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 140.75 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD-LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEV 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQG-FNLYPHLTVLENITLAPMKVKGQNAEqAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:PRK13636 85 GMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDE-VRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQF 235
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-236 |
1.31e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 139.80 E-value: 1.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 10 HFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPK----TDLNKIREEVGFVFQG 85
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 86 FNLYPHLTVLENITLaPMKVKGQNAEQAEKKAME-LLERVGL---AHKKDAFP-SQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK14246 99 PNPFPHLSIYDNIAY-PLKSHGIKEKREIKKIVEeCLRKVGLwkeVYDRLNSPaSQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-228 |
1.56e-40 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 139.01 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpkTDL---NKIRE 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI----THLpmhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGF------VFQGfnlyphLTVLENItLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:COG1137 79 GIGYlpqeasIFRK------LTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEmgfARE---VADRVIFVDKGQILEDETPEAFFTNPK 228
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VREtlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
2.99e-40 |
|
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: 137.88 E-value: 2.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDL----HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlnkIR 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHLTVLENITL--APMKVKGQNAEQAEKkamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLE---ELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-224 |
3.49e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 139.49 E-value: 3.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKT-DLNKIREEVGFVFQgfnlYPHL---- 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNkDIKQIRKKVGLVFQ----FPESqlfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 -TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK13649 101 eTVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 171 MVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-227 |
3.58e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 139.55 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 8 HKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFVFQGFN 87
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFVGLVFQNPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 ---LYPhlTVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK13652 89 dqiFSP--TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 165 SALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-228 |
4.44e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 139.58 E-value: 4.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVH------KHFKDLHVINgVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdPKT---DL 72
Cdd:PRK13641 3 IKFENVDyiyspgTPMEKKGLDN-ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHIT-PETgnkNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 73 NKIREEVGFVFQgfnlYPHL-----TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVA 146
Cdd:PRK13641 81 KKLRKKVSLVFQ----FPEAqlfenTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 147 IARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
..
gi 488162483 227 PK 228
Cdd:PRK13641 236 KE 237
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-227 |
4.99e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 138.97 E-value: 4.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD-LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPkTDLNKIREEV 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQ-------GFNLYPHLTV-LENITLAPMKVKgqnaeqaeKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGL 151
Cdd:PRK13644 80 GIVFQnpetqfvGRTVEEDLAFgPENLCLPPIEIR--------KRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGfAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-227 |
7.05e-40 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 140.63 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADP--KTDLNKIREEVGFVFQGFNLYPHLTVLEN 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 98 ITLAPMKVKGQNAEQAEKKAMELLervGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLK 177
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 178 VMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:TIGR02142 173 YLERLhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-214 |
1.29e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 135.85 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpktdLNKIREEVGFVFQgfNLYPHL--- 92
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-----AKERRKSIGYVMQ--DVDYQLftd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLApMKVKGQNAEQAEkkamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMV 172
Cdd:cd03226 88 SVREELLLG-LKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488162483 173 GEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
3.16e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 135.39 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHK-HFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKT-DLNKIREE 78
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-224 |
4.54e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnVADPKTdLNKIREEVGFVFQG-FNLYPHLTV- 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM-VLSEET-VWDVRRQVGMVFQNpDNQFVGATVq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 ------LENItlapmkvkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:PRK13635 101 ddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 169 PEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13635 173 PRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
4.81e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 136.40 E-value: 4.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK---DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvaDPKTDLN--KI 75
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG----DLLTEENvwDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQG-FNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGfarEVA--DRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-217 |
5.84e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 134.91 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpkTDLNKIREE------ 78
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG-------QPLHQMDEEaraklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 ---VGFVFQGFNLYPHLTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK10584 87 akhVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDkGQILED 217
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
7.25e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 135.55 E-value: 7.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIEsGEIWVDG------VNVADPKTDLNKI 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQGFNLYPhLTVLENITLAPM------KVKGQNAEQAEKKAMELLERVGLAHKKDAFpsQLSGGQQQRVAIAR 149
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDK-----GQILEDETPEAF 223
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|...
gi 488162483 224 FTNPKHERAKQFL 236
Cdd:PRK14258 244 FNSPHDSRTREYV 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-240 |
8.92e-39 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 135.32 E-value: 8.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA--DPKTdLNKIREEVGFVFQ----GFNly 89
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQ-RRAFRRDVQLVFQdspsAVN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHLTVlENITLAPMK-VKGQNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSAL 167
Cdd:TIGR02769 103 PRMTV-RQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 168 DPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEdETPEAFFTNPKHERAKQFLQQVM 240
Cdd:TIGR02769 182 DMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE-ECDVAQLLSFKHPAGRNLQSAVL 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-215 |
2.57e-38 |
|
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: 131.90 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIE-SGEIWVDGVNVadpktDLNKIREEVGFVFQGFNLYPHLT 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLGvSGEVLINGRPL-----DKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENITLApMKVKGqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVG 173
Cdd:cd03213 99 VRETLMFA-AKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488162483 174 EVLKVMKDLAESGMTMMCVTH----EMgFarEVADRVIFVDKGQIL 215
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-216 |
3.29e-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: 133.05 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF---KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREE 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD--LNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGfnlyPHL---TVLENITLAPMKVKGQNAEQAEKKA------MELLE----RVGlahkkdAFPSQLSGGQQQRV 145
Cdd:cd03249 79 IGLVSQE----PVLfdgTIAENIRYGKPDATDEEVEEAAKKAnihdfiMSLPDgydtLVG------ERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMkDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQILE 216
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVE 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-227 |
3.70e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.16 E-value: 3.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLH--VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL---ESIESGEIWVDGVNVADpKTDLNkIR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA-KTVWD-IR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQG-FNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFArEVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-236 |
5.80e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 133.37 E-value: 5.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLES-IES----GEIWVDGVNVADPKTDLNKIR 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHlTVLENITLAPmKVKGQNAEQAEKKAMELLERVGLAHKKDAFP---SQLSGGQQQRVAIARGLAM 153
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGA-RINGYKGDMDELVERSLRQAALWDEVKDKLKqsgLSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVD---------KGQILEDETPEAFF 224
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIF 247
|
250
....*....|..
gi 488162483 225 TNPKHERAKQFL 236
Cdd:PRK14243 248 NSPQQQATRDYV 259
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-200 |
6.88e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 132.25 E-value: 6.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV----ADPKTDLNKirEEVGFVFQGFNLYPH 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRN--QKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLENITLaPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEM 171
Cdd:PRK11629 102 FTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|
gi 488162483 172 VGEVLKVMKDL-AESGMTMMCVTHEMGFAR 200
Cdd:PRK11629 181 ADSIFQLLGELnRLQGTAFLVVTHDLQLAK 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-242 |
9.70e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 133.32 E-value: 9.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD-----LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD--PKTDLN 73
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 74 KIREEVGFVFQgfnlYPHL-----TVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAI 147
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESqlfeeTVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
250
....*....|....*
gi 488162483 228 KHERAKQFLQQVMTH 242
Cdd:PRK13643 236 DFLKAHELGVPKATH 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-240 |
1.37e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.50 E-value: 1.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNK-IREEVGFVFQ----GFNlyP 90
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKaFRRDIQMVFQdsisAVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLEnITLAPMK-VKGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:PRK10419 105 RKTVRE-IIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 169 PEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDET--PEAFFTNPkherAKQFLQQVM 240
Cdd:PRK10419 184 LVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTFSSP----AGRVLQNAV 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-215 |
1.38e-37 |
|
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: 131.24 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL---ESIESGEIWVDGVNVaDPKTdlnkIREEVGFVFQGFNL 88
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR-KPDQ----FQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 89 YPHLTVLENITLAP---MKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTS 165
Cdd:cd03234 93 LPGLTVRETLTYTAilrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 166 ALDPEMVGEVLKVMKDLAESGMTMMCVTHEMG---FarEVADRVIFVDKGQIL 215
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-221 |
1.51e-37 |
|
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: 131.20 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD-LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVG 80
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYpHLTVLENITLAPMKVKGQNAEQAEKKAM--ELLERVglahkKDAFPSQ-------LSGGQQQRVAIARGL 151
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQihDKIMRF-----PDGYDTIvgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMgfaREV--ADRVIFVDKGQILEDETPE 221
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHE 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-217 |
1.57e-37 |
|
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: 131.45 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK--DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEV 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA--LADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGfNLYPHLTVLENITLAPMKVKGQNAEQAEKKA------MELLERVGLAHKKDAfpSQLSGGQQQRVAIARGLAM 153
Cdd:cd03252 79 GVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAgahdfiSELPEGYDTIVGEQG--AGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAeSGMTMMCVTHEMGFAREvADRVIFVDKGQILED 217
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
3.21e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 131.36 E-value: 3.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK-----DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpktdlNKI 75
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-------TKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REE-----VGFVFQ----GfnLYPHLTVLENITLAPMKVKGQNAEQAEKKAM-----ELLERV--GLAHKKDAFPSQLSG 139
Cdd:COG1101 74 PEYkrakyIGRVFQdpmmG--TAPSMTIEENLALAYRRGKRRGLRRGLTKKRrelfrELLATLglGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 140 GQQQRVAiargLAM----EPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG1101 152 GQRQALS----LLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
...
gi 488162483 215 LED 217
Cdd:COG1101 228 ILD 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-216 |
5.43e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.59 E-value: 5.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlnkireEVG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-------ERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 161 DEPTSALDP---EMVGEVLkvMKDLAESGMTMMCVTHEMGFAREVADRVIFV--DKGQILE 216
Cdd:PRK11248 153 DEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-221 |
6.90e-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: 135.70 E-value: 6.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDL-----HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWV----DGVNVADPKTD 71
Cdd:TIGR03269 279 IIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 72 LN-KIREEVGFVFQGFNLYPHLTVLENITLA-----PmkvkgqnAEQAEKKAMELLERVGLAHKK-----DAFPSQLSGG 140
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNLTEAiglelP-------DELARMKAVITLKMVGFDEEKaeeilDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 141 QQQRVAIARGLAMEPRVMLFDEPTSALDP-EMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDET 219
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
..
gi 488162483 220 PE 221
Cdd:TIGR03269 512 PE 513
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-239 |
9.45e-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: 135.32 E-value: 9.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIE--SGEI-----------WVD------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIiyhvalcekcgYVErpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 62 -----GVNVADPKTDL--------NKIREEVGFVFQ-GFNLYPHLTVLENItLAPMKVKGQNAEQAEKKAMELLERVGLA 127
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 128 HKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRV 206
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|...
gi 488162483 207 IFVDKGQILEDETPEafftnpkhERAKQFLQQV 239
Cdd:TIGR03269 240 IWLENGEIKEEGTPD--------EVVAVFMEGV 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-236 |
2.80e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 129.11 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKTDLNKIREEVGFVFQGFNLYPHLTVLENI 98
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 99 TLaPMKVKGQNAEQAEKKA-MELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLK 177
Cdd:PRK11831 106 AY-PLREHTQLPAPLLHSTvMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 178 VMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHeRAKQFL 236
Cdd:PRK11831 185 LISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQFL 243
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-221 |
4.93e-36 |
|
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: 134.70 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVGFVFQGFNLYPHlTVL 95
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG--LDVQAVRRQLGVVLQNGRLMSG-SIF 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITL-APMKVKgqnaeqaekKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:TIGR03797 545 ENIAGgAPLTLD---------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRILLFDEA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 164 TSALD---PEMVGEVLKVMKdlaesgMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPE 221
Cdd:TIGR03797 616 TSALDnrtQAIVSESLERLK------VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYD 669
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-225 |
5.95e-36 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 127.51 E-value: 5.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVN-QLESIESGEIWV-----DGVNVADpktdlnk 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLfgerrGGEDVWE------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFV--FQGFNLYPHLTVLE--------NITLaPMKVkgqNAEQaEKKAMELLERVGLAHKKDAFPSQLSGGQQQR 144
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLDvvlsgffdSIGL-YREP---TDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESG-MTMMCVTH---EM--GFarevaDRVIFVDKGQILEDE 218
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAG 225
|
....*..
