|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-239 |
6.54e-172 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 472.56 E-value: 6.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMG 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 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 |
6.47e-139 |
|
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: 388.04 E-value: 6.47e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMGM 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
8.46e-131 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 369.51 E-value: 8.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN--------- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 --LNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:COG4598 88 rqLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTH 229
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKS 247
|
250
....*....|.
gi 515498091 230 QRTQNFLSRVL 240
Cdd:COG4598 248 ERLRQFLSSSL 258
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-239 |
6.25e-114 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 325.89 E-value: 6.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMG 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
1.10e-110 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 321.26 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKL 75
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEReLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPK-AEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQN 234
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*.
gi 515498091 235 FLSRVL 240
Cdd:COG1135 240 FLPTVL 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-240 |
1.43e-110 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 317.85 E-value: 1.43e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRV------IFEGNELSNHKNNLNK 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQN 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 515498091 235 FLSRVL 240
Cdd:PRK11264 243 FLEKFL 248
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
1.93e-97 |
|
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: 284.09 E-value: 1.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFG----KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN-NLNKL 75
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPK-AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-240 |
1.11e-94 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 280.92 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF--GKNEV--LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKL 75
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPK-AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQN 234
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
....*.
gi 515498091 235 FLSRVL 240
Cdd:PRK11153 240 FIQSTL 245
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
2-240 |
4.13e-94 |
|
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: 276.33 E-value: 4.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN----------- 70
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGrngplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 NLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTH 229
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 515498091 230 QRTQNFLSRVL 240
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
4.64e-94 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 275.00 E-value: 4.64e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKL 75
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEReLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 R-QKMGMVFQNFNLFPHKTVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAkDVSDKVIFMADGYVIEE 217
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-237 |
1.03e-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: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsNHKNNLN-----KLR 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSekairLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNIILAP-KLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPcKVLGLSK-EQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSpQQIFQSPTHQRTQNF 235
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239
|
..
gi 515498091 236 LS 237
Cdd:COG4161 240 LS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-237 |
6.04e-92 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 270.35 E-value: 6.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNE--LSNHKN--NLNKLRQ 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSdkAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQiFQSPTHQRTQNFLS 237
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYLS 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
1.09e-91 |
|
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: 278.71 E-value: 1.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHK-NNLNK 74
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQN-FN-LFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQ 230
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
....*....
gi 515498091 231 RTQNFLSRV 239
Cdd:COG1123 500 YTRALLAAV 508
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-236 |
2.00e-90 |
|
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: 266.46 E-value: 2.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQKM 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILApkLLNKSDLN--QLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFP--LREHTDLSeaEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPtHQRTQNFL 236
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
7.28e-89 |
|
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: 261.66 E-value: 7.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLR 76
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 -QKMGMVFQNFNLFPHKTVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDvSDKVIFMADGYV 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.74e-87 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 259.22 E-value: 1.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN-NLNKLRQK 78
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIiLAPKL------------LNKSDlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVA 146
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNV-LAGRLgrtstwrsllglFPPED----RERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-237 |
8.97e-87 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 257.66 E-value: 8.97e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL--ETP---TNGRVIFEGNELSNHKNNLNKLR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPhKTVLNNIILAPKL---LNKSDLNQLKQEALTlleKVGL----EDKANVYPSQLSGGQKQRVAIAR 149
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYGLRLhgiKSKSELDEIVEESLR---KAALwdevKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPevvydV--LKV---MKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDP-----IstAKIeelILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|...
gi 515498091 225 QSPTHQRTQNFLS 237
Cdd:COG1117 242 TNPKDKRTEDYIT 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-240 |
8.34e-86 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 255.28 E-value: 8.34e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELS-----------NHKN 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 NLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANV-YPSQLSGGQKQRVAIAR 149
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTH 229
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
250
....*....|.
gi 515498091 230 QRTQNFLSRVL 240
Cdd:PRK10619 246 PRLQQFLKGSL 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
1.46e-84 |
|
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: 250.95 E-value: 1.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL-----ETPTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPhKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLED--KANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
6.89e-84 |
|
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: 249.73 E-value: 6.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQKMG 80
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIilAPKLLNKSDLNQLKQEALTL--LEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENV--AFPLREHTRLSEEEIREIVLekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSpTHQRTQNF 235
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-223 |
3.43e-83 |
|
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: 248.25 E-value: 3.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQKM 79
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIiLAPKLLNKSDLNQL--------KQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV-LSGRLGRRSTWRSLfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
1.53e-82 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 245.73 E-value: 1.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQK 78
Cdd:COG2884 1 MIRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSR-KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-223 |
2.77e-82 |
|
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: 246.06 E-value: 2.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQK 78
Cdd:TIGR02315 1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIiLAPKLLNKSDLNQL--------KQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENV-LHGRLGYKPTWRSLlgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-227 |
2.78e-82 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 249.63 E-value: 2.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnklRQ 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppEK------RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 kMGMVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:COG3842 79 -VGMVFQDYALFPHLTVAENVAFGLRMrgVPKAEIRARVAELLEL---VGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTH--EMGFAkdVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHdqEEALA--LADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
3.50e-82 |
|
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: 244.93 E-value: 3.50e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMG 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT--KKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQN-FN-LFpHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:COG1122 79 LVFQNpDDqLF-APTVEEDVAFGPENLGLPR-EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.76e-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: 239.22 E-value: 1.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhknnlnKLR 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-------GPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPK-AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 157 IILFDEPTSALDP---EVVYDVLkvMKDLAKEGMTMVVVTHemgfakDV------SDKVIFMAD--GYVIEE 217
Cdd:COG1116 159 VLLMDEPFGALDAltrERLQDEL--LRLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVEE 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
1.82e-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: 236.31 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMGM 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILApkllnksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
3.86e-78 |
|
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: 234.71 E-value: 3.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QK-MGMVFQN----FNlfPHKTVLNNIILAPKLLNKSDLNQLKQEALTL-LEKVGL-EDKANVYPSQLSGGQKQRVAIAR 149
Cdd:cd03257 81 RKeIQMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-227 |
3.55e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 236.58 E-value: 3.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhKNNLNKLRQKMGM 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSK-AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-236 |
1.24e-76 |
|
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: 231.62 E-value: 1.24e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGK----NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV--TRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQN----FNlfPHKTVLNNIILAPKLLNKSDLnqlKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDR---EERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQ 230
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*.
gi 515498091 231 RTQNFL 236
Cdd:COG1124 234 YTRELL 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-229 |
3.52e-76 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 234.20 E-value: 3.52e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEG---NELSNHKNNlnklrq 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKDRN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 kMGMVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLLekvGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:COG3839 77 -IAMVFQSYALYPHMTVYENIAFPLKLrkVPKAEIDRRVREAAELL---GLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEvvydvLKV-----MKDLAKE-GMTMVVVTHE----MGFAkdvsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:COG3839 153 KVFLLDEPLSNLDAK-----LRVemraeIKRLHRRlGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVGTPEELYD 223
|
....
gi 515498091 226 SPTH 229
Cdd:COG3839 224 RPAN 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
2.03e-75 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 227.40 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLNKLRQKMGM 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLlNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-223 |
9.22e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.48 E-value: 9.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknnLNKLRQKMGM 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD---PAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPR-KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-229 |
4.55e-74 |
|
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: 227.63 E-value: 4.55e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFG-KNEVLK---DINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLETP--TNGRVIFEGNELSN-HKNNL 72
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAiLGLLPPPgiTSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 NKLR-QKMGMVFQN----FNlfPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGL---EDKANVYPSQLSGGQKQR 144
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 145 VAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*.
gi 515498091 224 FQSPTH 229
Cdd:COG0444 239 FENPRH 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
5.87e-74 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 223.50 E-value: 5.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMG 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNL-FPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFGLENLGLPE-EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-211 |
1.41e-73 |
|
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: 222.73 E-value: 1.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknnlnklRQ 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-------GP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPK-AEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 158 ILFDEPTSALDP---EVVYDVLkvMKDLAKEGMTMVVVTHemgfakDVsDKVIFMAD 211
Cdd:cd03293 153 LLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTH------DI-DEAVFLAD 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-227 |
2.16e-71 |
|
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: 226.32 E-value: 2.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF--GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPT---NGRVIFEGNELSNHKNNLnkL 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNF--NLFPHkTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAM 153
Cdd:COG1123 82 GRRIGMVFQDPmtQLNPV-TVGDQIAEALENLGLSR-AEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 154 HPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
5.85e-71 |
|
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: 218.07 E-value: 5.85e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhKNNLNKLRQKM 79
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD-EENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQN-FNLFPHKTVLNNIILAPKllNKS-DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVEDDVAFGLE--NLGvPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-227 |
1.25e-70 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 216.40 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE-VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMG 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR--EQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLnKSDLNQLKQEALTLLEKVGLEDK--ANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 159 LFDEPTSALDPeVVYDVL-KVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:cd03295 158 LMDEPFGALDP-ITRDQLqEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-227 |
4.43e-70 |
|
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: 215.59 E-value: 4.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN---------------EVLK---------DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGR 57
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 58 VIFEGNELS--NHKNNLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSdLNQLKQEALTLLEKVGLEDKANVYPS 135
Cdd:cd03294 81 VLIDGQDIAamSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVP-RAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 136 QLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
250
....*....|...
gi 515498091 215 IEEGSPQQIFQSP 227
Cdd:cd03294 240 VQVGTPEEILTNP 252
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-227 |
4.82e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 214.20 E-value: 4.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN---------------EVLK---------DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNG 56
Cdd:COG4175 3 KIEVRNLYKIFGKRperalklldqgkskdEILEktgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 57 RVIFEGNELSNH-KNNLNKLRQ-KMGMVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALtllEKVGLEDKANV 132
Cdd:COG4175 83 EVLIDGEDITKLsKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIqgVPKAERRERAREAL---ELVGLAGWEDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 133 YPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPevvydvL--KVMKDL-----AKEGMTMVVVTHEMGFAKDVSDK 205
Cdd:COG4175 160 YPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP------LirREMQDEllelqAKLKKTIVFITHDLDEALRLGDR 233
|
250 260
....*....|....*....|..