gi 488162483 219 TPEAFFT 225
Cdd:COG1119 226 PKEEVLT 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-217 |
5.98e-36 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 126.55 E-value: 5.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA--DPKTdlnkIRE 77
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPAD----LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFVFQGfnlyPHL---TVLENITLApmkvkGQNAEQAEkkAMELLERVGLAHKKDAFP-----------SQLSGGQQQ 143
Cdd:cd03245 79 NIGYVPQD----VTLfygTLRDNITLG-----APLADDER--ILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 144 RVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAeSGMTMMCVTHEMGFArEVADRVIFVDKGQILED 217
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-219 |
6.19e-36 |
|
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: 126.96 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEV 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRD--YTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYpHLTVLENITLAPMKVKGQNAEQAEKKA--MELLERV--GLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAAnaHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILEDET 219
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-222 |
2.36e-35 |
|
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: 132.68 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK--DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA--DPKTdlnkIRE 77
Cdd:TIGR03375 464 IEFRNVSFAYPgqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPAD----LRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFVFQGFNLYpHLTVLENITLApmkvkgqnAEQAEKKAM-ELLERVGL----AHKKDAFPSQ-------LSGGQQQRV 145
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG--------APYADDEEIlRAAELAGVtefvRRHPDGLDMQigergrsLSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 146 AIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFArEVADRVIFVDKGQILEDETPEA 222
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQ 685
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-225 |
3.10e-35 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 125.58 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKI---- 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 76 REEVGFVFQ-------GFNLYPHltvlenitlapmkVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIA 148
Cdd:COG4604 81 RQENHINSRltvrelvAFGRFPY-------------SKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIIT 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
3.59e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.39 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD-LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVaDPKTDlNKIREEVG 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENE-KWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQG-----FNLyphlTVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK13647 83 LVFQDpddqvFSS----TVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPE 221
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-226 |
1.29e-34 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 123.84 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlNKIREEVG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERvgLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-239 |
5.11e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 128.43 E-value: 5.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLNKIREEVGFVFQG--FNL 88
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 89 YPHLTVLENItLAPMKVKG-QNAEQAEKKAMELLERVGLAHKKD-AFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:PRK10261 415 DPRQTVGDSI-MEPLRVHGlLPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 167 LDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-216 |
8.57e-34 |
|
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: 128.32 E-value: 8.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEV 79
Cdd:TIGR01846 456 ITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA--IADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGfNLYPHLTVLENITL----APMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:TIGR01846 534 GVVLQE-NVLFSRSIRDNIALcnpgAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILE 216
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAE 671
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-228 |
1.39e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.58 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK-----DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTD--LNK 74
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 IREEVGFVFQgfnlYPHLTVLEN-----ITLAPmKVKGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIA 148
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFEDtvereIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 149 RGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
.
gi 488162483 228 K 228
Cdd:PRK13646 238 K 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-221 |
1.52e-33 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 120.79 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF-KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVG 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD--ISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHlTVLENITLApmkvkGQNAEQAEkkAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIAR 149
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG-----RPNATDEE--VIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPE 221
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHD 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-237 |
1.58e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.36 E-value: 1.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKST----LIRTVNQlesieSGEIWVDGvnvaDPKTDLNK-----IREEVGFVFQG 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDG----QPLHNLNRrqllpVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 86 FN--LYPHLTVLEnITLAPMKV--KGQNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK15134 371 PNssLNPRLNVLQ-IIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQ 237
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-231 |
2.02e-33 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 120.77 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDlNKIREEVGFVFQ 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 165 SALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHER 231
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-240 |
2.07e-33 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 126.70 E-value: 2.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLE---SIESGEIWVDGVnvadpKTDLNKIREEVGFVFQGFNLYPH 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGM-----PIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLENITLAPMKVKGQNAEQAEKKAM--ELLERVGL---AHKKDAFPSQ---LSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:TIGR00955 114 LTVREHLMFQAHLRMPRRVTKKEKRERvdEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 164 TSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMG---FarEVADRVIFVDKGQILEDETPE---AFFTN-----PKHERA 232
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDqavPFFSDlghpcPENYNP 271
|
....*...
gi 488162483 233 KQFLQQVM 240
Cdd:TIGR00955 272 ADFYVQVL 279
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-194 |
2.53e-33 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 125.94 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVGFVFQGfnlyPHL--- 92
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQD----AHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLApmkvkgqNAEQAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:TIGR02868 424 TVRENLRLA-------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|...
gi 488162483 162 EPTSALDPEMVGEVLKVMKDlAESGMTMMCVTH 194
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
2.89e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.18 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLA--PMKVKGQNAEQAEKKAME-LLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAAVErAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERA 232
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAA 235
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-207 |
4.63e-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: 125.09 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLnkIREEVGFVFQgfnlYPHL--- 92
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS--WRDQIAWVPQ----HPFLfag 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLAPMKVKGQNAEQAEKKA--MELLE--RVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:TIGR02857 411 TIAENIRLARPDASDAEIREALERAglDEFVAalPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 488162483 169 PEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVI 207
Cdd:TIGR02857 491 AETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIV 527
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-214 |
8.35e-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: 8.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFVFQGFNLYPHlTVL 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHVGYLPQDDELFSG-SIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENItlapmkvkgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEV 175
Cdd:cd03246 94 ENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 488162483 176 LKVMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQI 214
Cdd:cd03246 136 NQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-226 |
3.27e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 118.96 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-ADPKT--DLNKIREEVGFVFQ--GFN 87
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKikEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 LYPHlTVLENITLAPMKVkGQNAEQAEKKAMELLERVGLAHK-KDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 167 LDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTN 226
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
4.26e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.94 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpKTDLNKIReeVGF 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARAR--IGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENItLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:PRK13536 119 VPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEA 222
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-239 |
5.92e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 119.04 E-value: 5.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI-WVdGVNVAD-PKTDLNKIREEVGFVFQG--FN 87
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWL-GKDLLGmKDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 LYPHLTVLEnITLAPMKV--KGQNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK15079 111 LNPRMTIGE-IIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 165 SALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-226 |
7.35e-32 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 116.34 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIreevGF 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT--RKDLHKI----GS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENitlapMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:TIGR03740 75 LIESPPLYENLTAREN-----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKG------QILEDETPEAFFTN 226
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGvlgyqgKINKSENLEKLFVE 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-214 |
8.09e-32 |
|
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: 114.84 E-value: 8.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHV---INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdPKTDLNKIREEVGFV-----F 83
Cdd:cd03215 8 RGLSVkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT-RRSPRDAIRAGIAYVpedrkR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 84 QGfnLYPHLTVLENITLapmkvkgqnaeqaekkamellervglahkkdafPSQLSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:cd03215 87 EG--LVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 164 TSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-236 |
8.63e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.50 E-value: 8.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 6 NVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESI-----ESGEIWVDGVNVADPKtDLNKIREEVG 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPhLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHK-KDAF---PSQLSGGQQQRVAIARGLAMEPR 156
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvKDRLsdsPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-222 |
2.07e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 117.21 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpkTDLNKIREEVGF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENItLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEA 222
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-239 |
2.10e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.00 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLnkiREE 78
Cdd:PRK11160 339 LTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHlTVLENITLApmkvkgqnAEQA-EKKAMELLERVGLAHKKDAFPS----------QLSGGQQQRVAI 147
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLA--------APNAsDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMgFAREVADRVIFVDKGQILEDETPEAFFTnp 227
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA-- 562
|
250
....*....|..
gi 488162483 228 KHERAKQFLQQV 239
Cdd:PRK11160 563 QQGRYYQLKQRL 574
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-207 |
2.64e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 111.17 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnkiREEVGFVFQGFNL---YPhL 92
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVpdsLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITL---APMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP 169
Cdd:NF040873 73 TVRDLVAMgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 488162483 170 EMVGEVLKVMKDLAESGMTMMCVTHEMGFAREvADRVI 207
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-214 |
3.13e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 9 KHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVaDPKTDLNKIREEVGFV-----F 83
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSPRDAIRAGIAYVpedrkG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 84 QGfnLYPHLTVLENITLAPMKVKGQN---AEQAEKK-AMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG1129 339 EG--LVLDLSIRENITLASLDRLSRGgllDRRRERAlAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 159 LFDEPTSALDpemVG---EVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG1129 417 ILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-236 |
8.60e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.96 E-value: 8.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL-----ESIESGEIWVDGVNV--ADPKTdLNKIR-EEVGFVFQG-- 85
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLlhASEQT-LRGVRgNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 86 FNLYPhltvLENITLAPMKV----KGQNAEQAEKKAMELLERVGL---AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:PRK15134 103 VSLNP----LHTLEKQLYEVlslhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFL 236
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
8.83e-30 |
|
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: 110.66 E-value: 8.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVH-KHFKDLH-VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEV 79
Cdd:cd03244 3 IEFKNVSlRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS--KIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 G------FVFQGfnlyphlTVLENitLAPmkvkgqNAEQAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQ 142
Cdd:cd03244 81 SiipqdpVLFSG-------TIRSN--LDP------FGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 143 QRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDlAESGMTMMCVTHE----MGFarevaDRVIFVDKGQILEDE 218
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFD 219
|
..
gi 488162483 219 TP 220
Cdd:cd03244 220 SP 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-219 |
1.42e-29 |
|
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: 115.97 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtdLNKIREEV 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHlTVLENITL-APMKVKGQNAEQAEKKA--MELLERV--GLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYgRTEQADRAEIERALAAAyaQDFVDKLplGLDTPIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGfAREVADRVIFVDKGQILEDET 219
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
8.02e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.46 E-value: 8.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK--DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREE 78
Cdd:PRK13648 7 IIVFKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD--DNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQG-FNLYPHLTV-------LENITLApmkvkgqnAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARG 150
Cdd:PRK13648 85 IGIVFQNpDNQFVGSIVkydvafgLENHAVP--------YDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
1.22e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFK----------------------DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI 58
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 59 WVDGvNVADPktdLnkireEVGFvfqGFNlyPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAfP-SQL 137
Cdd:COG1134 84 EVNG-RVSAL---L-----ELGA---GFH--PELTGRENIYLN-GRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PvKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 138 SGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....
gi 488162483 218 ETPE 221
Cdd:COG1134 228 GDPE 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-217 |
2.14e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.86 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtdlNKIREEV 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGfnlyPHL---TVLENITLapmkvkgqnaeqaekkamellervglahkkdafpsQLSGGQQQRVAIARGLAMEPR 156
Cdd:cd03247 78 SVLNQR----PYLfdtTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGfAREVADRVIFVDKGQILED 217
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-224 |
2.68e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.26 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFVFQG-FNLYPH 91
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEM 171
Cdd:PRK13642 97 ATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 172 VGEVLKVMKDLAES-GMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFF 224
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-232 |
5.64e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.00 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpKTDLNKIREEVG 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMK----------VKGQNAEQAEKKAMEL----LERVGLAHKKDAFPSQLSGGQQQRVA 146
Cdd:PRK11300 84 RTFQHVRLFREMTVIENLLVAQHQqlktglfsglLKTPAFRRAESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 147 IARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
....*..
gi 488162483 226 NPKHERA 232
Cdd:PRK11300 244 NPDVIKA 250
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
6.15e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVdGVNVadpktdlnkireEVG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGF-NLYPHLTVLENIT-LAPmkvkgqnaEQAEKKAMELLERVGL----AHKKdafPSQLSGGQQQRVAIARGLAME 154
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRdGAP--------GGTEQEVRGYLGRFLFsgddAFKP---VGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 155 PRVMLFDEPTSALDPEMVgEVLKVMkdLAE-SGmTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:COG0488 451 PNVLLLDEPTNHLDIETL-EALEEA--LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
10-229 |
1.67e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 107.13 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 10 HFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKStlirtVNQLESIesGEIWVDGVNVADP----KTDLNKIRE---- 77
Cdd:PRK11022 12 HFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS-----VSSLAIM--GLIDYPGRVMAEKlefnGQDLQRISEkerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 -----EVGFVFQG--FNLYPHLTVLENITLApMKV-KGQNAEQAEKKAMELLERVGL---AHKKDAFPSQLSGGQQQRVA 146
Cdd:PRK11022 85 nlvgaEVAMIFQDpmTSLNPCYTVGFQIMEA-IKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 147 IARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAE-SGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFT 225
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
....
gi 488162483 226 NPKH 229
Cdd:PRK11022 244 APRH 247
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-229 |
2.49e-27 |
|
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: 105.30 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 18 NGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI--------WVDGVNVADPKTDLnKIREEVGFVFQGF--N 87
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaELELYQLSEAERRR-LMRTEWGFVHQNPrdG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 LYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:TIGR02323 99 LRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 167 LDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQH 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-213 |
2.51e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 108.86 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTvnqLESIE-----SGEIWVDGvnvaDPKTDLNkIR--E 77
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKV---LSGVYphgtyEGEIIFEG----EELQASN-IRdtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFV--FQGFNLYPHLTVLENITLA--PMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:PRK13549 81 RAGIAiiHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-227 |
4.85e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.04 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF---KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadPKTDLNKIREE 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHRQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHlTVLENITLAPMKVKGQNAEQAEKKA------MELLErvGLAHKKDAFPSQLSGGQQQRVAIARGLA 152
Cdd:TIGR00958 557 VALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAAnahdfiMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKdlaESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
5.84e-27 |
|
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: 103.38 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF----------------------KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIW 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 60 VDGvNVAdPKTDLNkireevgfvfQGFNlyPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSG 139
Cdd:cd03220 81 VRG-RVS-SLLGLG----------GGFN--PELTGRENIYLN-GRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 140 GQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDE 218
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
6.18e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.40 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD----LHVINGVNLEIKKGEVVVVCGPSGSGKS----TLIRTVNQLES-IESGEIWVDGVN--VAD-- 67
Cdd:PRK10261 12 VLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGlVQCDKMLLRRRSrqVIEls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 68 --PKTDLNKIR-EEVGFVFQG--FNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDA---FPSQLSG 139
Cdd:PRK10261 92 eqSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 140 GQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDE 218
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|.
gi 488162483 219 TPEAFFTNPKHERAKQFLQQV 239
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAV 272
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-216 |
1.10e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.80 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF--KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtdLNKIREEV 79
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYpHLTVLENITLApmkVKGQ-NAEQAEKKA-----MELLERvgLAHKKDAFPSQ----LSGGQQQRVAIAR 149
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYA---RTEQySREQIEEAArmayaMDFINK--MDNGLDTVIGEngvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 150 GLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLaESGMTMMCVTHEMGfAREVADRVIFVDKGQILE 216
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
2.85e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpkTDLNKIREEVg 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD-------KPISMLSSRQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 fvfqgfnLYPHLTVLENITLAPMKVK-------------------GQNAEQAEKKAMELLERVGLAHKKdafPSQLSGGQ 141
Cdd:PRK11231 74 -------LARRLALLPQHHLTPEGITvrelvaygrspwlslwgrlSAEDNARVNQAMEQTRINHLADRR---LTDLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 142 QQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPE 221
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
250
....*....|....*...
gi 488162483 222 AFFTnpkheraKQFLQQV 239
Cdd:PRK11231 224 EVMT-------PGLLRTV 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-239 |
3.18e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 104.04 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHV-----------INGVNLEIKKGEVVVVCGPSGSGKS-TLIRTVNQLES--IESGEIWVDGVNVAD-PKTDLNKIR 76
Cdd:PRK09473 16 KDLRVtfstpdgdvtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNlPEKELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 -EEVGFVFQG--FNLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGL--AHKK-DAFPSQLSGGQQQRVAIARG 150
Cdd:PRK09473 96 aEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMpeARKRmKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSH 255
|
250
....*....|
gi 488162483 230 ERAKQFLQQV 239
Cdd:PRK09473 256 PYSIGLLNAV 265
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-215 |
6.40e-26 |
|
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: 105.12 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvADPKT-DLNKIREEVGFVFQGFNLYPHlTV 94
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG---ADLKQwDRETFGKHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENItlAPMkvkGQNAEqAEK--------KAMELLERVGLAHKKDAFP--SQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:TIGR01842 409 AENI--ARF---GENAD-PEKiieaaklaGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 165 SALDPEmvGE--VLKVMKDLAESGMTMMCVTHEMGfAREVADRVIFVDKGQIL 215
Cdd:TIGR01842 483 SNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIA 532
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-218 |
6.81e-26 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 100.42 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDgvnvadpktdlnkireevgfvFQGFNLYPHLTV 94
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------VPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITlapmkvkgqnAEQAEKKAMELLERVGLAhkkDAF-----PSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP 169
Cdd:COG2401 103 IDAIG----------RKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 170 EMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVA-DRVIFVDKGQILEDE 218
Cdd:COG2401 170 QTAKRVARNLQKLArRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEK 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
9.67e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 9.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI--------WVDGVNVADPKTDLnKIR 76
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRR-LLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQ----GfnLYPHLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKK-DAFPSQLSGGQQQRVAIARGL 151
Cdd:PRK11701 89 TEWGFVHQhprdG--LRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-221 |
1.00e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.53 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHV-------INGVNLEIKKGEVVVVCGPSGSGKSTLIRTV--NQLESIESGEIWVDGVNVADPKTDlNKIREEVGFV 82
Cdd:COG0396 4 KNLHVsvegkeiLKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPD-ERARAGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 83 FQgfnlYP----HLTVLENITLAPMKVKGQ--NAEQAEKKAMELLERVGLAhkkDAFPSQ-----LSGGQQQRVAIARGL 151
Cdd:COG0396 83 FQ----YPveipGVSVSNFLRTALNARRGEelSAREFLKLLKEKMKELGLD---EDFLDRyvnegFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 152 AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHemgFAR----EVADRVIFVDKGQILEDETPE 221
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVKSGGKE 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-217 |
1.07e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 100.48 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 7 VHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvaDPKTDLNKIREEVGFVF-QG 85
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 86 FNLYPHLTVLEniTLAPMK-VKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:cd03267 104 TQLWWDLPVID--SFYLLAaIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 165 SALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
1.38e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.10 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVnvADPKTDlNKIREE-- 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI--NYNKLD-HKLAAQlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTVLENI---TLAPMKVKGQNA---EQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLA 152
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKG 212
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-214 |
2.71e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 101.49 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 6 NVHKHFKDLHVinGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREE--VGFVF 83
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKrrIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 84 QGFNLYPHLTVLENITLApmkVKGQNAEQAEKkAMELLervGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:PRK11144 83 QDARLFPHYKVRGNLRYG---MAKSMVAQFDK-IVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 164 TSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-210 |
3.05e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.07 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 4 FKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdLNKIREEVGFVF 83
Cdd:PRK11288 7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST-TAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 84 QGFNLYPHLTVLENITLAPMKVKGQ--NAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRV-IFVD 210
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKD 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
3.18e-25 |
|
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: 103.36 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVI-NGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAD-PKTDLnkiREEV 79
Cdd:COG5265 358 VRFENVSFGYDPERPIlKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASL---RAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVfqgfnlyPHLTVLENITLA-------PmkvkgqNAEQAE-----KKA-----MELL---------ERvGLahkkdaf 133
Cdd:COG5265 435 GIV-------PQDTVLFNDTIAyniaygrP------DASEEEveaaaRAAqihdfIESLpdgydtrvgER-GL------- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 134 psQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQ 213
Cdd:COG5265 494 --KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
...
gi 488162483 214 ILE 216
Cdd:COG5265 570 IVE 572
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
3.18e-25 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 102.98 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQL--ESIESGEIWVDGvnvADPKTDLNKIREE 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSG---SPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVF--QGFNLYPHLTVLENITLA-PMKVKGQNAEQAE--KKAMELLERVGLAHKKDAFP-SQLSGGQQQRVAIARGLA 152
Cdd:TIGR02633 78 AGIVIihQELTLVPELSVAENIFLGnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 153 MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-197 |
3.85e-25 |
|
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: 97.81 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpkTDLNKIREEVGFVFqgfnLY------ 89
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG-------TPLAEQRDEPHENI----LYlghlpg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 --PHLTVLENIT-LAPMKVKGQNAeqaekkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:TIGR01189 84 lkPELSALENLHfWAAIHGGAQRT------IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|..
gi 488162483 167 LDPEMVGEVLKVMKD-LAESGMTMMCVTHEMG 197
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLARGGIVLLTTHQDLG 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-214 |
4.22e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 4.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 4 FKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnkiREEVGFVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-------------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 84 QGFNLYPHLTVLENI-----TLAPMKVKGQNAEQAEKKAMELLERVG-LAHKKDA------------------FP----- 134
Cdd:COG0488 68 QEPPLDDDLTVLDTVldgdaELRALEAELEELEAKLAEPDEDLERLAeLQEEFEAlggweaearaeeilsglgFPeedld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 135 ---SQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVG---EVLKvmkdlAESGmTMMCVTHEMGFAREVADRVIF 208
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFLK-----NYPG-TVLVVSHDRYFLDRVATRILE 221
|
....*.
gi 488162483 209 VDKGQI 214
Cdd:COG0488 222 LDRGKL 227
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-214 |
4.77e-25 |
|
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: 98.31 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNV---HKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadPKTDLNKIREE 78
Cdd:cd03248 12 VKFQNVtfaYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHlTVLENITLAPMKVKGQNAEQAEKKA-----MELLERvGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFArEVADRVIFVDKGQI 214
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-216 |
5.93e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 5.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVGFVFQGFNLYpHLTVLE 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRNIAVVFQDAGLF-NRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 97 NI-------TLAPMKvkgQNAEQAEkkAMELLERvglahKKDAFP-------SQLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:PRK13657 428 NIrvgrpdaTDEEMR---AAAERAQ--AHDFIER-----KPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 163 PTSALDPEMVGEVlKVMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQILE 216
Cdd:PRK13657 498 ATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVE 549
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
10-194 |
6.62e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.58 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 10 HFKDLHV--------INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWV-DGVNVA----DPKTDLNKIR 76
Cdd:COG4178 364 ALEDLTLrtpdgrplLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqRPYLPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVgfvfqgfnLYPHLTvlENITLAPMKvkgqnaeqaekkamELLERVGLAH------KKDAFPSQLSGGQQQRVAIARG 150
Cdd:COG4178 444 EAL--------LYPATA--EAFSDAELR--------------EALEAVGLGHlaerldEEADWDQVLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDlAESGMTMMCVTH 194
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-231 |
7.07e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.91 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlNKIREEVGFVFQGFNLYPHLTVL 95
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITLA-----PMKVKGQNA-EQAEKKAMellERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDP 169
Cdd:PRK10253 100 ELVARGryphqPLFTRWRKEdEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 170 EMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHER 231
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-220 |
1.07e-24 |
|
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: 102.40 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvADPKTDLNKIREEVGFVFQGFNLYPHLTVLE 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 97 NItLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVL 176
Cdd:TIGR01257 1023 HI-LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488162483 177 KVMKDLaESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETP 220
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-214 |
1.57e-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: 101.36 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRT-VNQLESIeSGEIWVDGVNVAD-PKTDLnkiREEVGFVFQGFNLYPHlT 93
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVWPPT-AGSVRLDGADLSQwDREEL---GRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENItlAPM-KVKGQNAEQAEKKA--MELLERvglahkkdaFP-----------SQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:COG4618 422 IAENI--ARFgDADPEKVVAAAKLAgvHEMILR---------LPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 160 FDEPTSALDPEmvGE--VLKVMKDLAESGMTMMCVTHEMGfAREVADRVIFVDKGQI 214
Cdd:COG4618 491 LDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-207 |
1.89e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA--DPKTdlnkIREE 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEI----YRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHlTVLENITLaPMKVKGQNAEqaEKKAMELLERVGLA-HKKDAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIF-PWQIRNQQPD--PAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEmgfAREV--ADRVI 207
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD---KDEInhADKVI 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-194 |
2.23e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 96.10 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPktdlnKIREEVGFVFQGFNLYPHLTVL 95
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP-----DVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITL-ApmKVKGqnaeQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGE 174
Cdd:PRK13539 92 ENLEFwA--AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|.