gi 515498091 206 VIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG4175 234 IAIMKDGRIVQIGTPEEILTNP 255
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-214 |
6.95e-68 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 208.33 E-value: 6.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLR 76
Cdd:TIGR02982 2 ISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGaSKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAkDVSDKVIFMADGYV 214
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEqGCTILMVTHDNRIL-DVADRILQMEDGKL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-228 |
7.89e-68 |
|
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: 208.63 E-value: 7.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhkNNLNKLRQKMGM 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI----TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLnKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-227 |
1.02e-67 |
|
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: 208.45 E-value: 1.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLnklRQKMGM 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE---IARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 V--FQNFNLFPHKTVLNNIILAPKLLNKSDLN---------QLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:cd03219 78 GrtFQIPRLFPELTVLENVMVAAQARTGSGLLlararreerEARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-239 |
1.39e-67 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 212.25 E-value: 1.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLNKLRQKMGM 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR----LHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLL---NKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLS 237
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
..
gi 515498091 238 RV 239
Cdd:PRK10851 239 EV 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-236 |
3.57e-67 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 207.19 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknnlnKLRQK-MG 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV-----PVQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKS---DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFL 236
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-228 |
6.61e-67 |
|
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: 207.20 E-value: 6.61e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS--RRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQ----NFNL----------FPHKTVLnniilapKLLNKSDlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVA 146
Cdd:COG1120 79 YVPQeppaPFGLtvrelvalgrYPHLGLF-------GRPSAED----REAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
...
gi 515498091 226 SPT 228
Cdd:COG1120 228 PEL 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-228 |
2.16e-66 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 206.53 E-value: 2.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNEL-SNHKNNLNKL 75
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQnfnlFPHK-----TVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDK-ANVYPSQLSGGQKQRVAIAR 149
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNLGLSE-EEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 |
9.70e-66 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 203.45 E-value: 9.70e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGknEVLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLL---ETPTNGRVIFEGNELSNhknnLNKLRQ 77
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLRFDLTIAAGERVAILGPSGAGKSTLL---NLIagfLPPDSGRILWNGQDLTA----LPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIILA--PKL-LNKSDLNQLKQealtLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:COG3840 72 PVSMLFQENNLFPHLTVAQNIGLGlrPGLkLTAEQRAQVEQ----ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQ 233
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
....*
gi 515498091 234 NFLSR 238
Cdd:COG3840 228 AYLGI 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
1.19e-65 |
|
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: 204.12 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnklRQ 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlppHR------IA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMV--FQNFNLFPHKTVLNNIILA--------------PKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQ 141
Cdd:COG0411 78 RLGIArtFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
250
....*....|.
gi 515498091 221 QQIFQSPTHQR 231
Cdd:COG0411 238 AEVRADPRVIE 248
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
4.67e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 202.24 E-value: 4.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsnhknNLNKLRQKMG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-------PPRRARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNL---FPhKTV-------LNNIILAPKLLNKSDlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:COG1121 79 YVPQRAEVdwdFP-ITVrdvvlmgRYGRRGLFRRPSRAD----REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGyVIEEGSPQQIFQSPTHQ 230
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLS 232
|
..
gi 515498091 231 RT 232
Cdd:COG1121 233 RA 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
1.93e-64 |
|
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: 199.97 E-value: 1.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLN--- 73
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA----LDeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 --KLR-QKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:COG4181 84 raRLRaRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDA---RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDvSDKVIFMADGYVIEE 217
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-237 |
2.54e-63 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 200.34 E-value: 2.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF--------GKNEVLK---DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HK 69
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 70 NNLNKLRQKMGMVFQN----FNlfPHKTVlNNIILAPKLLNKS-DLNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQ 143
Cdd:COG4608 88 RELRPLRRRMQMVFQDpyasLN--PRMTV-GDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 144 RVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQ 222
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDE 244
|
250
....*....|....*
gi 515498091 223 IFQSPTHQRTQNFLS 237
Cdd:COG4608 245 LYARPLHPYTQALLS 259
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-209 |
2.04e-62 |
|
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: 193.99 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELS--NHKNNLNKLRQKMGM 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPplNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALtllEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYkkLSKKEKREKKKEAL---EKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKdVSDKVIFM 209
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
2.27e-62 |
|
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: 195.08 E-value: 2.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGneLSNHKNNlNKLRQKMG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEP-REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNI-ILAPklLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:COG4555 78 VLPDERGLYDRLTVRENIrYFAE--LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
3.59e-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: 193.62 E-value: 3.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQK 78
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKE-REIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-212 |
1.81e-61 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 191.57 E-value: 1.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMGM 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM--PPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPhKTVLNNIILAPKLLNKSDlnqLKQEALTLLEKVGLED---KANVypSQLSGGQKQRVAIARALAMHPDII 158
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPFPFQLRERKF---DRERALELLERLGLPPdilDKPV--ERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
1.18e-60 |
|
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: 188.38 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnlNKLRQKMGM 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP---EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIilapkllnksdlnqlkqealtllekvgledkanvypsQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
5.26e-59 |
|
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: 194.52 E-value: 5.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN----EVLKDINLEIKKGEVLAIIGPSGSGKS-TLLRCMNLLETP---TNGRVIFEGNELSNHKNN- 71
Cdd:COG4172 6 LLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 LNKLR-QKMGMVFQ------NfnlfPHKTV---LNNIILAPKLLNKSdlnQLKQEALTLLEKVGL---EDKANVYPSQLS 138
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtslN----PLHTIgkqIAEVLRLHRGLSGA---AARARALELLERVGIpdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 139 GGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250
....*....|....*.
gi 515498091 218 GSPQQIFQSPTHQRTQ 233
Cdd:COG4172 239 GPTAELFAAPQHPYTR 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-237 |
9.91e-59 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 186.53 E-value: 9.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMN----LLET-PTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlndLIPGfRVEGKVTFHGKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPhKTVLNNIILAPKLLN-KSDLNQLKQEAL---TLLEKVglEDKANVYPSQLSGGQKQRVAIARALA 152
Cdd:PRK14243 91 RRIGMVFQKPNPFP-KSIYDNIAYGARINGyKGDMDELVERSLrqaALWDEV--KDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDVSDKVIFMA---------DGYVIEEGSPQQI 223
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKI 246
|
250
....*....|....
gi 515498091 224 FQSPTHQRTQNFLS 237
Cdd:PRK14243 247 FNSPQQQATRDYVS 260
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
4.18e-58 |
|
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: 181.29 E-value: 4.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLRQKMGMV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--AKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQnfnlfphktvlnniilapkllnksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
5.35e-58 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 182.99 E-value: 5.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEV-LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQKM 79
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPP-REIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
6.06e-58 |
|
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: 183.02 E-value: 6.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnKLRQK 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlppHE----RARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKvgLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
1.06e-57 |
|
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: 181.09 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMGMV 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS--PKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQnfnlfphktvlnniilapkllnksdlnqlkqealtLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-237 |
2.65e-57 |
|
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: 182.15 E-value: 2.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKfGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLNKLRQKMGM 81
Cdd:cd03299 1 LKVENLSKD-WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLnKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKR-KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLS 237
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
4.45e-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: 180.53 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhkNNLNKLRQKMGM 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKlLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLK-LRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVieegspQQI 223
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI------QQI 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
6.08e-57 |
|
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: 192.36 E-value: 6.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKM 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI--DPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFpHKTVLNNIILApkllnKSDLNQlkQEALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIA 148
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENITLG-----DPDATD--EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLA 698
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-237 |
1.57e-56 |
|
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: 187.97 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 7 LNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLetPTNGRVIFEGNELSNHKNN-LNKLRQKMGMVFQ 84
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAlLRLI--PSEGEIRFDGQDLDGLSRRaLRPLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 N----FNlfPHKTVLNNI-----ILAPKLlnksDLNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:COG4172 370 DpfgsLS--PRMTVGQIIaeglrVHGPGL----SAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQ 233
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
....
gi 515498091 234 NFLS 237
Cdd:COG4172 524 ALLA 527
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-227 |
1.01e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 182.07 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKNNLNklrqk 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVN----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 mgMVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK09452 90 --TVFQSYALFPHMTVFENVAFGLRMqkTPAAEITPRVMEALRM---VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 157 IILFDEPTSALDpevvYDVLKVM----KDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK09452 165 VLLLDESLSALD----YKLRKQMqnelKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-240 |
1.21e-55 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 178.50 E-value: 1.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL-----ETPTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNIILAPKLLN----KSDLNQLKQEAL---TLLEKVglEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvksKKELDERVEWALkkaALWDEV--KDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTH 229
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|.