gi 488162483 175 VLKVMKD-LAESGMTMMcVTH 194
Cdd:PRK13539 166 FAELIRAhLAQGGIVIA-ATH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
4.38e-24 |
|
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: 93.67 E-value: 4.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnkiREEVGF 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-------------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VfqgfnlyphltvlenitlapmkvkgqnaeqaekkamellervglahkkdafpSQLSGGQQQRVAIARGLAMEPRVMLFD 161
Cdd:cd03221 68 F----------------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 162 EPTSALDPEMVgEVLKVMkdLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:cd03221 96 EPTNHLDLESI-EALEEA--LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-237 |
1.94e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.77 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKS--------TLIRTVNQLesieSGEIWVDGVNVAdpktdLNKIR-EEVGFVFQ--- 84
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaaalgILPAGVRQT----AGRVLLDGKPVA-----PCALRgRKIATIMQnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 -GFNlyPHLTVLENiTLAPMKVKGQNAEQAekKAMELLERVGLAHKK---DAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK10418 90 sAFN--PLHTMHTH-ARETCLALGKPADDA--TLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKHERAKQFLQ 237
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-216 |
2.74e-23 |
|
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: 92.98 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLES--IESGEIWVDGVNVADpktdlnkireev 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 gfvfqgfnLYPHLTVLENITLA---PMKVKGQnaeqaekKAMELLERVGLAhkkdafpsqLSGGQQQRVAIARGLAMEPR 156
Cdd:cd03217 69 --------LPPEERARLGIFLAfqyPPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTH-EMGFAREVADRVIFVDKGQILE 216
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVK 185
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-217 |
2.90e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.89 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEVGFVFQGfnlyPHL--- 92
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFINYLPQE----PYIfsg 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLApmkvKGQNAEQAE-KKAMELLE--------RVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:TIGR01193 563 SILENLLLG----AKENVSQDEiWAACEIAEikddienmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 164 TSALDPEMVGEVLKVMKDLAESgmTMMCVTHEMGFAREVaDRVIFVDKGQILED 217
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQ 689
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-206 |
4.00e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 97.17 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRT---VNQLESIEsGEIWVDGVNVAdpktdLNKIR--EEV 79
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVlsgVYPHGSYE-GEILFDGEVCR-----FKDIRdsEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVF--QGFNLYPHLTVLENITLAPMKVKGQ--NAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:NF040905 79 GIVIihQELALIPYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRV 206
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-216 |
4.18e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdPKTDLNKIREEVGFVFQ-----GF 86
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYITEsrrdnGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 87 nlYPHLTVLENITLAP-MKVKGQNA------EQAEKKAMELlERVGLA---HKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:PRK09700 353 --FPNFSIAQNMAISRsLKDGGYKGamglfhEVDEQRTAEN-QRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 157 VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-232 |
4.51e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 11 FKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLNKIREEVGFVFQGFNLYP 90
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 171 MVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETP-EAFFTNPKHERA 232
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgEVFACTEAMEQA 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-216 |
7.77e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.45 E-value: 7.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIEsGEIWVDGVNVADpkTDLNKIREEVGFVFQGFNLyPHLTVLENIT 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRE--LDPESWRKHLSWVGQNPQL-PHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 100 LApmkvkgqNAEQAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:PRK11174 445 LG-------NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488162483 169 PEMVGEVLKVMKDLAESGMTMMcVTHEMGFAREVaDRVIFVDKGQILE 216
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIVQ 563
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-213 |
1.43e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 91.38 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIeSGEIWVDGvnvadpktdlnkireEVGFVFQgfnlYPHL-- 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELEKL-SGSVSVPG---------------SIAYVSQ----EPWIqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 -TVLENITL-APMkvkgqNAEQAEK--KAMELLERVglahkkDAFPSQ-----------LSGGQQQRVAIARGLAMEPRV 157
Cdd:cd03250 80 gTIRENILFgKPF-----DEERYEKviKACALEPDL------EILPDGdlteigekginLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 158 MLFDEPTSALDPEmVGEVL--KVMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQ 213
Cdd:cd03250 149 YLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-206 |
1.65e-22 |
|
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: 91.02 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtdlNKIREEVGFVFQGFNLYPHLTVL 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITLapmkvkgQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEV 175
Cdd:cd03231 92 ENLRF-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 488162483 176 LKVMKD-LAESGMTMMCVTHEMGFAREVADRV 206
Cdd:cd03231 165 AEAMAGhCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-206 |
7.81e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 7.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdPKTDLNKIREEVG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-RLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKvkgqnAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRV 206
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-222 |
1.04e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.27 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVaDPKtDLNkIREEVGF 81
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAG-DIA-TRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGFNLYPHLTVLENITL-ApmKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIArgLAM--EPRVM 158
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA--VAVihKPELL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFArEVADRVIFVDKGQILEDETPEA 222
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-213 |
1.16e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.14 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKTDlnkirEE 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSS-----QE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 --VGFVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEK---KAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:PRK10762 79 agIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-236 |
1.21e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 11 FKDLHV--INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA----------------DPKTDL 72
Cdd:PRK15112 21 FRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrsqrirmifqDPSTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 73 NKiREEVGfvfqgfnlyphltvleNITLAPMKVKGQ-NAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARG 150
Cdd:PRK15112 101 NP-RQRIS----------------QILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 151 LAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 243
|
....*..
gi 488162483 230 ERAKQFL 236
Cdd:PRK15112 244 ELTKRLI 250
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-199 |
1.75e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 88.32 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpkTDLNKIREEvgfvFQGFNLY--------P 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDE----YHQDLLYlghqpgikT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLApMKVKGQNAEQAekkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK13538 88 ELTALENLRFY-QRLHGPGDDEA---LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|
gi 488162483 171 MVGEVLKVMKD-LAESGMTMMCVTHEMGFA 199
Cdd:PRK13538 164 GVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-216 |
2.43e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.34 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHViNGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIREEV 79
Cdd:PRK10522 323 LELRNVTFAYQDngFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHLTvlenitlapmkvkGQNAEQAEKKAMEL-LERVGLAHK---KDAFPS--QLSGGQQQRVAIARGLAM 153
Cdd:PRK10522 400 SAVFTDFHLFDQLL-------------GPEGKPANPALVEKwLERLKMAHKlelEDGRISnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 154 EPRVMLFDEPTSALDP----EMVGEVLKVMKdlaESGMTMMCVTHEMGFArEVADRVIFVDKGQILE 216
Cdd:PRK10522 467 ERDILLLDEWAADQDPhfrrEFYQVLLPLLQ---EMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-222 |
1.02e-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: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVING-----VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpkTDLNKIR 76
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA--DNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQGFNLYPHLTvlenitlapmkvkGQNAEQAEKKAMELLERVGLAHK----KDAFPS-QLSGGQQQRVAIArgL 151
Cdd:COG4615 406 QLFSAVFSDFHLFDRLL-------------GLDGEADPARARELLERLELDHKvsveDGRFSTtDLSQGQRKRLALL--V 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 AM-EPR-VMLFDEPTSALDP--------EMVGEvLKVMkdlaesGMTMMCVTH-EMGFarEVADRVIFVDKGQILEDETP 220
Cdd:COG4615 471 ALlEDRpILVFDEWAADQDPefrrvfytELLPE-LKAR------GKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGP 541
|
..
gi 488162483 221 EA 222
Cdd:COG4615 542 AA 543
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-229 |
1.25e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 88.81 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 14 LHVINGVNLEIKKGEVVVVCGPSGSGKS----TLIRTVNQLESIESGEIWVDGVNVAD--PKTDLNKIREEVGFVFQ--G 85
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKlsPRERRKIIGREIAMIFQepS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 86 FNLYPHLTV----LENITLAPMKVK-GQNAEQAEKKAMELLERVGLA-HKK--DAFPSQLSGGQQQRVAIARGLAMEPRV 157
Cdd:COG4170 100 SCLDPSAKIgdqlIEAIPSWTFKGKwWQRFKWRKKRAIELLHRVGIKdHKDimNSYPHELTEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLAE-SGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHH 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
3.22e-20 |
|
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: 85.16 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKN-VHKHFKDL-HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEV 79
Cdd:cd03369 7 IEVENlSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGFNLYPHlTVLENitLAPMKvkgqnaEQAEKKAMELLERVGLAhkkdafpSQLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSN--LDPFD------EYSDEEIYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 160 FDEPTSALDPEMVGEVLKVMKDLAeSGMTMMCVTHEMgfaREVA--DRVIFVDKGQILEDETP 220
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEF-TNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-217 |
3.53e-20 |
|
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: 88.73 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIESGEIWVDGVNVaDPKTDLNKIREEVGFVFQG---FNLYPHL 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLAPMK---VKGQNAEQAEKKAmeLLERVGLAHKKDAFP----SQLSGGQQQRVAIARGLAMEPRVMLFDEPTS 165
Cdd:TIGR02633 355 GVGKNITLSVLKsfcFKMRIDAAAELQI--IGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 166 ALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-195 |
6.30e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.40 E-value: 6.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 3 KFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIE-SGEIWVDGVNVADPktdlnkIREEVG 80
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTILANNRKPTKQ------ILKRTG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENITLAPMKVKGQNAEQAEKK--AMELLERVGLAHKKD-----AFPSQLSGGQQQRVAIARGLAM 153
Cdd:PLN03211 144 FVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKIlvAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHE 195
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-229 |
1.08e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.01 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLeSIESGEIWVDGVNVAD-------PKTDLNKIREEVGFVFQgfnl 88
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDidllrlsPRERRKLVGHNVSMIFQ---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 89 YPH--LTVLENITLAPMKV------KG---QNAEQAEKKAMELLERVGLAHKKDA---FPSQLSGGQQQRVAIARGLAME 154
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNipgwtyKGrwwQRFGWRKRRAIELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAE-SGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNPKH 229
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-196 |
4.15e-19 |
|
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: 85.61 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 25 KKGEVVVVCGPSGSGKSTLIRtvnqlesIESGEIwvdGVNVADPKTDLNKirEEVGFVFQGFNLYPHLTVLEN------- 97
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-------ILSGEL---KPNLGDYDEEPSW--DEVLKRFRGTELQDYFKKLANgeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 98 ----ITLAPMKVKGQNAEQAEK-----KAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:COG1245 165 kpqyVDLIPKVFKGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 488162483 169 pemVGE---VLKVMKDLAESGMTMMCVTHEM 196
Cdd:COG1245 245 ---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
8.33e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 8.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHF-------------KDL--------HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTvnqLESI---ESG 56
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalKGLfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM---LTGIlvpTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 57 EIWVDGVnvaDPKTDLNKIREEVGFVF-QGFNLYPHLTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPS 135
Cdd:COG4586 78 EVRVLGY---VPFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLL-KAIYRIPDAEYKKRLDELVELLDLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 136 QLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL-AESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
...
gi 488162483 215 LED 217
Cdd:COG4586 234 IYD 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-226 |
3.28e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK-DLH-VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEV 79
Cdd:PLN03130 1238 IKFEDVVLRYRpELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFV------FQG---FNLYPHltvlenitlapmkvkgqnAEQAEKKAMELLERvglAHKKDAFP--------------SQ 136
Cdd:PLN03130 1316 GIIpqapvlFSGtvrFNLDPF------------------NEHNDADLWESLER---AHLKDVIRrnslgldaevseagEN 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 137 LSGGQQQRVAIARGLAMEPRVMLFDEPTSALDpemVGEVLKVMKDLAES--GMTMMCVTHEMGFAREvADRVIFVDKGQI 214
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
250
....*....|..
gi 488162483 215 LEDETPEAFFTN 226
Cdd:PLN03130 1451 VEFDTPENLLSN 1462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-214 |
4.48e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.74 E-value: 4.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKTDLNKireevGFVF-----QGFNLY 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLAN-----GIVYisedrKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHLTVLENITLAPM----KVKGQNAEQAEKKAMEllervglaHKKDAF----PSQ------LSGGQQQRVAIARGLAMEP 155
Cdd:PRK10762 343 LGMSVKENMSLTALryfsRAGGSLKHADEQQAVS--------DFIRLFniktPSMeqaiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 156 RVMLFDEPTSALDpemVG---EVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK10762 415 KVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-214 |
5.46e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 14 LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlNKIREE-VGFV---FQGFNLY 89
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP--RERRRLgVAYIpedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHLTVLENITL-----APMKVKG-QNAEQAEKKAMELLERVGL-AHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:COG3845 349 PDMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 163 PTSALDpemVG---EVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:COG3845 429 PTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-214 |
7.30e-18 |
|
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: 78.84 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIES--GEIWVDGVnvaDPKTDLNKIREEVGFVFQGFNLYPHLT 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGI---PYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENITLApMKVKGqnaeqaekkamellervglahkkDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVG 173
Cdd:cd03233 100 VRETLDFA-LRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488162483 174 EVLKVMKDLA-ESGMT-MMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:cd03233 156 EILKCIRTMAdVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-168 |
8.71e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.77 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnKIReeVG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPH--LTVLENITLAPmkvkgqnaeqAEKKA--MELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:PRK09544 71 YVPQKLYLDTTlpLTVNRFLRLRP----------GTKKEdiLPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 488162483 157 VMLFDEPTSALD 168
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-210 |
9.87e-18 |
|
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: 79.37 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 23 EIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVA------DPKTDLnKIREEVGFVFQGFNLYPHLtvlE 96
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyiKADYEG-TVRDLLSSITKDFYTHPYF---K 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 97 NITLAPMKVKGqnaeqaekkameLLERVGLahkkdafpsQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVL 176
Cdd:cd03237 97 TEIAKPLQIEQ------------ILDREVP---------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMAS 155
|
170 180 190
....*....|....*....|....*....|....*
gi 488162483 177 KVMKDLAESG-MTMMCVTHEMGFAREVADRVIFVD 210
Cdd:cd03237 156 KVIRRFAENNeKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-232 |
3.01e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDlhvingVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKTDLNKI--RE 77
Cdd:PRK15056 14 VTWRNGHTALRD------ASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVAYVpqSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFVFQgfnlyphlTVLENITL----APMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAM 153
Cdd:PRK15056 88 EVDWSFP--------VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 154 EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVdKGQILEDETPEAFFTNPKHERA 232
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELA 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-215 |
4.13e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESiESGEIWVDGVNVAD-PKTDLNKIReevGFVFQGFNLYPHLTVLEN 97
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwSAAELARHR---AYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 98 ITL-APmkvKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIAR-------GLAMEPRVMLFDEPTSALDP 169
Cdd:COG4138 90 LALhQP---AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488162483 170 EMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQIL 215
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-196 |
5.65e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 24 IKKGEVVVVCGPSGSGKSTLIRtvnqlesIESGEIwvdgV-NVADPKTDLNKirEEVGFVFQGFNLYPHLTVLEN----- 97
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGEL----IpNLGDYEEEPSW--DEVLKRFRGTELQNYFKKLYNgeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 98 ------ITLAPMKVKGQNAEQAEK-----KAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:PRK13409 163 vhkpqyVDLIPKVFKGKVRELLKKvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190
....*....|....*....|....*....|...
gi 488162483 167 LDpemVGE---VLKVMKDLAEsGMTMMCVTHEM 196
Cdd:PRK13409 243 LD---IRQrlnVARLIRELAE-GKYVLVVEHDL 271
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-226 |
8.15e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 79.25 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD--LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREE 78
Cdd:PLN03232 1234 SIKFEDVHLRYRPglPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHlTVLENITlaPMkvkgqnAEQAEKKAMELLERvglAHKKDAFP--------------SQLSGGQQQR 144
Cdd:PLN03232 1312 LSIIPQSPVLFSG-TVRFNID--PF------SEHNDADLWEALER---AHIKDVIDrnpfgldaevseggENFSVGQRQL 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFF 224
Cdd:PLN03232 1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELL 1457
|
..
gi 488162483 225 TN 226
Cdd:PLN03232 1458 SR 1459
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-214 |
8.64e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIESGEIWVDGVNVaDPKTDLNKIREEVGFVFQG---FNLYPH 91
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV-KIRNPQQAIAQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLENITLAPM-KVKGQNAEQAEKKAMELLERVGLAHKKDAFP----SQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:PRK13549 356 MGVGKNITLAALdRFTGGSRIDDAAELKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 167 LDpemVG---EVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK13549 436 ID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-212 |
2.00e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 74.59 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLE--SIESGEIWVDGVnvadPKTDlnKIREEVGFVFQGFNLY 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILINGR----PLDK--NFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHLTVLENITLAPmkvkgqnaeqaekkameLLERVGLAHKKdafpsqlsggqqqRVAIARGLAMEPRVMLFDEPTSALDP 169
Cdd:cd03232 92 PNLTVREALRFSA-----------------LLRGLSVEQRK-------------RLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488162483 170 EMVGEVLKVMKDLAESGMTMMCVTHEMG---FarEVADRVIFVDKG 212
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHQPSasiF--EKFDRLLLLKRG 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-194 |
3.91e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.50 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvaDPKTDLNKIReEVGFVFQGFNLYPHL 92
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSR-FMAYLGHLPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLApMKVKGQNAEQAEKKAMELlerVGLAHKKDAFPSQLSGGQQQRVAIARgLAMEPRVM-LFDEPTSALDPEM 171
Cdd:PRK13543 98 STLENLHFL-CGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLEG 172
|
170 180
....*....|....*....|...
gi 488162483 172 VGEVLKVMKDLAESGMTMMCVTH 194
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-222 |
4.53e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 27 GEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTDLnkIREEVGFVFQGFNLYPHLTVLENITLA----- 101
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEGMTVRELVAIGrypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 102 -PMKVKGQNAEQAEKKAMELLERVGLAHKkdaFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMK 180
Cdd:PRK10575 115 gALGRFGAADREKVEEAISLVGLKPLAHR---LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVH 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488162483 181 DLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEA 222
Cdd:PRK10575 192 RLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-242 |
4.67e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHK----HFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTvnqlesiESGEIWVDGVNVADpkTDLNKIRE 77
Cdd:PTZ00265 1226 IVFKNEHTndmtNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFK-------NSGKILLDGVDICD--YNLKDLRN 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFVFQGFNLYpHLTVLENITLAPMKVKGQNAEQAEKKAM--ELLErvGLAHKKDA----FPSQLSGGQQQRVAIARGL 151
Cdd:PTZ00265 1297 LFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAidEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIARAL 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 152 AMEPRVMLFDEPTSALDP---EMVGEVLKVMKDLAESgmTMMCVTHEMGFAREvADRVIfvdkgqiledetpeaFFTNPk 228
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIASIKR-SDKIV---------------VFNNP- 1434
|
250
....*....|....
gi 488162483 229 hERAKQFLQQVMTH 242
Cdd:PTZ00265 1435 -DRTGSFVQAHGTH 1447
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-169 |
5.69e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.70 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlnkiREEVG- 80
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH-----RRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 ---FVFQGF--NLYPHLTVLENI----TLApmkvkGQNAEQAEKKAMELLERVGLAhkkdAFPS----QLSGGQQQRVAI 147
Cdd:NF033858 77 riaYMPQGLgkNLYPTLSVFENLdffgRLF-----GQDAAERRRRIDELLRATGLA----PFADrpagKLSGGMKQKLGL 147
|
170 180
....*....|....*....|..
gi 488162483 148 ARGLAMEPRVMLFDEPTSALDP 169
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDP 169
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-240 |
6.18e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIrtvnqleSIESGEIwvdgvnvaDPKTDLN-KIREEVGFVFQG---FNL 88
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI-------SAMLGEL--------PPRSDASvVIRGTVAYVPQVswiFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 89 yphlTVLENITL-APMkvkgqNAEQAEKKamelLERVGLAHKKDAFPS-----------QLSGGQQQRVAIARGLAMEPR 156
Cdd:PLN03130 694 ----TVRDNILFgSPF-----DPERYERA----IDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 157 VMLFDEPTSALDPEMVGEVL-KVMKDlAESGMTMMCVTHEMGFAREVaDRVIFVDKGQILEDETPEAFFTNPKherakqF 235
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRQVFdKCIKD-ELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGP------L 832
|
....*
gi 488162483 236 LQQVM 240
Cdd:PLN03130 833 FQKLM 837
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-217 |
9.81e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.16 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlnkIREEVGF 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRA----LRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 ---VFQGFNlyPHLTVLENITLAPMKVKgQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:NF000106 90 hrpVR*GRR--ESFSGRENLYMIGR*LD-LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILED 217
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-214 |
9.85e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 9.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 22 LEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG-VNVA----DPKtdlnkiREEVGFVF---------QGFN 87
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVArlqqDPP------RNVEGTVYdfvaegieeQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 88 L--YPHLTVL-------ENIT-LAPM--KVKGQNAEQAEKKAMELLERVGLahKKDAFPSQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK11147 98 LkrYHDISHLvetdpseKNLNeLAKLqeQLDHHNLWQLENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESgmtMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-194 |
1.07e-15 |
|
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: 72.19 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 21 NLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnkiREEVGFVFQgfnlYPHLTVLeniTL 100
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-------------GEDLLFLPQ----RPYLPLG---TL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 101 ApmkvkgqnaeqaekkamELLervglahkkdAFPSQ--LSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKV 178
Cdd:cd03223 81 R-----------------EQL----------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 488162483 179 MKDLaesGMTMMCVTH 194
Cdd:cd03223 134 LKEL---GITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-226 |
1.22e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRT-VNQLESIESGEIWVDGVNVADPktdlnkireEVGFVFQGfnlyphlTVL 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVP---------QVSWIFNA-------TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITLapmkvkGQNAEqaEKKAMELLERVGLAHKKDAFPSQ-----------LSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PLN03232 697 ENILF------GSDFE--SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488162483 165 SALDPEMVGEVL-KVMKDLAEsGMTMMCVTHEMGFAREVaDRVIFVDKGQILEDETPEAFFTN 226
Cdd:PLN03232 769 SALDAHVAHQVFdSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-216 |
1.26e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKtdLNKIREEVGFVFQgfnlYPHL--- 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--LDSWRSRLAVVSQ----TPFLfsd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENITLAPMKVKGQNAEQAEKKA--------------MELLERvGLahkkdafpsQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:PRK10789 404 TVANNIALGRPDATQQEIEHVARLAsvhddilrlpqgydTEVGER-GV---------MLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAEsGMTMMCVTHEMGFAREvADRVIFVDKGQILE 216
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTE-ASEILVMQHGHIAQ 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-213 |
2.03e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVaDPKTDLNKIREEVGFVFQ 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 85 GFNLYPHLTVLENITLAPMKVKGQNAEQAE--KKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-214 |
8.88e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDG--VNVADPKTDLN-------KIREEVGFVfqgfnlyP 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRagimlcpEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITL------APMKV---KGQNAEQAEKKAMELleRVglahkKDAFPSQ----LSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK11288 345 VHSVADNINIsarrhhLRAGClinNRWEAENADRFIRSL--NI-----KTPSREQlimnLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 158 MLFDEPTSALDpemVG---EVLKVMKDLAESGMTMMCVTHE----MGfareVADRVIFVDKGQI 214
Cdd:PRK11288 418 ILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRI 474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-220 |
1.18e-14 |
|
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: 73.06 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK---DLhVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREE 78
Cdd:TIGR00957 1285 VEFRNYCLRYRedlDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--KIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVFQGFNLYPHLTvleNITLAPMkvkGQNAEQAEKKAMEllervgLAHKKDAFPSQ--------------LSGGQQQR 144
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSL---RMNLDPF---SQYSDEEVWWALE------LAHLKTFVSALpdkldhecaeggenLSVGQRQL 1429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREVAdRVIFVDKGQILEDETP 220
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAP 1503
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-229 |
1.24e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 11 FKDLHVI-NGVNLEIKKGEVVVVCGPSGSGKSTLIRTV--NQLESIES------GEIWVDGVNVAD-PKTDLNKIRE--- 77
Cdd:PRK13547 10 ARRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPrgarvtGDVTLNGEPLAAiDAPRLARLRAvlp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 ---EVGFVFQGFNL-----YPHltvlenitlapMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIAR 149
Cdd:PRK13547 90 qaaQPAFAFSAREIvllgrYPH-----------ARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAM---------EPRVMLFDEPTSALDPEMVGEVLKVMKDLA-ESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDET 219
Cdd:PRK13547 159 VLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|
gi 488162483 220 PEAFFTnPKH 229
Cdd:PRK13547 239 PADVLT-PAH 247
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-213 |
2.56e-14 |
|
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: 68.50 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLIrtvnqLESI-ESGEIWVDGvnvADPKTDLNKIreevgfVFQGfnlypHLT 93
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLyASGKARLIS---FLPKFSRNKL------IFID-----QLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENITLAPMKVkGQNAeqaekkamellervglahkkdafpSQLSGGQQQRVAIARGLAMEPR--VMLFDEPTSALDPEM 171
Cdd:cd03238 70 FLIDVGLGYLTL-GQKL------------------------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488162483 172 VGEVLKVMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKGQ 213
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-227 |
3.18e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLI-RTVNQLESieSGEIWVDGVNVAD-PKTDLNKIR------EEVGF---VFQGFNL 88
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLLPG--SGSIQFAGQPLEAwSAAELARHRaylsqqQTPPFampVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 89 YPHltvlenitlapmkvKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIA-------RGLAMEPRVMLFD 161
Cdd:PRK03695 93 HQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 162 EPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILEDETPEAFFTNP 227
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-214 |
3.85e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.24 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADPKTdlnKIREEVGFVF-----QGFNLYPHLTV 94
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITLAPMKVKGQNAEQAEKKAmeLLER------VGLAHKKDAFPSqLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPARENA--VLERyrralnIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488162483 169 PEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
4.85e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.99 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKD--LHVINGvnlEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDgVNVA-DP---KTDlnk 74
Cdd:PRK13409 340 LVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISyKPqyiKPD--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 ireevgfvfqgfnlyPHLTVLENItlapMKVKGQNAEQAEKKamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAME 154