gi 515498091 230 QRTQNFLSRVL 240
Cdd:PRK14267 242 ELTEKYVTGAL 252
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-236 |
1.53e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 181.07 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnlNKLRQK-MGMV 82
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-----RSIQQRdICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQNFNLFPHKTVLNNIILAPKLLN--KSDLNQLKQEALTLLEKVGLEDKanvYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGvpKEERKQRVKEALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFL 236
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFM 237
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
1.82e-55 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 178.73 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKM 79
Cdd:PRK13639 1 ILETRDLKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFN--LFPhKTVLNNIILAPK--LLNKSDLNQLKQEALtllEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:PRK13639 81 GIVFQNPDdqLFA-PTVEEDVAFGPLnlGLSKEEVEKRVKEAL---KAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNF 235
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANL 236
|
....*
gi 515498091 236 -LSRV 239
Cdd:PRK13639 237 rLPRV 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
5.86e-55 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 177.59 E-value: 5.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE------VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhKNNLNK 74
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD-EENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQNfnlfPHKTVLNNIILAPKLLNKSDLNQLKQEALT----LLEKVGLEDKANVYPSQLSGGQKQRVAIARA 150
Cdd:PRK13633 83 IRNKAGMVFQN----PDNQIVATIVEEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIF 224
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.29e-54 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 176.33 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQK 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQN-FNLFPHKTVLNNIilAPKLLNKS-DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK13632 85 IGIIFQNpDNQFIGATVEDDI--AFGLENKKvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKEGM-TMVVVTHEMGFAKdVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-236 |
2.62e-54 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 175.41 E-value: 2.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF---------GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNEL--SNHKN 70
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLeyGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 NLNKLRqkmgMVFQNFNlfphkTVLN---NI--IL-APKLLNkSDLNQLKQEAL--TLLEKVGL-EDKANVYPSQLSGGQ 141
Cdd:COG4167 85 RCKHIR----MIFQDPN-----TSLNprlNIgqILeEPLRLN-TDLTAEEREERifATLRLVGLlPEHANFYPHMLSSGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:COG4167 155 KQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKT 234
|
250
....*....|....*.
gi 515498091 221 QQIFQSPTHQRTQNFL 236
Cdd:COG4167 235 AEVFANPQHEVTKRLI 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-237 |
2.76e-54 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 177.08 E-value: 2.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNH-KNNLNKLRQKMGMVFQN--FNLFPHKT 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdPEAQKLLRQKIQIVFQNpyGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VlnNIILAPKLLNKSDLN--QLKQEALTLLEKVGLE-DKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPE 170
Cdd:PRK11308 111 V--GQILEEPLLINTSLSaaERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 171 VVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLS 237
Cdd:PRK11308 189 VQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
4.29e-54 |
|
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: 171.41 E-value: 4.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFG--KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKM 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFpHKTVLNNIilapkllnksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADG 212
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-237 |
4.84e-54 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 174.19 E-value: 4.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL-----ETPTNGRVIFEGNELSNHKNNLNKL 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNFNLFPHkTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLED--KANVYPSQ--LSGGQKQRVAIARAL 151
Cdd:PRK14239 85 RKEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDevKDRLHDSAlgLSGGQQQRVCIARVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQR 231
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKE 242
|
....*.
gi 515498091 232 TQNFLS 237
Cdd:PRK14239 243 TEDYIS 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-207 |
7.36e-54 |
|
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: 172.33 E-value: 7.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhknnlnKLRQKMGMV 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-------KERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQNFNL---FPhKTVLNNIILAP-------KLLNKSDlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALA 152
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLyghkglfRRLSKAD----KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVI 207
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-165 |
1.25e-53 |
|
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: 169.75 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLRQKMGMVFQNFNLFPHKTVLN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 97 NIILAPKLLNKSDLNQlKQEALTLLEKVGLEDKAN----VYPSQLSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:pfam00005 79 NLRLGLLLKGLSKREK-DARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-237 |
2.40e-53 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 172.40 E-value: 2.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL-----ETPTNGRVIFEGNELsnHKNNLNKLR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDI--FKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNIILAPKL----LNKSDLNQLKQEAL---TLLEKVglEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALekaQLWDEV--KDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTH 229
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*...
gi 515498091 230 QRTQNFLS 237
Cdd:PRK14247 239 ELTEKYVT 246
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
3.12e-53 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 173.28 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN--LNKLRQKMGMVFQnfnlFP---- 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkkLKPLRKKVGIVFQ----FPehql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 -HKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:PRK13634 99 fEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 169 PEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-239 |
8.42e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 172.33 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhknNLNKLRQKMG 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS----HVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQdkLPKAEIASRVNEMLGL---VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDV-LKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLS 237
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIG 251
|
..
gi 515498091 238 RV 239
Cdd:PRK11607 252 SV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-212 |
8.77e-52 |
|
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: 167.05 E-value: 8.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnlnKLRQKM-GM 81
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSiGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQN--FNLFpHKTVLNNIILAPKLLNKSdlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03226 76 VMQDvdYQLF-TDSVREELLLGLKELDAG-----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-223 |
1.05e-51 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 167.09 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIK---KGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNEL--SNHKNNLNKLRQKMGMVFQNFNLFPH 91
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNIILAPKLLNKSDLNQLKQEaltLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEV 171
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDE---LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 172 VYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIfmadgyVIEEGSPQQI 223
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIV------VMEDGRLQYI 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-225 |
1.30e-51 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 169.07 E-value: 1.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:PRK13637 3 IKIENLTHIYMEGtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQ--NFNLFpHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGL--EDKANVYPSQLSGGQKQRVAIARALA 152
Cdd:PRK13637 83 KKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSE-EEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-199 |
4.02e-51 |
|
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: 164.90 E-value: 4.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMGMVFQNFN--LF 89
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 pHKTVLNNIILAPKLLNKSD--LNQLKQEALTLLEKVGLEDKAnvyPSQLSGGQKQRVAIARALAMHPDIILFDEPTSAL 167
Cdd:TIGR01166 83 -AADVDQDVAFGPLNLGLSEaeVERRVREALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 515498091 168 DPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFA 199
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-222 |
1.14e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.43 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLLE---TPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNL 88
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLV---NLLLrfyDPTSGRILIDGVDIRDL--TLESLRRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 89 FpHKTVLNNIILApkLLNKSDlnqlkQEALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIARALAMHPDI 157
Cdd:COG1132 426 F-SGTIRENIRYG--RPDATD-----EEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQ 222
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHEE 560
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-213 |
1.23e-50 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 164.51 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNK----KFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN--HKNNLNK 74
Cdd:NF038007 1 MLNMQNAEKcyitKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQNFNLFPHKTVLNNIILAPKLLN---KSDLNQLKQealtLLEKVGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGvakKERIERVNQ----VLNLFGIDNRRNHKPMQLSGGQQQRVAIARAM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGfAKDVSDKVIFMADGY 213
Cdd:NF038007 157 VSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGK 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
1.32e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 165.62 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGrvifegnELSNHKNNLNKLRQKMGMVF 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 84 QNFNLFPHKTVLNNIILAPKllnksdlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGLK-------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 164 TSALDPEVVYDvlkvMKDL-----AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:PRK11247 161 LGALDALTRIE----MQDLieslwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
6.69e-50 |
|
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: 162.67 E-value: 6.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlnKLRQKM 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK---AARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPK-SEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
9.31e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 169.43 E-value: 9.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnHKNNLNKLRQKMG 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILA--PKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
1.05e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 164.03 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS--EETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQN-FNLFPHKTVLNNIILApkLLN----KSDLNQLKQEALtllEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:PRK13635 84 GMVFQNpDNQFVGATVQDDVAFG--LENigvpREEMVERVDQAL---RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGM-TMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-217 |
1.48e-49 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 162.29 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKF--GK--NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLR-QKM 79
Cdd:PRK11629 10 NLCKRYqeGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKViFMADGYVIEE 217
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
2.20e-49 |
|
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: 161.69 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLeTPTNGRVIFEGNELSN---HKnnlnklR 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAiSGLL-PPRSGSIRFDGEDITGlppHR------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVF--QNFNLFPHKTVLNNIILAPKLL-NKSDLNQLKQEALTLLEKvgLEDKANVYPSQLSGGQKQRVAIARALAM 153
Cdd:COG0410 76 ARLGIGYvpEGRRIFPSLTVEENLLLGAYARrDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 154 HPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-227 |
4.45e-49 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 164.50 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIeNLNKKFGKNEVlkDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQK-- 78
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIIL----APKLLNKSDLNQLkqeaLTLLekvGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYgrkrAPRAERRISFDEV----VELL---GIGHLLDRRPATLSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGfakDV---SDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLD---EVarlADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
1.86e-48 |
|
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: 158.53 E-value: 1.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNklrqKMGM 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR----RIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSdlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-236 |
2.02e-48 |
|
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: 161.89 E-value: 2.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 32 IIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLlNKSDLN 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAFGLKM-RKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 112 QLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMV 190
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515498091 191 VVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFL 236
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
2.40e-48 |
|
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: 166.86 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhkNNLNKLRQKMG 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFpHKTVLNNIILAPKLLNKSDLNQLkqealtlLEKVGLEDKANVYP-----------SQLSGGQKQRVAIAR 149
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLGRPDASDEELEAA-------LEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
5.12e-48 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 158.71 E-value: 5.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNK----L 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSReLAKrlaiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQ-------NFNLFPH-KTVLNniilapkllnKSDlNQLKQEALTLLEkvgLEDKANVYPSQLSGGQKQRVAI 147
Cdd:COG4604 81 RQENHINSRltvrelvAFGRFPYsKGRLT----------AED-REIIDEAIAYLD---LEDLADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 148 ARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP 226
|
..
gi 515498091 227 PT 228
Cdd:COG4604 227 EV 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
7.26e-48 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 159.13 E-value: 7.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE---VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQ 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT--EENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQN-FNLFPHKTVLNNIilAPKLLNKS-DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:PRK13650 82 KIGMVFQNpDNQFVGATVEDDV--AFGLENKGiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKdVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
1.33e-47 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 157.97 E-value: 1.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMG 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWS--PWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNL-FPHkTVLNNIIL--APKLLNKSDLNQLKQEALtllEKVGLEDKANVYPSQLSGGQKQRVAIARALA----- 152
Cdd:COG4559 79 VLPQHSSLaFPF-TVEEVVALgrAPHGSSAAQDRQIVREAL---ALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 153 --MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPThq 230
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDEL-- 232
|
....*....