Cdd:PRK13409 413 ---------------YDGTVEDLL----RSITDDLGSSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRD 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488162483 155 PRVMLFDEPTSALDPEMVGEVLKVMKDLAE-SGMTMMCVTHEMGFAREVADRVI 207
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIYMIDYISDRLM 525
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-237 |
5.21e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 24 IKKGEVVVVCGPSGSGKSTLIRTV----NQLESIESGEIWVDGVNVADPKtdlNKIREEVGFVFQGFNLYPHLTVLENI- 98
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIK---KHYRGDVVYNAETDVHFPHLTVGETLd 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 99 TLAPMK-----VKGQNAEQAEKKAMELLERV-GLAHKKDA-----FPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSAL 167
Cdd:TIGR00956 161 FAARCKtpqnrPDGVSREEYAKHIADVYMATyGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 168 DPEMVGEVLKVMKDLA-ESGMT-MMCVTHEMGFAREVADRVIFVDKGQILedetpeaFFTNPKHerAKQFLQ 237
Cdd:TIGR00956 241 DSATALEFIRALKTSAnILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQI-------YFGPADK--AKQYFE 303
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-194 |
8.07e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV--NQLESIESGEIWVDGVNVADPKTDlnkIREE 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE---ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGfVFQGFNlYP-HLTVLENITLAPM----KVKGQNAEQAE-----KKAMELLERVGLahkKDAFPSQ-----LSGGQQQ 143
Cdd:CHL00131 84 LG-IFLAFQ-YPiEIPGVSNADFLRLaynsKRKFQGLPELDpleflEIINEKLKLVGM---DPSFLSRnvnegFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 144 RVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTH 194
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-213 |
8.51e-14 |
|
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: 69.96 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWV-DGVNVadpktdlnkireevGFVFQGFNLYPHLT 93
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV--------------GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENITLAPMKVKGQ---------------------NAEQAE-------KKAMEL---LERVGLAHK---KDAFPSQLSG 139
Cdd:TIGR03719 85 VRENVEEGVAEIKDAldrfneisakyaepdadfdklAAEQAElqeiidaADAWDLdsqLEIAMDALRcppWDADVTKLSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 140 GQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVG--EvlkvmKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-194 |
1.09e-13 |
|
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: 69.78 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVhkhfkDL------HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNV-----ADPK 69
Cdd:TIGR00954 451 GIKFENI-----PLvtpngdVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKlfyvpQRPY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 70 TDLNKIREEVgfvfqgfnLYPHlTVLEnitlapMKVKG---QNAEQ--AEKKAMELLER-VGLAHKKDaFPSQLSGGQQQ 143
Cdd:TIGR00954 526 MTLGTLRDQI--------IYPD-SSED------MKRRGlsdKDLEQilDNVQLTHILEReGGWSAVQD-WMDVLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488162483 144 RVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLaesGMTMMCVTH 194
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-207 |
1.91e-13 |
|
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: 69.04 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKD--LHVINGvnlEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDgVNVA-DPKTDLNKIREE 78
Cdd:COG1245 342 VEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISyKPQYISPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 79 VGFVfqgfnLYPHLTvlENITLAPMKVkgqnaeqaekkamELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVM 158
Cdd:COG1245 418 VEEF-----LRSANT--DDFGSSYYKT-------------EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDLAES-GMTMMCVTHEMGFAREVADRVI 207
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-231 |
2.34e-13 |
|
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: 67.39 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 25 KKGEVVVVCGPSGSGKSTLIRtvnqlesIESGEIwVDGVNVADPKTDLNKIREEvgfvFQGFNLYPHLTVL--------- 95
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALK-------ILAGKL-KPNLGKFDDPPDWDEILDE----FRGSELQNYFTKLlegdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 --ENITLAPMKVKGQNAEQAEKKAM-----ELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALD 168
Cdd:cd03236 92 kpQYVDLIPKAVKGKVGELLKKKDErgkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 169 PEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADrVIFVDKGqiledeTPEAF--FTNPKHER 231
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSD-YIHCLYG------EPGAYgvVTLPKSVR 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
2.38e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpKTDLNKIREEVG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI---KKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 81 FVFQGFNLYPHLTVLENiTLAPMKVKGQNAEqaekkAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PRK13540 78 FVGHRSGINPYLTLREN-CLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHE 195
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-212 |
2.72e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLES---IESGEIWVDGvnvadPKTDLNKIREeVGFVFQGFNLY 89
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNG-----RPLDSSFQRS-IGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHLTVLENITLAPMKVKGQNAEQAEK-----KAMELLERVGLAHKKDAFPSQ-LSGGQQQRVAIARGLAMEPRVMLF-DE 162
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKmeyveEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDE 928
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHE---MGFarEVADRVIFVDKG 212
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLADHGQAILCTIHQpsaILF--EEFDRLLLLQKG 979
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
3.98e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 68.43 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIEsGEIWVDGVNVADPKTDL---NKIREEVGFvfqGFNLYP-- 90
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVE-GHVHMKGSVAYVPQQAWiqnDSLRENILF---GKALNEky 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLAP---MKVKGQNAEQAEKKAmellervglahkkdafpsQLSGGQQQRVAIARGLAMEPRVMLFDEPTSAL 167
Cdd:TIGR00957 730 YQQVLEACALLPdleILPSGDRTEIGEKGV------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 168 DPEMVGEVLKvmKDLAESGM----TMMCVTHEMGFAREVaDRVIFVDKGQILE 216
Cdd:TIGR00957 792 DAHVGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-231 |
7.54e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHF---KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWV-DGVNVADpkTDLNKIRE 77
Cdd:PTZ00265 383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKD--INLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 78 EVGFVFQGFNLYPHlTVLENITLAPMKVK-----------GQNAEQAEKKA---------------MELLERVGLAHKK- 130
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKdlealsnyyneDGNDSQENKNKrnscrakcagdlndmSNTTDSNELIEMRk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 131 -----------------------DAFP-----------SQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVL 176
Cdd:PTZ00265 540 nyqtikdsevvdvskkvlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 177 KVMKDLA--ESGMTMMcVTHEMGFAREVadRVIFV----------DKGQILEDETPEAFFTNPKHER 231
Cdd:PTZ00265 620 KTINNLKgnENRITII-IAHRLSTIRYA--NTIFVlsnrergstvDVDIIGEDPTKDNKENNNKNNK 683
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-212 |
8.71e-13 |
|
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: 65.43 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 13 DLHVINGVNLEIKKGEVVVVCGPSGSGKSTLI-RTVNQLESIESGEIWVDGVNVADPKTDLNKI-REEVGFVFQGFNLYp 90
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYSVAYAAQKPWLL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLapmkvkGQNAEQAEKKAmeLLERVGLAHKKDAFPS-----------QLSGGQQQRVAIARGLAMEPRVML 159
Cdd:cd03290 92 NATVEENITF------GSPFNKQRYKA--VTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 160 FDEPTSALDPEMVGEVLK--VMKDLAESGMTMMCVTHEMGFAREvADRVIFVDKG 212
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-212 |
1.76e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.58 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 24 IKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpkTDLNKIREEVGFVFQGFNLYPHLTVLENITLAPm 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA- 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 104 KVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLA 183
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 488162483 184 ESGMTMMCVTHEMGFAREVADRVIFVDKG 212
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
15-207 |
2.29e-12 |
|
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: 64.20 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTL----IRTVNQLESIES---------GEI------WVDGVNVA---DPKTDL 72
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtIYAEGQRRYVESlsayarqflGQMdkpdvdSIEGLSPAiaiDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 73 NKIREEVGFVFQgfnLYPHLTVLEnitlapmkvkgqnAEQAEKKAMELLERVGLAH---KKDAfpSQLSGGQQQRVAIAR 149
Cdd:cd03270 89 RNPRSTVGTVTE---IYDYLRLLF-------------ARVGIRERLGFLVDVGLGYltlSRSA--PTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 150 GLAMEPRVML--FDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREvADRVI 207
Cdd:cd03270 151 QIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
4.26e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIwvdgvnvadpktdlnKIREEV-- 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI---------------KIGETVkl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 80 GFVFQGF-NLYPHLTVLENIT--LAPMKV----------------KGqnAEQaEKKamellerVGlahkkdafpsQLSGG 140
Cdd:PRK11819 390 AYVDQSRdALDPNKTVWEEISggLDIIKVgnreipsrayvgrfnfKG--GDQ-QKK-------VG----------VLSGG 449
|
170 180 190
....*....|....*....|....*....|
gi 488162483 141 QQQRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
8-214 |
4.34e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 8 HKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV--NQLESIESGEIWVDGVNVadpktDLNKIREEVG----F 81
Cdd:NF040905 267 HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEV-----DVSTVSDAIDaglaY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQ-----GFNLypHLTVLENITLAPMK------VKGQNAEQ--AEK-------KAMELLERVGlahkkdafpsQLSGGQ 141
Cdd:NF040905 342 VTEdrkgyGLNL--IDDIKRNITLANLGkvsrrgVIDENEEIkvAEEyrkkmniKTPSVFQKVG----------NLSGGN 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 142 QQRVAIARGLAMEPRVMLFDEPTSALDpemVG---EVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-242 |
4.92e-12 |
|
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: 64.11 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIEsGEIWVDGVNVAdpKTDLNKIREEVG------FVFQGfnly 89
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWN--SVPLQKWRKAFGvipqkvFIFSG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 phlTVLENitLAPmkvkgqNAEQAEKKAMELLERVGLAHKKDAFPSQL-----------SGGQQQRVAIARGLAMEPRVM 158
Cdd:cd03289 92 ---TFRKN--LDP------YGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 159 LFDEPTSALDPEMVGEVLKVMKDlAESGMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFFTNpkheraKQFLQQ 238
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE------KSHFKQ 232
|
....
gi 488162483 239 VMTH 242
Cdd:cd03289 233 AISP 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-239 |
7.34e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvaDPKTDLNK--IREEVGFVFQGfnly 89
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----RPLSSLSHsvLRQGVAMVQQD---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 90 PHL---TVLENITLapmkvkGQNAeqAEKKAMELLERVGLAHKKDAFP-----------SQLSGGQQQRVAIARGLAMEP 155
Cdd:PRK10790 424 PVVladTFLANVTL------GRDI--SEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMKDLAESgMTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFFTnpKHERAKQF 235
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA--AQGRYWQM 571
|
....*.
gi 488162483 236 --LQQV 239
Cdd:PRK10790 572 yqLQLA 577
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-180 |
8.18e-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: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIEsGEIWVDGVNVAdpKTDLNKIREEVG------FVFQG---F 86
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWN--SVTLQTWRKAFGvipqkvFIFSGtfrK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 87 NLYPHltvlenitlapmkvkgqnAEQAEKKAMELLERVGLAHKKDAFPSQL-----------SGGQQQRVAIARGLAMEP 155
Cdd:TIGR01271 1311 NLDPY------------------EQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372
|
170 180
....*....|....*....|....*
gi 488162483 156 RVMLFDEPTSALDPEMVGEVLKVMK 180
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLK 1397
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-210 |
8.45e-12 |
|
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: 61.82 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 23 EIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpktdlnkireevgfvfqgfnlyphltvlenitLAP 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV---------------------------------YKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 103 MKVKgqnaeqaekkamellervglahkkdafpsqLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDL 182
Cdd:cd03222 68 QYID------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 488162483 183 AESGM-TMMCVTHEMGFAREVADRVIFVD 210
Cdd:cd03222 118 SEEGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
9.24e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVdGVNVadpktdlnkireEVGF 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 82 VFQGF-NLYPHLTVLENIT--LAPMKV----------------KGQNAEQaekkamelleRVGlahkkdafpsQLSGGQQ 142
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISggLDIIKLgkreipsrayvgrfnfKGSDQQK----------KVG----------QLSGGER 449
|
170 180
....*....|....*....|....*...
gi 488162483 143 QRVAIARGLAMEPRVMLFDEPTSALDPE 170
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
16-224 |
2.75e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 61.85 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFVFQG---------F 86
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS--KLPLHTLRSRLSIILQDpilfsgsirF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 87 NLYPHLTVLENITLAPMKVkgqnaeqAEKKAMELLERVGLahkkDAFPSQ----LSGGQQQRVAIARGLAMEPRVMLFDE 162
Cdd:cd03288 114 NLDPECKCTDDRLWEALEI-------AQLKNMVKSLPGGL----DAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 163 PTSALDpeMVGE-VLK--VMKDLAESgmTMMCVTHEMGFAREvADRVIFVDKGQILEDETPEAFF 224
Cdd:cd03288 183 ATASID--MATEnILQkvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
1.63e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV---------NQL----ESIESGE-IWvdgvnvad 67
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgRRRGSGEtIW-------- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 68 pktdlnKIREEVGFVFQGFNL-YPHLTVLENITLA----PMKVKGQNAEQAEKKAMELLERVGLAHK--KDAFPSqLSGG 140
Cdd:PRK10938 333 ------DIKKHIGYVSSSLHLdYRVSTSVRNVILSgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRtaDAPFHS-LSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 141 QQQRVAIARGLAMEPRVMLFDEPTSALDP---EMVGEVLKVMkdLAESGMTMMCVTHEMGFARE-VADRVIFVDKGQI 214
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVL--ISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-213 |
2.87e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 32 VCGPSGSGKSTLIRTVNQLESIESGEIWV-DGVNVadpktdlnkireevGFVFQGFNLYPHLTVLENITLAPMKVKGQ-- 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV--------------GYLPQEPQLDPEKTVRENVEEGVAEVKAAld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 109 -----NAEQAEKKAM--ELLERVG-------------LAHK------------KDAFPSQLSGGQQQRVAIARGLAMEPR 156
Cdd:PRK11819 104 rfneiYAAYAEPDADfdALAAEQGelqeiidaadawdLDSQleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 157 VMLFDEPTSALDPEmvgEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQ 213
Cdd:PRK11819 184 MLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGR 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
14-195 |
9.44e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 14 LHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLES---IEsGEIWVDGVnvadPKTDLNKIREEvGFVFQGFNLYP 90
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggyIE-GDIRISGF----PKKQETFARIS-GYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 91 HLTVLENITLA-----PMKVKGQNAEQAEKKAMELLERVGLahkKDA---FP--SQLSGGQQQRVAIARGLAMEPRVMLF 160
Cdd:PLN03140 967 QVTVRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNL---KDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|....*
gi 488162483 161 DEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHE 195
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.83e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIE--SGEIWVDGVNVA--DPKtdlNKIR 76
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLelSPE---DRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 77 EEVGFVFQgfnlYP-------HLTVLENITLAPMKVKGQNA-----------EQAEKKAM--ELLER---VGlahkkdaf 133
Cdd:PRK09580 78 EGIFMAFQ----YPveipgvsNQFFLQTALNAVRSYRGQEPldrfdfqdlmeEKIALLKMpeDLLTRsvnVG-------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 134 psqLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTH 194
Cdd:PRK09580 146 ---FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-212 |
1.92e-09 |
|
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: 54.69 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 26 KGEVVVVCGPSGSGKSTLIRTV-NQLESIESGEIWVDGvnvadpktdlNKIREEVGFVFQGFNLYPHltvlenitlapmk 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG----------EDILEEVLDQLLLIIVGGK------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 105 vkgqnaeqaekkamellervglahkkdafPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLK------V 178
Cdd:smart00382 58 -----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 488162483 179 MKDLAESGMTMMCVTHEMGF-----AREVADRVIFVDKG 212
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-214 |
3.05e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 20 VNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLEsIESGEIWVDgvnvadpktdlnkirEEVGFVFQGFNLYpHLTVLENI 98
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLlSQFE-ISEGRVWAE---------------RSIAYVPQQAWIM-NATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 99 TL-----APMKVKGQNAEQAEKKAMELleRVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEmVG 173
Cdd:PTZ00243 742 LFfdeedAARLADAVRVSQLEADLAQL--GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH-VG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488162483 174 EvlKVMKDL---AESGMTMMCVTHEMGFArEVADRVIFVDKGQI 214
Cdd:PTZ00243 819 E--RVVEECflgALAGKTRVLATHQVHVV-PRADYVVALGDGRV 859
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-214 |
4.24e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVADpKTDLNKIREEVGFVFQ---GFNLYPHLT 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN-HNANEAINHGFALVTEerrSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 94 VLENITLAPMKvkgqnaeqAEKKAMELLERVGLahKKDA----------FPSQ------LSGGQQQRVAIARGLAMEPRV 157
Cdd:PRK10982 343 IGFNSLISNIR--------NYKNKVGLLDNSRM--KSDTqwvidsmrvkTPGHrtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488162483 158 MLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
15-207 |
4.93e-09 |
|
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: 55.31 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLI----------------RTVNQLESIESGEiWVDGVNVAD----------- 67
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarrlhlkkEQPGNHDRIEGLE-HIDKVIVIDqspigrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 68 PKT---DLNKIREEVGFVFQG--FNLyphlTVLEnitlapMKVKGQN--------AEQAEK---------KAMELLERVG 125
Cdd:cd03271 88 PATytgVFDEIRELFCEVCKGkrYNR----ETLE------VRYKGKSiadvldmtVEEALEffenipkiaRKLQTLCDVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 126 LAHKKDAFPS-QLSGGQQQRVAIARGLAMEPR---VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFARe 201
Cdd:cd03271 158 LGYIKLGQPAtTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK- 236
|
....*.
gi 488162483 202 VADRVI 207
Cdd:cd03271 237 CADWII 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-240 |
1.74e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEvgfvfqgFNLYPHLTVL 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--AYGLRELRRQ-------FSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 96 ENITLApmkvkgQN------AEQAEK-KAMELL---ERV-----GLAHKKDAFPSQLSGGQQQRVAIARGLAMEPR-VML 159
Cdd:PTZ00243 1396 FDGTVR------QNvdpfleASSAEVwAALELVglrERVaseseGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFIL 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 160 FDEPTSALDPEMVGEV-LKVMKdlAESGMTMMCVTHEMgfaREVA--DRVIFVDKGQILEDETPEAFFTNPK---HE--- 230
Cdd:PTZ00243 1470 MDEATANIDPALDRQIqATVMS--AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQsifHSmve 1544
|
250
....*....|....*
gi 488162483 231 -----RAKQFLQQVM 240
Cdd:PTZ00243 1545 algrsEAKRFLQLVG 1559
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-216 |
1.89e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 2 IKFKNVHKHFK----------DL----------HVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVnqlesiesgeiwvd 61
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklkDLffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 62 gVNVADPKTDLNKIREEVGFVFQGFNLYPHLTVLENITLAPMkVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQ 141
Cdd:PRK13545 71 -AGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 142 QQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
8-211 |
5.10e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 8 HKHFKDLHVINGVNleikkGEVVVVCGPSGSGKSTLIRTVnqlesiesgeIWVDGVN-VADPKTDLNKIREEVGFVfqgf 86
Cdd:cd03227 7 FPSYFVPNDVTFGE-----GSLTIITGPNGSGKSTILDAI----------GLALGGAqSATRRRSGVKAGCIVAAV---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 87 nlyphltvlenitlapmkvkgqnaeqaekkAMELLERVglahkkdafpSQLSGGQQQRVAIARGLAME---PRVM-LFDE 162
Cdd:cd03227 68 ------------------------------SAELIFTR----------LQLSGGEKELSALALILALAslkPRPLyILDE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488162483 163 PTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFArEVADRVIFVDK 211
Cdd:cd03227 108 IDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHIKK 155
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-214 |
7.72e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 7.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 5 KNVHKHFKDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRT-VNQLEsIESGEI-WVDGVNV--------ADPKTDLNk 74
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTVkWSENANIgyyaqdhaYDFENDLT- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 75 ireevgfVFQGFNLYphltvlenitlapmkVKGQNAEQAEKKAM-ELLERVGLAHKKdafPSQLSGGQQQRVAIARGLAM 153
Cdd:PRK15064 401 -------LFDWMSQW---------------RQEGDDEQAVRGTLgRLLFSQDDIKKS---VKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488162483 154 EPRVMLFDEPTSALDPEMVgEVLKVMKDLAESgmTMMCVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESI-ESLNMALEKYEG--TLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-241 |
8.23e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 137 LSGGQQQRVAIARGLAMEPR--VMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFArEVADRVIFVDK--- 211
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgag 555
|
90 100 110
....*....|....*....|....*....|...
gi 488162483 212 ---GQILEDETPEAFFTNpKHERAKQFLQQVMT 241
Cdd:PRK00635 556 ifgGEVLFNGSPREFLAK-SDSLTAKYLRQELT 587
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-221 |
1.95e-07 |
|
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: 50.63 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESiESGEIWVDGVNVADPKTDL---NKIREEVGFVFQgFNLYPH 91
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEP-SEGKIKHSGRISFSSQFSWimpGTIKENIIFGVS-YDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLenitlapmkvkgqnaeqaekKAMELLERVGLAHKKDAFPS-----QLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:cd03291 130 KSVV--------------------KACQLEEDITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488162483 167 LDPEMVGEVLK--VMKDLAESgmTMMCVTHEMGFAREvADRVIFVDKGQI--------LEDETPE 221
Cdd:cd03291 190 LDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGSSyfygtfseLQSLRPD 251
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-212 |
2.91e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTV-NQLESIEsGEIWVDGVNVADPKTDL---NKIREEVGFVFQgFNLYPH 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPSE-GKIKHSGRISFSPQTSWimpGTIKDNIIFGLS-YDEYRY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLenitlapmkvkgqnaeqaekKAMELLERVGLAHKKDAFP-----SQLSGGQQQRVAIARGLAMEPRVMLFDEPTSA 166
Cdd:TIGR01271 519 TSVI--------------------KACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488162483 167 LDPEMVGEVLK--VMKDLAESgmTMMCVTHEMGFAREvADRVIFVDKG 212
Cdd:TIGR01271 579 LDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-216 |
5.77e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 12 KDLHVINGVNLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGvnvadpktdlnkireEVGFVFQGFNLYPH 91
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 92 LTVLENITLApMKVKGQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEM 171
Cdd:PRK13546 100 LTGIENIEFK-MLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488162483 172 VGEVLKVMKDLAESGMTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-217 |
7.18e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 21 NLEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEIWVDGVNVAdpKTDLNKIREEVGFVFQGFN---LYPH-----L 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHIT--RLSFEQLQKLVSDEWQRNNtdmLSPGeddtgR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 93 TVLENItlapmkvkgQNAEQAEKKAMELLERVGLAHKKDAFPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMV 172
Cdd:PRK10938 101 TTAEII---------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488162483 173 GEVLKVMKDLAESGMTMMCVTHEMGfarEVADrviFVDKGQILED 217
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFD---EIPD---FVQFAGVLAD 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-221 |
1.37e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 1 MIKFKNVHKH-FKDlhvingVNLEIKKGEVVVVCGPSGSGKSTLIRTV------NQLE----------SIESGE-----I 58
Cdd:TIGR00630 613 FLTLKGARENnLKN------ITVSIPLGLFTCITGVSGSGKSTLINDTlypalaNRLNgaktvpgrytSIEGLEhldkvI 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 59 WVDG--------------VNVADP------KTDLNKIReevG-----FVF----------QG-------FNLYPHLTV-- 94
Cdd:TIGR00630 687 HIDQspigrtprsnpatyTGVFDEirelfaETPEAKVR---GytpgrFSFnvkggrceacQGdgvikieMHFLPDVYVpc 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 ------------LEnitlapMKVKGQN--------AEQAEK---------KAMELLERVGLAHKKDAFPS-QLSGGQQQR 144
Cdd:TIGR00630 764 evckgkrynretLE------VKYKGKNiadvldmtVEEAYEffeavpsisRKLQTLCDVGLGYIRLGQPAtTLSGGEAQR 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGL---AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAReVADRVIFV-----DK-GQIL 215
Cdd:TIGR00630 838 IKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeggDGgGTVV 916
|
....*.
gi 488162483 216 EDETPE 221
Cdd:TIGR00630 917 ASGTPE 922
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-194 |
5.87e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 34 GPSGSGKSTLIRTVNQLESIESGEIWVDGVNVadpktdlNKIREE-VGFVFQGFNLYPHLTVLENITlapMKVKGQNAEQ 112
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-------NNIAKPyCTYIGHNLGLKLEMTVFENLK---FWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 113 AEKKAMELLERVGLAHKKDAfpsQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVGEV--LKVMKdlAESGMTMM 190
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLnnLIVMK--ANSGGIVL 177
|
....
gi 488162483 191 CVTH 194
Cdd:PRK13541 178 LSSH 181
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-43 |
1.25e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 1.25e-05
10 20
....*....|....*....|....*
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTL 43
Cdd:COG0178 18 NIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
109-207 |
2.24e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 109 NAEQAEKKAMELLerVGLAHKKDA---FPSQLSGGQQQRVAIARGLAMEPRVMLFDEPTSALDpemVGEVLKVMKDLAES 185
Cdd:PLN03073 316 DAYTAEARAASIL--AGLSFTPEMqvkATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKW 390
|
90 100
....*....|....*....|..