gi 515498091 231 rtqnfLSRV 239
Cdd:COG4559 233 -----LERV 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-238 |
4.61e-47 |
|
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: 163.78 E-value: 4.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLL---ETPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFpHK 92
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLL---ALLlrfLDPQSGSITLGGVDLRDL--DEDDLRRRIAVVPQRPHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILA-PkllNKSDlnqlkQEALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:COG4987 424 TLRENLRLArP---DATD-----EELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQspTHQRTQNFLSR 238
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLA--QNGRYRQLYQR 569
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-225 |
1.42e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 156.06 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN--LNKLRQKMGMVFQnfnlFPH--- 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQIRKKVGLVFQ----FPEsql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 --KTVLNNIILAPKL--LNKSDLNQLKQEALTLlekVGL-EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSA 166
Cdd:PRK13649 99 feETVLKDVAFGPQNfgVSQEEAEALAREKLAL---VGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 167 LDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK13649 176 LDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
5-239 |
2.15e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 158.66 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 5 ENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN-NLNKLR-QKMGMV 82
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaELREVRrKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQNFNLFPHKTVLNNIILAPKLLNKSdLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGIN-AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 163 PTSALDPEVVYDVL-KVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK10070 191 AFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
2.70e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 156.01 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN------ 70
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 ----------------NLNKLRQKMGMVFQ--NFNLFpHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGL-EDKAN 131
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 132 VYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMAD 211
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|..
gi 515498091 212 GYVIEEGSPQQI 223
Cdd:PRK13651 241 GKIIKDGDTYDI 252
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
4.19e-46 |
|
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: 151.04 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHkNNLNKLRQKMGM 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-SPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQnfnlfphktvlnniilapkllnksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVI 215
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-227 |
4.52e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 154.99 E-value: 4.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFG-----KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN--LNK 74
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQnfnlFPH-----KTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIA 148
Cdd:PRK13641 83 LRKKVSLVFQ----FPEaqlfeNTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
5.03e-46 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.81 E-value: 5.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLL---ETPTNGRVIFEGNELsNHKNNLNKLRQ 77
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL---MKILyglYQPDSGEILIDGKPV-RIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIILA--PKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQ 222
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-236 |
5.54e-46 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 154.15 E-value: 5.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGN---ELSNHKnnLNKLRQ 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSR--LYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIilAPKLLNKSDLNQ--LKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNV--AYPLREHTQLPAplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIfQSPTHQRTQN 234
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL-QANPDPRVRQ 241
|
..
gi 515498091 235 FL 236
Cdd:PRK11831 242 FL 243
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
1.13e-45 |
|
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: 151.09 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLnklRQKMG 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY---RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNksdLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYG---LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-239 |
1.26e-45 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 152.88 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL-----ETPTNGRVIFEGNELSNHKNNLNKLR 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPhKTVLNNIILAPKLLN---KSDLNQLKQEALTLLEkVGLEDKANVYPS--QLSGGQKQRVAIARAL 151
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpKLEIDDIVESALKDAD-LWDEIKHKIHKSalDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLA-KEGMTMVVVTHEMGFAKDVSDKVIFMAD-----GYVIEEGSPQQIFQ 225
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|....*
gi 515498091 226 SPTHQRTQNF-LSRV 239
Cdd:PRK14258 246 SPHDSRTREYvLSRL 260
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-221 |
1.51e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 160.66 E-value: 1.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQK-MGMVFQNFNLFPHK 92
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV 172
Cdd:PRK10535 102 TAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 515498091 173 YDVLKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQ 221
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-225 |
1.56e-45 |
|
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: 151.92 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 14 NEVLKDINLEIKKGEVLAIIGPSGSGKSTllrCMNLLE---TPTNGRVIFEGNELSNhkNNLNKLRQKMGMVFQNFNLFP 90
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDGVDIRD--LNLRWLRSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 hKTVLNNIilapkLLNKSDLNQLKQEALTLLEK-----VGLEDKANV----YPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03249 91 -GTIAENI-----RYGKPDATDEEVEEAAKKANihdfiMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPE---VVYDVLkvmkDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:cd03249 165 EATSALDAEsekLVQEAL----DRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-218 |
1.56e-45 |
|
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: 151.11 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 19 DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknnLNKLRQKMGMVFQNFNLFPHKTVLNNI 98
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA----APPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 99 ILA--PKLlnksDLNQLKQEAL-TLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDV 175
Cdd:cd03298 92 GLGlsPGL----KLTAEDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515498091 176 LKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03298 168 LDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-222 |
1.74e-45 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 152.47 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLET---PTNGRVIFEGNELSNH---KNNLNK 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 LRQKMGMVFQNFNLFPHKTVLNNIILAPklLNKSDL---------NQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRV 145
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGA--LGSTPFwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 146 AIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAK-EGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQ 222
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
2.15e-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: 150.98 E-value: 2.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnlNKLRQKMGM 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP---REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPG-AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 162 EPTSALDPEV---VYDVLKVMKDlaKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:cd03265 157 EPTIGLDPQTrahVWEYIEKLKE--EFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-222 |
2.24e-45 |
|
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: 151.61 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFG---KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMG 80
Cdd:cd03253 1 IEFENVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFpHKTVLNNIILApkllnksDLNQLKQEALTLLEKVGLEDKANVYPSQ-----------LSGGQKQRVAIAR 149
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQ 222
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-223 |
3.47e-45 |
|
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: 152.93 E-value: 3.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 9 KKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknNLNKLRQKMGMVFQNFNL 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR---EPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 89 FPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:TIGR01188 78 DEDLTGRENLEMMGRLYGLPK-DEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 169 P---EVVYDVLKVMKdlaKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:TIGR01188 157 PrtrRAIWDYIRALK---EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
3.48e-45 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 150.04 E-value: 3.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGeVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlnKLRQKMGM 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ---KLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTV---LNNIILAPKLLNKsdlnQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:cd03264 77 LPQEFGVYPNFTVrefLDYIAWLKGIPSK----EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAkEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
5.66e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 150.02 E-value: 5.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQK 78
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNReVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-223 |
9.29e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.73 E-value: 9.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFgknEVLK-DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsNHkNNLNKLRQKM 79
Cdd:PRK10771 1 MLKLTDITWLY---HHLPmRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ---DH-TTTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIIL--APKL-LNKSDLNQLKQEAltllEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNIGLglNPGLkLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-228 |
9.48e-45 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 150.31 E-value: 9.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRcmnLLE---TPTNGRVIFEGNELSNHKnnLNKLRQ 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLR---ALSgelSPDSGEVRLNGRPLADWS--PAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNL-FPHkTVLnNII---LAPKLLNKSDLNQLKQEALTLLEKVGLEDKAnvYPsQLSGGQKQRVAIARALA- 152
Cdd:PRK13548 77 RRAVLPQHSSLsFPF-TVE-EVVamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 153 -----MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
..
gi 515498091 227 PT 228
Cdd:PRK13548 232 ET 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-219 |
2.26e-44 |
|
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: 148.83 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlNKLRQKMGMV 82
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH-ERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKvgLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGS 219
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
3.67e-44 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 148.38 E-value: 3.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlnklrqKMgMVFQNFNLFPHKTVLN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD------RM-VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 97 NIILAPKLLNKsDLNQLKQEALT--LLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYD 174
Cdd:TIGR01184 74 NIALAVDRVLP-DLSKSERRAIVeeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 515498091 175 VL-KVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
4.36e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 149.04 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL------ETPTNGRVIFEGNELsnHKNNLNKLRQKMGMVFQNFNLF 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDI--FQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 PHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGL----EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 166 ALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFL 236
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-226 |
7.76e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 149.16 E-value: 7.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVifEGNELSNHKNNLNK----LRQKMGMVFQnfnlFP 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV--TVDDITITHKTKDKyirpVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 HK-----TVLNNIILAPKLLNKsDLNQLKQEALTLLEKVGLE-DKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPT 164
Cdd:PRK13646 95 ESqlfedTVEREIIFGPKNFKM-NLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 165 SALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-227 |
9.11e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 150.95 E-value: 9.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRvIFEGNELsnhKNNLNKLRQKMGM 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-LFIGEKR---MNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLLEKVGLEDKAnvyPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLagAKKEEINQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 160 FDEPTSALDP----EVVYDVLKVMKDLakeGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK11000 157 LDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
1.27e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 147.10 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnklRQ 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHK------RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGM--------VFQNFnlfphkTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:COG1137 77 RLGIgylpqeasIFRKL------TVEDNILAVLELRKLSK-KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTmVVVT----HEMgfaKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRET---LGICDRAYIISEGKVLAEGTPEEILN 225
|
..
gi 515498091 226 SP 227
Cdd:COG1137 226 NP 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
1.57e-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: 146.53 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnklRQK 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmHK------RAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVF--QNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENILAVLEIRGLSK-KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
3.39e-43 |
|
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: 152.65 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTL---LRCMNLLEtPTNGRVIFE----------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYE-PTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 62 ------GNELSNHKNNL--------NKLRQKMGMVFQ-NFNLFPHKTVLNNIILAPKLLNKSDLNQLKQeALTLLEKVGL 126
Cdd:TIGR03269 80 epcpvcGGTLEPEEVDFwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGR-AVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 127 EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDK 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....*...
gi 515498091 206 VIFMADGYVIEEGSPQQI 223
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEV 256
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-222 |
4.11e-43 |
|
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: 154.34 E-value: 4.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:TIGR03797 452 IEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA--GLDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPhKTVLNNIILApkllnksdlNQLKQ-EALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAI 147
Cdd:TIGR03797 530 GVVLQNGRLMS-GSIFENIAGG---------APLTLdEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 148 ARALAMHPDIILFDEPTSALDPEVvydVLKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQ 222
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRT---QAIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
7.34e-43 |
|
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: 144.68 E-value: 7.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE-VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLRQKMG 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPhKTVLNNIILAPKLLNKSDLNQLKQE--ALTLLEKV--GLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:cd03254 81 VVLQDTFLFS-GTIMENIRLGRPNATDEEVIEAAKEagAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-237 |
9.31e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 146.01 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNG-----RVIFEGNELSNHKNNLnKLRQKMG 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL-EFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPhKTVLNNI---ILAPKLLNKSDLNQLKQEALTlleKVGL----EDKANVYPSQLSGGQKQRVAIARALAM 153
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVlagVRAHKLVPRKEFRGVAQARLT---EVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 154 HPDIILFDEPTSALDPEVVYDVLKVMKDLAkEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQ 233
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
....
gi 515498091 234 NFLS 237
Cdd:PRK14271 260 RYVA 263
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-240 |
9.33e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.39 E-value: 9.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlnklR 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 qkmGMVFQNFNLFPHKTVLNNIILAPKLlNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 157 IILFDEPTSALDP-------EVVYDVlkvmkdLAKEGMTMVVVTHemgfakDVsDKVIFMADGYVIEEGSPQQIfqspTH 229
Cdd:COG4525 155 FLLMDEPFGALDAltreqmqELLLDV------WQRTGKGVFLITH------SV-EEALFLATRLVVMSPGPGRI----VE 217
|
250
....*....|.
gi 515498091 230 QRTQNFLSRVL 240
Cdd:COG4525 218 RLELDFSRRFL 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.69e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 146.53 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE-----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRV----IFEGNELSNHKN- 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 ---------NLNKLRQKMGMVFQ--NFNLFpHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGL-EDKANVYPSQLS 138
Cdd:PRK13631 101 tnpyskkikNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 139 GGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|
gi 515498091 219 SPQQIFQSPT 228
Cdd:PRK13631 259 TPYEIFTDQH 268
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-236 |
1.74e-42 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 146.43 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEV----LKDINLEIKKGEVLAIIGPSGSGKS-TLLRCMNLLETPtnGRVIFEgnELSNHKNNLNKL 75
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAE--KLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQK---------MGMVFQN--FNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKA---NVYPSQLSGGQ 141
Cdd:PRK11022 79 SEKerrnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLA-KEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250
....*....|....*.
gi 515498091 221 QQIFQSPTHQRTQNFL 236
Cdd:PRK11022 239 HDIFRAPRHPYTQALL 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-222 |
1.90e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 143.01 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMN-LLETP--TNGRVIFEGNELsnhkNNLNKLRQ 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRL----TALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFPHKTVLNNIILA-PKLLNKsdlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:COG4136 77 RIGILFQDDLLFPHLSVGENLAFAlPPTIGR---AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 157 IILFDEPTSALDPEVVYDVLK-VMKDLAKEGMTMVVVTHemgfakDVSDKVifmADGYVIEEGSPQQ 222
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH------DEEDAP---AAGRVLDLGNWQH 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-227 |
2.66e-42 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 146.80 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 19 DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNEL--SNHKNNLNKLRQKMGMVFQNFNLFPHKTVLN 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 97 NIILAPKLLNKSDLNQLKQEALTLLekvGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVL 176
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515498091 177 KVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
4.52e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 144.22 E-value: 4.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGK-NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKM 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQ--NFNLFPhKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPE-DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
5.22e-42 |
|
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: 142.03 E-value: 5.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnlnklRQKMGM 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKL--LNKSDLnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLkgLKKEEA---RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-239 |
6.19e-42 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 145.23 E-value: 6.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 18 KDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN-LNKLRQKMGMVFQN--FNLFPHKTV 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDeWRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 lNNIILAPKLLNKSDLN--QLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEV 171
Cdd:PRK15079 118 -GEIIAEPLRTYHPKLSrqEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 172 VYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK15079 197 QAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
8.83e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 144.10 E-value: 8.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNK------ 74
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD--PEDRRRigylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 ---LRQKMgmvfqnfnlfphkTVLNNII-LApKL--LNKSDlnqLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIA 148
Cdd:COG4152 79 ergLYPKM-------------KVGEQLVyLA-RLkgLSKAE---AKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVyDVLK-VMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNV-ELLKdVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
9.34e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 143.20 E-value: 9.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGK-NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHkNNLNKLRQKM 79
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNL-FPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEkVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAE-IGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQSPTHQ 230
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-226 |
1.09e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 142.97 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQN-FNLFPHKTVL 95
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD--NFEKLRKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 96 NNIilAPKLLNKS-DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYD 174
Cdd:PRK13648 103 YDV--AFGLENHAvPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 175 VLKVMKDLAKE-GMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13648 181 LLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
1.60e-41 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 139.66 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPhKTVLNNIilapkllnksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03246 79 GYLPQDDELFS-GSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 160 FDEPTSALDPE---VVYDVLKVMKdlaKEGMTMVVVTHEMGFAKDVsDKVIFMADGYV 214
Cdd:cd03246 120 LDEPNSHLDVEgerALNQAIAALK---AAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
2.40e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 142.25 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT--KENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFN--LFPhKTVLNNIILAPKLLNKsDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK13652 81 GLVFQNPDdqIFS-PTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
2.68e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.18 E-value: 2.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGK-NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLRQKMG 80
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV--NAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFN--LFPhKTVLNNIILAPK--LLNKSDLNQLKQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK13647 83 LVFQDPDdqVFS-STVWDDVAFGPVnmGLDKDEVERRVEEALKA---VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQ 221
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-222 |
3.15e-41 |
|
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: 140.83 E-value: 3.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLLE---TPTNGRVIFEGNELSNHKnnLNKLR 76
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPrfyDVDSGRILIDGHDVRDYT--LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFpHKTVLNNI------------ILAPKLLNKSDLNQLKQEaltllekvGLEDKANVYPSQLSGGQKQR 144
Cdd:cd03251 76 RQIGLVSQDVFLF-NDTVAENIaygrpgatreevEEAARAANAHEFIMELPE--------GYDTVIGERGVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 145 VAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQ 222
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-225 |
5.70e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 141.79 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFeGNEL---SNHKNNL 72
Cdd:PRK13643 1 MIKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVvssTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 NKLRQKMGMVFQnfnlFPH-----KTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKA-NVYPSQLSGGQKQRVA 146
Cdd:PRK13643 80 KPVRKKVGVVFQ----FPEsqlfeETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-226 |
1.06e-40 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 139.54 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhkNNLNKLRQKM 79
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAL--ADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFpHKTVLNNIIL------------APKLLNKSD-LNQLKQEALTLLEKVGledkanvypSQLSGGQKQRVA 146
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNIALadpgmsmervieAAKLAGAHDfISELPEGYDTIVGEQG---------AGLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-225 |
1.15e-40 |
|
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: 147.71 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNNLNKLRQKMGMVFQNFNLFpHKTVL 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI--RQIDPADLRRNIGYVPQDPRLF-YGTLR 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 96 NNIILAPKLLNKSDLnqlkQEALTLlekVGLEDKANVYPS-----------QLSGGQKQRVAIARALAMHPDIILFDEPT 164
Cdd:TIGR03375 557 DNIALGAPYADDEEI----LRAAEL---AGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 165 SALDPEVVYDVLKVMKDLAkEGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQVLE 688
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-227 |
3.12e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 141.52 E-value: 3.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNG------RVIfegnelsnhkNNLN 73
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGeiwiggRVV----------NELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 KLRQKMGMVFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEALTLLEKVGLEDKAnvyPSQLSGGQKQRVAIARAL 151
Cdd:PRK11650 73 PADRDIAMVFQNYALYPHMSVRENMAYGLKIrgMPKAEIEERVAEAARILELEPLLDRK---PRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 152 AMHPDIILFDEPTSALDPEvvydvLKV-M----KDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAK-----LRVqMrleiQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
..
gi 515498091 226 SP 227
Cdd:PRK11650 225 KP 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
3.13e-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: 137.50 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGneLSNHKNNLnKLR 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPA-EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHKTVLNNiilapkLLNKSDLNQLKQEALT-----LLEKVGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTAREN------LEYFAGLYGLKGDELTarleeLADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-234 |
3.28e-40 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 139.05 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNK-LRQKMGMVFQ 84
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKaFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 N----FNlfPHKTVlnNIILAPKLLNKSDLNQLKQEA--LTLLEKVGLEDK-ANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK10419 97 DsisaVN--PRKTV--REIIREPLRHLLSLDKAERLAraSEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG--SPQQIFQSPTHQRTQN 234
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQpvGDKLTFSSPAGRVLQN 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-236 |
1.01e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 143.31 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGK----NEVLKDINLEIKKGEVLAIIGPSGSGKS-TLLRCMNLLETP----TNGRVIFEGNELSN-HKN 70
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHaSEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 71 NLNKLR-QKMGMVFQN--FNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKA---NVYPSQLSGGQKQR 144
Cdd:PRK15134 85 TLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 145 VAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
250
....*....|...
gi 515498091 224 FQSPTHQRTQNFL 236
Cdd:PRK15134 245 FSAPTHPYTQKLL 257
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-228 |
2.37e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 137.24 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 13 KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETP---TNGRVIFEGNELSnhKNNLNKLRQKMGMVFQN-FNL 88
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLT--AKTVWDIREKVGIVFQNpDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 89 FPHKTVLNNIilAPKLLNKS-DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSAL 167
Cdd:PRK13640 97 FVGATVGDDV--AFGLENRAvPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 168 DPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAkDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:PRK13640 175 DPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-239 |
3.81e-39 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 137.93 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 19 DINLEIKKGEVLAIIGPSGSGKS-TLLRCMNLLetPTNGRV----IFEGNELSNHKNN-LNKLR-QKMGMVFQN--FNLF 89
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLPEKeLNKLRaEQISMIFQDpmTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 PHKTV---LNNIILAPKLLNKSdlnQLKQEALTLLEKVGLED---KANVYPSQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK09473 112 PYMRVgeqLMEVLMLHKGMSKA---EAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 164 TSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-237 |
5.74e-39 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 141.38 E-value: 5.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 7 LNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKST----LLRCMNlletpTNGRVIFEGNELSN-HKNNLNKLRQKMGM 81
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlNRRQLLPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFN--LFPHKTVLNniILAPKL-LNKSDLNQLKQEA--LTLLEKVGLE-DKANVYPSQLSGGQKQRVAIARALAMHP 155
Cdd:PRK15134 367 VFQDPNssLNPRLNVLQ--IIEEGLrVHQPTLSAAQREQqvIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQN 234
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQ 524
|
...