gi 488162483 186 GMTMMCVTHemgfAREVADRVI 207
Cdd:PLN03073 391 PKTFIVVSH----AREFLNTVV 408
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-237 |
2.46e-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: 44.61 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 17 INGVNLEIKKGEVVVVcGPSGSGKSTLI------------RTV-----NQLESIESGEIWVDGV---------------- 63
Cdd:COG3593 14 IKDLSIELSDDLTVLV-GENNSGKSSILealrlllgpsssRKFdeedfYLGDDPDLPEIEIELTfgsllsrllrlllkee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 64 NVADPKTDLNKIREEVGFVFQGFN--LYPHLTVLENITLAPMKVKGQNAEQAEKKAmelleRVGLAHKKDAFPSQLSGGQ 141
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNelLSEYLKELLDGLDLELELSLDELEDLLKSL-----SLRIEDGKELPLDRLGSGF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 142 QQRVAIARGLAM-------EPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAREV-ADRVIFVDKGq 213
Cdd:COG3593 168 QRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRD- 246
|
250 260
....*....|....*....|....
gi 488162483 214 ilEDETPEAFFTNPKHERAKQFLQ 237
Cdd:COG3593 247 --SGGTTSTKLIDLDDEDLRKLLR 268
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-216 |
4.18e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 24 IKKGEVVVVCGPSGSGKSTLIrtvnqleSIESGEIWVDGVNVADPKT-DLNKIREE--------VGFVFQGFNLYPHLTV 94
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLL-------ALLKNEISADGGSYTFPGNwQLAWVNQEtpalpqpaLEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LEN----------ITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFP-SQLSGGQQQRVAIARGLAMEPRVMLFDEP 163
Cdd:PRK10636 97 QLHdanerndghaIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 164 TSALDPEMVGEVLKVMKDLAEsgmTMMCVTHEMGFAREVADRVIFVDKGQILE 216
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
71-194 |
6.65e-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: 43.15 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 71 DLNKIREEVGFVFQGFNLYPHltvlenITLAPMKVKGQNAEQAEKKAMELLERVGLAHKKDAFP---SQLSGGQQQ---R 144
Cdd:pfam13304 174 DLALFPDLKELLQRLVRGLKL------ADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpaFELSDGTKRllaL 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488162483 145 VAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTH 194
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
136-211 |
8.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 43.55 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 136 QLSGGQQ------QRVAIARGLAMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFaREVADRVIFV 209
Cdd:NF041034 779 ALSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL-KEISDYIISV 857
|
..
gi 488162483 210 DK 211
Cdd:NF041034 858 EK 859
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-207 |
1.61e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488162483 135 SQLSGGQQQRVAIARGL---AMEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMMCVTHEMGFAReVADRVI 207
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
26-58 |
1.66e-04 |
|
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: 41.23 E-value: 1.66e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488162483 26 KGEVVVVCGPSGSGKSTLIrtvNQL---ESIESGEI 58
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLL---NALlpeLVLATGEI 116
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
26-45 |
2.95e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 39.81 E-value: 2.95e-04
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
26-58 |
5.01e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 5.01e-04
10 20 30
....*....|....*....|....*....|...
gi 488162483 26 KGEVVVVCGPSGSGKSTLIRTVNQLESIESGEI 58
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRTGEI 137
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
29-80 |
5.05e-04 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 5.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488162483 29 VVVVCGPSGSGKSTLIRT-VNQLESIESGEIWVDGVNVADPKTDLNKIREEVG 80
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRlLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALG 59
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-44 |
5.40e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 5.40e-04
10 20
....*....|....*....|....*.
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTLI 44
Cdd:COG0178 623 NVDVEIPLGVLTCVTGVSGSGKSTLV 648
|
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
22-71 |
7.33e-04 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain] Cd Length: 637 Bit Score: 40.32 E-value: 7.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488162483 22 LEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEiWVDGVNVADPKTD 71
Cdd:TIGR00602 105 LENAPKRILLITGPSGCGKSTTIKILSKELGIQVQE-WSNPTLPDFQKND 153
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1-44 |
7.76e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 7.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488162483 1 MIKFKNVHKHfkdlhviN--GVNLEIKKGEVVVVCGPSGSGKSTLI 44
Cdd:PRK00349 614 FLKLKGAREN-------NlkNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
35-211 |
8.34e-04 |
|
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: 39.55 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 35 PSGSGKSTLIRTVnqleSIESGEIWVDGVNVadPKTDLNKIREEVGFVFQgfNLYphltvleNITLAPMKVKGQNAEQAE 114
Cdd:cd03272 88 PIDKEEVRLRRTI----GLKKDEYFLDKKNV--TKNDVMNLLESAGFSRS--NPY-------YIVPQGKINSLTNMKQDE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 115 KKAMEllervglahkkdafpsQLSGGQQQRVAIARGLAM---EPRVM-LFDEPTSALDPEMVGEVLKVMKDLAESGMtMM 190
Cdd:cd03272 153 QQEMQ----------------QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQYRTAVANMIKELSDGAQ-FI 215
|
170 180
....*....|....*....|....*.
gi 488162483 191 CVTH--EMgfaREVAD---RVIFVDK 211
Cdd:cd03272 216 TTTFrpEL---LEVADkfyGVKFRNK 238
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
24-101 |
9.03e-04 |
|
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410885 [Multi-domain] Cd Length: 168 Bit Score: 38.91 E-value: 9.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 24 IKKGEVVVVCGPSGSGKSTLIRTVnqLESIESGEiwvDGVNVADPktdlnkirEEvgFVFQGFNLYPHLTVLENITLA 101
Cdd:cd19477 7 IAIGKNVIVCGGTGSGKTTYIKSI--LEFIPKEE---RIISIEDT--------EE--IVFKHHKNYTQLFFGGNITSA 69
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
15-43 |
9.51e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 9.51e-04
10 20
....*....|....*....|....*....
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTL 43
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-168 |
1.10e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 34 GPSGSGKSTLIRtvnqlesIESGEIWVDGVNVA-DPKTDLNKIREEvGFVFQGFNLYPhlTVL-------------ENIT 99
Cdd:PRK15064 34 GANGCGKSTFMK-------ILGGDLEPSAGNVSlDPNERLGKLRQD-QFAFEEFTVLD--TVImghtelwevkqerDRIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 100 LAP-------MKV---KGQNAE----QAEKKAMELLERVGLAHKKDAFP-SQLSGGQQQRVAIARGLAMEPRVMLFDEPT 164
Cdd:PRK15064 104 ALPemseedgMKVadlEVKFAEmdgyTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
....
gi 488162483 165 SALD 168
Cdd:PRK15064 184 NNLD 187
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
26-45 |
1.36e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 38.51 E-value: 1.36e-03
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
19-43 |
1.51e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.51e-03
10 20
....*....|....*....|....*
gi 488162483 19 GVNLEIKKGEVVVVCGPSGSGKSTL 43
Cdd:PRK00349 18 NIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
29-49 |
1.84e-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: 37.51 E-value: 1.84e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-214 |
1.85e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 1.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488162483 137 LSGGQQQRVAIARGLAMEPRVMLFDEPTSALDPEMVgEVLKVMKDLAESGMTMmcVTHEMGFAREVADRVIFVDKGQI 214
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EALIQGLVLFQGGVLM--VSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
26-58 |
2.17e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.65 E-value: 2.17e-03
10 20 30
....*....|....*....|....*....|....*.
gi 488162483 26 KGEVVVVCGPSGSGKSTLIrtvNQL---ESIESGEI 58
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLL---NALapdLELKTGEI 195
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
26-69 |
2.19e-03 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 37.78 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 26 KGEVVVVCGPSGSGKSTLIRTVNQ---LES-----IESGEIWVDGVNVADPK 69
Cdd:COG4088 3 SPMLLILTGPPGSGKTTFAKALAQrlyAEGiavalLHSDDFRRFLVNESFPK 54
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-181 |
4.08e-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: 35.67 E-value: 4.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 135 SQLSGGQQQR-VAIARGLAM------------EPRVMLFDEPTSALDPEMVGEVLKVMKD 181
Cdd:pfam13558 31 GGLSGGEKQLlAYLPLAAALaaqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
29-45 |
4.44e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 36.52 E-value: 4.44e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
115-207 |
4.49e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 115 KKAMELLERVGL--------AhkkdafpSQLSGGQQQRVAIARGLAMEPR---VMLFDEPTSALDPEMVGEVLKVMKDLA 183
Cdd:COG0178 804 ARKLQTLQDVGLgyiklgqpA-------TTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLV 876
|
90 100
....*....|....*....|....*..
gi 488162483 184 ESGMTMMCVTHEMgfarEV---ADRVI 207
Cdd:COG0178 877 DKGNTVVVIEHNL----DViktADWII 899
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
95-228 |
4.91e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 95 LENITLAPmkVKGQNAEQAEKkamELLER------VGLAH---KKDAfpSQLSGGQQQRVAIARGLAMEPRVMLF--DEP 163
Cdd:TIGR00630 445 FNQLTLTP--EEKKIAEEVLK---EIRERlgflidVGLDYlslSRAA--GTLSGGEAQRIRLATQIGSGLTGVLYvlDEP 517
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488162483 164 TSAL---DPEMVGEVLKVMKDLaesGMTMMCVTHEMGFAREvADRVI------FVDKGQILEDETPEAFFTNPK 228
Cdd:TIGR00630 518 SIGLhqrDNRRLINTLKRLRDL---GNTLIVVEHDEDTIRA-ADYVIdigpgaGEHGGEVVASGTPEEILANPD 587
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
25-64 |
5.00e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 36.99 E-value: 5.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488162483 25 KKGEVVVVCGPSGSGKSTLIRTV-NQLESIE-----------SGEiwVDGVN 64
Cdd:PRK00300 3 RRGLLIVLSGPSGAGKSTLVKALlERDPNLQlsvsattraprPGE--VDGVD 52
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-212 |
5.80e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488162483 118 MELLERVGLAH-----KKDAfpsqLSGGQQQRVAIARGLA--MEPRVMLFDEPTSALDPEMVGEVLKVMKDLAESGMTMM 190
Cdd:PRK00635 1368 LTFIDKVGLSYitlgqEQDT----LSDGEHYRLHLAKKISsnLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVI 1443
|
90 100
....*....|....*....|..
gi 488162483 191 cVTHEMGFAREVADRVIFVDKG 212
Cdd:PRK00635 1444 -ATDRSGSLAEHADHLIHLGPG 1464
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
27-60 |
5.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 37.92 E-value: 5.93e-03
10 20 30
....*....|....*....|....*....|....
gi 488162483 27 GEVVVVCGPSGSGKSTLIRTVnqLESIESGEIWV 60
Cdd:COG3899 311 GELVLVSGEAGIGKSRLVREL--ARRARARGGRV 342
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
15-44 |
8.28e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 8.28e-03
10 20 30
....*....|....*....|....*....|
gi 488162483 15 HVINGVNLEIKKGEVVVVCGPSGSGKSTLI 44
Cdd:pfam13555 10 GTFDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| dnd_assoc_3 |
TIGR03238 |
DNA phosphorothioation-dependent restriction protein DptF; A DNA sulfur modification ... |
16-87 |
8.71e-03 |
|
DNA phosphorothioation-dependent restriction protein DptF; A DNA sulfur modification (phosphorothioation) system, dnd (degradation during electrophoresis), is sparsely and sporadically distributed among the bacteria. This protein is one member of a three-gene restriction enzyme cassette that depends on DNA phosphorothioation. [DNA metabolism, Restriction/modification]
Pssm-ID: 132282 Cd Length: 504 Bit Score: 36.81 E-value: 8.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488162483 16 VINGVNLEIKKGEVVVVCGPSGSGKSTLIRTvNQLESIESGEIWVDGVNVADPKTDLNKIREEvgfVFQGFN 87
Cdd:TIGR03238 21 ILVKFNKELPSSSLLFLCGSSGDGKSEILAE-NKRKFSEGYEFFLDATHSFSPNKNAMETLDE---IFDGFN 88
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
22-68 |
9.47e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 36.09 E-value: 9.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488162483 22 LEIKKGEVVVVCGPSGSGKSTLIRTVNQLESIESGEiWVDGVNVADP 68
Cdd:pfam03215 40 LENAKHRILLISGPSGCGKSTVIKELSKELGPKYRE-WSNPTSFRSP 85
|
|
| |