gi 515498091 235 FLS 237
Cdd:PRK15134 525 LLA 527
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-226 |
6.95e-39 |
|
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: 135.21 E-value: 6.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRV--IFeGNELSNHknNLNKLRQK 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrLF-GERRGGE--DVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMV----FQNFNlfPHKTVLNnIIL-----APKLLNKSDLNQlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:COG1119 80 IGLVspalQLRFP--RDETVLD-VVLsgffdSIGLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEG-MTMVVVTH---EM--GFakdvsDKVIFMADGYVIEEGSPQQI 223
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKEEV 230
|
...
gi 515498091 224 FQS 226
Cdd:COG1119 231 LTS 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-240 |
7.21e-39 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 135.44 E-value: 7.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNE--------LSNHKNNL 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 nKLRQKMGMVFQNF--NLFPHKTVLNNIilAPKLLNKSDLN--QLKQEALTLLEKVGLE-DKANVYPSQLSGGQKQRVAI 147
Cdd:PRK11701 86 -LLRTEWGFVHQHPrdGLRMQVSAGGNI--GERLMAVGARHygDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 148 ARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDD 242
|
250
....*....|....
gi 515498091 227 PTHQRTQNFLSRVL 240
Cdd:PRK11701 243 PQHPYTQLLVSSVL 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-228 |
1.79e-38 |
|
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: 139.94 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFE-GNELSN--HKNNL 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDmtKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 NKLRQK--MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKqeALTLLEKVGLEDKA-----NVYPSQLSGGQKQRV 145
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMK--AVITLKMVGFDEEKaeeilDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 146 AIARALAMHPDIILFDEPTSALDPEVVYDVLK-VMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
....
gi 515498091 225 QSPT 228
Cdd:TIGR03269 517 EELT 520
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-214 |
2.12e-38 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 132.68 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 21 NLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGnelSNHkNNLNKLRQKMGMVFQNFNLFPHKTVLNNIIL 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND---QSH-TGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 101 A--PKLlnksDLNQLKQEAL-TLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLK 177
Cdd:TIGR01277 94 GlhPGL----KLNAEQQEKVvDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 515498091 178 VMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:TIGR01277 170 LVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-227 |
5.26e-38 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 133.19 E-value: 5.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNE---LSNHKnnlnklRQ 77
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQ------IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMV--FQNFNLFPHKTVLNNIILA----------PKLLNKSDLNQLKQEAL----TLLEKVGLEDKANVYPSQLSGGQ 141
Cdd:PRK11300 79 RMGVVrtFQHVRLFREMTVIENLLVAqhqqlktglfSGLLKTPAFRRAESEALdraaTWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
....*..
gi 515498091 221 QQIFQSP 227
Cdd:PRK11300 239 EEIRNNP 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
6.52e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 139.61 E-value: 6.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKS-TLLRCMNLLETPT------------NGRVIFEGN 63
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGglvqcdkmllrrRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 64 ELSNHKnnLNKLR-QKMGMVFQN--FNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANV---YPSQL 137
Cdd:PRK10261 92 EQSAAQ--MRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 138 SGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIE 216
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVE 249
|
250 260
....*....|....*....|...
gi 515498091 217 EGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTRALLAAV 272
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-237 |
1.42e-37 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 132.22 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKN---------EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnHKNN 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 LNKLRQKMGMVFQN--FNLFPHKTVlNNIILAPKLLNkSDLNQLKQEA--LTLLEKVGL-EDKANVYPSQLSGGQKQRVA 146
Cdd:PRK15112 82 YSYRSQRIRMIFQDpsTSLNPRQRI-SQILDFPLRLN-TDLEPEQREKqiIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDL-AKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|..
gi 515498091 226 SPTHQRTQNFLS 237
Cdd:PRK15112 240 SPLHELTKRLIA 251
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
1.56e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 131.05 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNE----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKL 75
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 R-QKMGMVFQNFNLFPHKTVLNNIILaPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVsDKVIFMADGYVIEE 217
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARC-DRRLRLVNGQLQEE 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-218 |
2.33e-37 |
|
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: 130.40 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 13 KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMGMVFQNFNLFpHK 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR--QLDPADLRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILApkLLNKSDlnqlkQEALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03245 93 TLRDNITLG--APLADD-----ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAkEGMTMVVVTHEMGFAkDVSDKVIFMADGYVIEEG 218
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-218 |
3.60e-37 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 128.82 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMN--LLETPTNGRVIFEGnelsnHKNNLNKLRQKMGMVFQNFNLFPHK 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING-----RPLDKRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILAPKLlnksdlnqlkqealtllekvgledkanvypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV 172
Cdd:cd03213 98 TVRETLMFAAKL------------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 173 YDVLKVMKDLAKEGMTMVVVTH----EMgFAKdvSDKVIFMADGYVIEEG 218
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHqpssEI-FEL--FDKLLLLSQGRVIYFG 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-225 |
3.90e-37 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 130.90 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlnKLRQKMG 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSR--QLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNfNLFPHKTVLNNIIL---APKL-----LNKSDlNQLKQEALtllEKVGLEDKANVYPSQLSGGQKQRVAIARALA 152
Cdd:PRK11231 80 LLPQH-HLTPEGITVRELVAygrSPWLslwgrLSAED-NARVNQAM---EQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-218 |
8.23e-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: 128.93 E-value: 8.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 8 NKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLR---CMNLLETPTNGRVIFEGNELSNHKnnlnkLRQKMGMVFQ 84
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDaisGRVEGGGTTSGQILFNGQPRKPDQ-----FQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 NFNLFPHKTVLNNIILAPKLLN---KSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMG---FakDVSDKVIFMADGYVIEEG 218
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-225 |
1.94e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 129.05 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnlnklrQKMG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-------AERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKSDLnQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKM-QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 161 DEPTSALDP----EVVYDVLKVMKDLAKEgmtMVVVTHEMgfakdvsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK11248 153 DEPFGALDAftreQMQTLLLKLWQETGKQ---VLLITHDI-------EEAVFMATELVLLSPGPGRVVE 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-237 |
2.18e-36 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 128.66 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 18 KDINLEIKKGEVLAIIGPSGSGKStlLRCMNLLE------TPTNGRVIFEGNELSnhknnLNKLRQKM-GMVFQN----F 86
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA-----PCALRGRKiATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 87 NlfPHKTVLNNIILAPKLLNKSDLNQLKQEALtllEKVGLEDKANV---YPSQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK10418 93 N--PLHTMHTHARETCLALGKPADDATLTAAL---EAVGLENAARVlklYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 164 TSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLS 237
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
2.81e-36 |
|
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: 127.55 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF------GKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM--NLLetPTNGRVIFegnelsNHKNN 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILV------RHDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 ------------LNKLRQKMGMVFQNFNLFPHKTVLNnIILAPKLLNKSDLNQLKQEALTLLEKVGL-EDKANVYPSQLS 138
Cdd:COG4778 76 wvdlaqaspreiLALRRRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 139 GGQKQRVAIARALAMHPDIILFDEPTSALDP---EVVYDVLkvmKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVELI---EEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-226 |
3.52e-36 |
|
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: 134.87 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN--EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:TIGR01846 456 ITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA--IADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFpHKTVLNNI------------ILAPKLLNKSD-LNQLKQEALTLLEKVGledkanvypSQLSGGQKQRVA 146
Cdd:TIGR01846 534 GVVLQENVLF-SRSIRDNIalcnpgapfehvIHAAKLAGAHDfISELPQGYNTEVGEKG---------ANLSGGQRQRIA 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLAL 681
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
1.15e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 126.77 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLnklRQKMG 80
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE---IARLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MV--FQNFNLFPHKTVLNNIILA---PKLLNKSDLNQLKQEALT----LLEKVGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:COG4674 87 IGrkFQKPTVFEELTVFENLELAlkgDRGVFASLFARLTAEERDrieeVLETIGLTDKADRLAGLLSHGQKQWLEIGMLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:COG4674 167 AQDPKLLLLDEPVAGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
2.95e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.23 E-value: 2.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlnKLRQKMGM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR---HARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSA-AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-194 |
1.25e-34 |
|
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: 129.40 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGneLSNHKNNLNKLRQKMGMVFQNFNLFpH 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG--VPVSSLDQDEVRRRVSVCAQDAHLF-D 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNIILAPKllNKSDlnqlkQEALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:TIGR02868 423 TTVRENLRLARP--DATD-----EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLL 495
|
170 180 190
....*....|....*....|....*....|....
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDlAKEGMTMVVVTH 194
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
2.83e-34 |
|
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: 128.56 E-value: 2.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMG 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA--DADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPhKTVLNNIILAPKLLNKSDLnqlkQEALtllEKVGLEDKANVYP-----------SQLSGGQKQRVAIAR 149
Cdd:TIGR02857 400 WVPQHPFLFA-GTIAENIRLARPDASDAEI----REAL---ERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAkEGMTMVVVTHEMGFAKDVsDKVIFM 209
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-219 |
4.92e-34 |
|
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: 121.74 E-value: 4.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLnklrQKMGM 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT--RKDL----HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDlnqlkQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:TIGR03740 75 LIESPPLYENLTARENLKVHTTLLGLPD-----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGS 219
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
5.09e-34 |
|
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: 120.50 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLnklRQKM 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFphktvlnniilapkllnksdlnqlkqeALTLLEKVGLedkanvypsQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03247 78 SVLNQRPYLF---------------------------DTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEG 218
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
7.63e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----------------------GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 59 IFEGN-----ELsnhknnlnklrqkmGMVFQnfnlfPHKTVLNNIILAPKLLNKSdlnqlKQEALTLLEKV----GLEDK 129
Cdd:COG1134 84 EVNGRvsallEL--------------GAGFH-----PELTGRENIYLNGRLLGLS-----RKEIDEKFDEIvefaELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 130 ANV----YPSqlsgGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDK 205
Cdd:COG1134 140 IDQpvktYSS----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDR 215
|
250 260
....*....|....*....|
gi 515498091 206 VIFMADGYVIEEGSPQQIFQ 225
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIA 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
1.63e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 121.35 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGK---NE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnl 72
Cdd:COG1101 1 MLELKNLSKTFNPgtvNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpeYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 nklRQKM-GMVFQNFNL--FPHKTVLNNIILAPK------L---LNKSDLNQLKqEALTLLEkVGLEDKANVYPSQLSGG 140
Cdd:COG1101 78 ---RAKYiGRVFQDPMMgtAPSMTIEENLALAYRrgkrrgLrrgLTKKRRELFR-ELLATLG-LGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 141 QKQrvaiARALAM----HPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVI 215
Cdd:COG1101 153 QRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-220 |
1.91e-33 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 120.94 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLL-----ETPTNGRVIFEG---NELSNHKnnlnk 74
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTL---AKVLmghpkYEVTSGSILLDGediLELSPDE----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 75 lRQKMG--MVFQNFNLFPHKTVLN--NIILAPKLLNKSDLNQLKQEALTLLEKVGLEDK-----ANVypsQLSGGQKQRV 145
Cdd:COG0396 74 -RARAGifLAFQYPVEIPGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLDEDfldryVNE---GFSGGEKKRN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 146 AIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVS-DKVIFMADGYVIEEGSP 220
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSGGK 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
2.20e-33 |
|
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: 119.50 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE-----VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMnLLETP-TNGRVIFEGnelsnhknnlnkl 75
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGELEkLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 rqKMGMVFQN---FNLfphkTVLNNIILA----PKLLNK--------SDLNQLKQEALTLlekVGlEDKANvypsqLSGG 140
Cdd:cd03250 67 --SIAYVSQEpwiQNG----TIRENILFGkpfdEERYEKvikacalePDLEILPDGDLTE---IG-EKGIN-----LSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 141 QKQRVAIARALAMHPDIILFDEPTSALDPEV---VYDvlKVMKDLAKEGMTMVVVTHEMGFAKDVsDKVIFMADG 212
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVgrhIFE--NCILGLLLNNKTRILVTHQLQLLPHA-DQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-233 |
3.05e-33 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 126.02 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFPh 91
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW--DREELGRHIGYLPQDVELFD- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNI-----------ILAPKLLNKSDL-NQLKQEALTLLEKVGledkanvypSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:COG4618 420 GTIAENIarfgdadpekvVAAAKLAGVHEMiLRLPDGYDTRIGEGG---------ARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQSPTHQRTQ 233
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV-DKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-223 |
8.93e-33 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 119.71 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 5 ENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlNKLRQKMGMVFQ 84
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 NFNLfPHKTVLNNIILAPKLLNKSDLNQLKQE---ALT-LLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:PRK10253 89 NATT-PGDITVQELVARGRYPHQPLFTRWRKEdeeAVTkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-228 |
9.78e-33 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.22 E-value: 9.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 13 KNEVLKDINLEIKKGEVLAIIGPSGSGKSTllrCMNLLET---PTNGRVIFEGNELS--NHKNnlnkLRQKMGMVFQNFN 87
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVqyDHHY----LHRQVALVGQEPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 88 LFpHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLED--KANVYP--SQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:TIGR00958 566 LF-SGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgyDTEVGEkgSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 164 TSALDPEVVYDVLKVMKdlaKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:TIGR00958 645 TSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-224 |
1.30e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 119.34 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLNKLRQKMG 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNfnlfPHKTVLNNII---LAPKLLN----KSDLNQLKQEALTLLEKVGLEDKanvyPSQ-LSGGQKQRVAIARALA 152
Cdd:PRK13638 81 TVFQD----PEQQIFYTDIdsdIAFSLRNlgvpEAEITRRVDEALTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIF 224
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-239 |
1.64e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.20 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 13 KNEV--LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQKMGMVFQN--FN 87
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 88 LFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLE-DKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSA 166
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 167 LDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQRTQNFLSRV 239
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
5.80e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.17 E-value: 5.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlnKLRQKMGM 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR---LARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNksdLNQLKQEAL--TLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLLVFGRYFG---MSTREIEAVipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-231 |
1.51e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 115.76 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 5 ENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN---HKnnlnKLRQKMGM 81
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplHA----RARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPTHQR 231
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
1.57e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 117.03 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMN-LLETPTNGRVIFEGNELSNHKN--NLN 73
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNgLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 KLRQKMGMVFQ--NFNLFpHKTVLNNIILAPKLLNkSDLNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARA 150
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLF-QETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 151 LAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
2.20e-31 |
|
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: 114.90 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLEtPTNGRVIFEGNELSnhKNNLNKLRQK 78
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAlFRLVE-LSSGSILIDGVDIS--KIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPhKTVLNNiiLAP-------KLLNKSDLNQLKQEALTLLEkvGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:cd03244 80 ISIIPQDPVLFS-GTIRSN--LDPfgeysdeELWQALERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 152 AMHPDIILFDEPTSALDPEVvyDvlKVMKDLAKEGM---TMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSP 220
Cdd:cd03244 155 LRKSKILVLDEATASVDPET--D--ALIQKTIREAFkdcTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
2.72e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDIN---LEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQ 77
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQN-FNLFPHKTVLNNII--LAPKLLNKSDLNQLKQEALTlleKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:PRK13642 82 KIGMVFQNpDNQFVGATVEDDVAfgMENQGIPREEMIKRVDEALL---AVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLA-KEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-220 |
2.87e-31 |
|
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: 113.78 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM--NLLETPTNGRVIFEGNELSNHKNNlnkLRQKM 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPE---ERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 G--MVFQNFNLFPHKTVLNNIilapkllnkSDLNqlkqealtllekVGledkanvypsqLSGGQKQRVAIARALAMHPDI 157
Cdd:cd03217 78 GifLAFQYPPEIPGVKNADFL---------RYVN------------EG-----------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTH-EMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
4.03e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 119.78 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNElsnhknnlnklrqKMGMVF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 84 QNFNLFPHKTVLNNII--------------LAPKLLNKSDLNQLKQEAL-----------------TLLEKVGL-EDKAN 131
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgdaelraleaeleELEAKLAEPDEDLERLAELqeefealggweaearaeEILSGLGFpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 132 VYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV-----YdvlkvmkdLAKEGMTMVVVTHEMGFAKDVSDKV 206
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIewleeF--------LKNYPGTVLVVSHDRYFLDRVATRI 219
|
....*.
gi 515498091 207 IFMADG 212
Cdd:COG0488 220 LELDRG 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-196 |
4.63e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.10 E-value: 4.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 11 FGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNE----LSNHKNNLNKL----RQKMGMv 82
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPDSLpltvRDLVAM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 fqnfNLFPHKTVLnniilapKLLNKSDlnqlKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:NF040873 81 ----GRWARRGLW-------RRLTRDD----RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEM 196
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
5.51e-31 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 119.12 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhknnlNKLRQKM- 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-------NKLDHKLa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 -----GMVFQNFNLFPHKTVLNNIILAPKLLNKS------DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIA 148
Cdd:PRK09700 78 aqlgiGIIYQELSVIDELTVLENLYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
7.13e-31 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.64 E-value: 7.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhkNNLNKLRQKMG 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNL---FPHKTVLNnIILAPKLLNKSDLNQLKQEAL-TLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK09536 81 SVPQDTSLsfeFDVRQVVE-MGRTPHRSRFDTWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-212 |
7.24e-31 |
|
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: 112.14 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsNHKNNLNKLRQKMGMV---FQNFNLFPHK 92
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV-TRRSPRDAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILapkllnksdlnqlkqealtllekvgledkanvyPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV 172
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 515498091 173 YDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-225 |
8.03e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.16 E-value: 8.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLLE---TPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFPHk 92
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTrawDPQQGEILLNGQPIADY--SEAALRQAISVVSQRVHLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILAPKllNKSDlNQLkqeaLTLLEKVGLEDKANVYPS----------QLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:PRK11160 429 TLRDNLLLAAP--NASD-EAL----IEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMgFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELLA 562
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-212 |
1.23e-30 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 118.60 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFPh 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW--DRETFGKHIGYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNI------------ILAPKLLNKSDLNQ-LKQEALTLLEKVGledkanvypSQLSGGQKQRVAIARALAMHPDII 158
Cdd:TIGR01842 406 GTVAENIarfgenadpekiIEAAKLAGVHELILrLPDGYDTVIGPGG---------ATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGfAKDVSDKVIFMADG 212
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDG 529
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-227 |
1.24e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 116.13 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIeNLNKKFGknEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN--NLNKLRQK 78
Cdd:PRK11144 1 MLEL-NFKQQLG--DLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiCLPPEKRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQealtLLekvGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK11144 78 IGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVA----LL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-219 |
1.29e-30 |
|
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: 118.67 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMGMVFQNFNLFpHKTV 94
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQVALVSQDVVLF-NDTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LNNIIL-APKLLNKSDLNQLKQEAlTLLEKV-----GLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:TIGR02203 423 ANNIAYgRTEQADRAEIERALAAA-YAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515498091 169 PEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGS 219
Cdd:TIGR02203 502 NESERLVQAALERL-MQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
3.92e-30 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 117.46 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLLETPTNGRVIFEGNELSN-HKNNLNKLRQKMGMVFQNFNLFPHKT 93
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTL---MNALAFRSPKGVKGSGSVLLNgMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIILAPKLLNKSDLNQ-LKQEALT-LLEKVGLEDKANV---YPSQ---LSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKkEKRERVDeVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 166 ALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMG---FakDVSDKVIFMADGYVIEEGSPQQ 222
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-196 |
2.08e-29 |
|
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: 109.87 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTllrCMNLLET---PTNGRVIFEGNELSNHKNNLnkLRQKMGMVFQNFNLFPhK 92
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKY--LHSKVSLVGQEPVLFA-R 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIilAPKLLNKSD--LNQLKQEA-----LTLLEKvGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:cd03248 103 SLQDNI--AYGLQSCSFecVKEAAQKAhahsfISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190
....*....|....*....|....*....|.
gi 515498091 166 ALDPEVVYDVLKVMKDlAKEGMTMVVVTHEM 196
Cdd:cd03248 180 ALDAESEQQVQQALYD-WPERRTVLVIAHRL 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-226 |
2.10e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLLE---TPTNGRVIFEGNELSnhKNNLNKLRQ 77
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQrvfDPQSGRILIDGTDIR--TVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMGMVFQNFNLFpHKTVLNNIILA-PKLLNKSDLNQLKQ-EALTLLEK--VGLEDKANVYPSQLSGGQKQRVAIARALAM 153
Cdd:PRK13657 410 NIAVVFQDAGLF-NRSIEDNIRVGrPDATDEEMRAAAERaQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 154 HPDIILFDEPTSALDPEVVYDVlKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-217 |
2.73e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.35 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKfgknEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnHKNNLNKLRQKMGMV 82
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQN---FNLFPHKTVLNNIILA--PKLLNKS--DLNQLKQEALTLLEKV-----GLEDKAnvypSQLSGGQKQRVAIARA 150
Cdd:COG1129 333 PEDrkgEGLVLDLSIRENITLAslDRLSRGGllDRRRERALAEEYIKRLriktpSPEQPV----GNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 151 LAMHPDIILFDEPTSALDpevV---YDVLKVMKDLAKEGMTMVVVTHEM----GfakdVSDKVIFMADGYVIEE 217
Cdd:COG1129 409 LATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELpellG----LSDRILVMREGRIVGE 475
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-227 |
5.23e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 114.17 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 20 INLEIKKGEVLAIIGPSGSGKSTLLrcmNLLE--TPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFpHKTVLNN 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL--DPESWRKHLSWVGQNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 98 IILAPKLLNKSDLNQLKQEA-----LTLLEKvGLE----DKAnvypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAwvsefLPLLPQ-GLDtpigDQA----AGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 169 pevVYDVLKVMKDL--AKEGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK11174 518 ---AHSEQLVMQALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
1.31e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFeGNELsnhknnlnklrqKMG 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNF-NLFPHKTVLNNII-LAPkllnksdlNQLKQEALTLLEKVGL-EDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:COG0488 382 YFDQHQeELDPDKTVLDELRdGAP--------GGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 158 ILFDEPTSALDPEvvydVLKVMKD-LAK-EGmTMVVVTHEMGFAKDVSDKVIFMADGYVIE 216
Cdd:COG0488 454 LLLDEPTNHLDIE----TLEALEEaLDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-219 |
2.42e-28 |
|
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: 112.22 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMGMVFQNFNLFpHKTV 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT--QASLRAAIGIVPQDTVLF-NDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LNNI------------ILAPKLLNKSDL-NQLKQEALTLLEKVGLedkanvypsQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:COG5265 449 AYNIaygrpdaseeevEAAARAAQIHDFiESLPDGYDTRVGERGL---------KLSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGS 219
Cdd:COG5265 520 EATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
2.53e-28 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 106.85 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF----------------------GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVI 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 60 FEGN-----ELsnhknnlnklrqkmGMVFQnfnlfPHKTVLNNIILAPKLLNKSdlnqlKQEALTLLEKV----GLEDKA 130
Cdd:cd03220 81 VRGRvssllGL--------------GGGFN-----PELTGRENIYLNGRLLGLS-----RKEIDEKIDEIiefsELGDFI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 131 NVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMA 210
Cdd:cd03220 137 DLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
|
....*...
gi 515498091 211 DGYVIEEG 218
Cdd:cd03220 217 KGKIRFDG 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-217 |
1.10e-27 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 105.04 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM--NLLETPTNGRVIFEGNELSnhknnlnklrqkmgmvfqnfnlfPHKT 93
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG-----------------------REAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIilaPKLLNKSDlnqlkqeALTLLEKVGLEDKANVY--PSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEV 171
Cdd:COG2401 102 LIDAI---GRKGDFKD-------AVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515498091 172 VYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVS-DKVIFMADGYVIEE 217
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-220 |
3.26e-27 |
|
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: 109.72 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKF---GKNEVLKdINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhKNNLNKLRQKMG 80
Cdd:TIGR01257 931 VKNLVKIFepsGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKS-DLNQLKQEALtlLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSwEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 160 FDEPTSALDP---EVVYDVLkvMKdlAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSP 220
Cdd:TIGR01257 1085 LDEPTSGVDPysrRSIWDLL--LK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
3.97e-27 |
|
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: 101.37 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFegnelsnhknnlnklrqkmgm 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 vfqnfnlfpHKTVlnniilapkllnksdlnqlkqealtlleKVGledkanvYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03221 60 ---------GSTV----------------------------KIG-------YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 515498091 162 EPTSALDPE---VVYDVLKvmkdlAKEGmTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:cd03221 96 EPTNHLDLEsieALEEALK-----EYPG-TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-212 |
9.65e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.32 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLLET--PT---NGRVIFEGNELsnHKNNLNKLRQK-M 79
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTL---MKVLSGvyPHgtyEGEIIFEGEEL--QASNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILAPKLLNKS--DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
1.30e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.03 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlNKLRQKMG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKvgLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKvifmadGYVIEEG 218
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR------GYVLENG 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-212 |
4.51e-26 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 105.38 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsNHKNNLNKLRQKMGMVFQN 85
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALAAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 86 FNLFPHKTVLNNIILApKLLNKS---DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDE 162
Cdd:PRK11288 88 LHLVPEMTVAENLYLG-QLPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 163 PTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-219 |
5.67e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 105.49 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNE-VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMGMVFQNFNLFp 90
Cdd:PRK11176 353 GKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQVALVSQNVHLF- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 HKTVLNNIILAPKllNKSDLNQLKQEA-----LTLLEKV--GLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK11176 430 NDTIANNIAYART--EQYSREQIEEAArmayaMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 164 TSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGS 219
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-223 |
1.26e-25 |
|
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: 104.82 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN-EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMG 80
Cdd:TIGR01193 474 IVINDVSYSYGYGsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPhKTVLNNIILAPK-------LLNKSDLNQLKQEaltlLEKV--GLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:TIGR01193 552 YLPQEPYIFS-GSILENLLLGAKenvsqdeIWAACEIAEIKDD----IENMplGYQTELSEEGSSISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 152 AMHPDIILFDEPTSALDpevVYDVLKVMKDLAK-EGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQI 223
Cdd:TIGR01193 627 LTDSKVLILDESTSNLD---TITEKKIVNNLLNlQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-194 |
2.43e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.73 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIF-EGNELsnhknnlnklrqkmgmvfqnfnLF----- 89
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 --PHKTvLNNIILAPKLLNKSDLNQLKQealtLLEKVGLE------DKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:COG4178 436 ylPLGT-LREALLYPATAEAFSDAELRE----ALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|...
gi 515498091 162 EPTSALDPEVVYDVLKVMKDlAKEGMTMVVVTH 194
Cdd:COG4178 511 EATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
4.95e-25 |
|
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: 97.87 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN--EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKM 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFpHKTVLNNiiLAPklLNKSDLNQLKqEALTLLEKvgledkanvyPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:cd03369 85 TIIPQDPTLF-SGTIRSN--LDP--FDEYSDEEIY-GALRVSEG----------GLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSP 220
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
6.81e-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: 102.21 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLL--ETPTNGRVIFEGNELSNhKNNLNKLRQK 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKA-SNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNNIILAPKLLNKSDL---NQLKQEALTLLEKVGLEDKANVYP-SQLSGGQKQRVAIARALAMH 154
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRmayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-194 |
8.22e-25 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.25 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSN-----------HK 69
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeachylgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 70 NNLNklrqkmgmvfqnfnlfPHKTVLNNIILAPKLLNKSDLnqlkqEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIAR 149
Cdd:PRK13539 82 NAMK----------------PALTVAENLEFWAAFLGGEEL-----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515498091 150 ALAMHPDIILFDEPTSALDPEVVYDVLKVMKD-LAKEGMtMVVVTH 194
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGI-VIAATH 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-233 |
9.01e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 99.98 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLE---TPTNGRVIFEGNELSnhKNNL 72
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKdnwHVTADRFRWNGIDLL--KLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 73 NKLRQKMG----MVFQNFN--LFPHKTV---LNNIILAPKLLNK--SDLNQLKQEALTLLEKVGLED-KA--NVYPSQLS 138
Cdd:COG4170 81 RERRKIIGreiaMIFQEPSscLDPSAKIgdqLIEAIPSWTFKGKwwQRFKWRKKRAIELLHRVGIKDhKDimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 139 GGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAK-EGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250
....*....|....*.
gi 515498091 218 GSPQQIFQSPTHQRTQ 233
Cdd:COG4170 241 GPTEQILKSPHHPYTK 256
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-202 |
1.27e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlNKLRQKMG 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--EIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFpHKTVLNNIILAPKLLNKS-DLNQLKQEaltlLEKVGLED---KANVypSQLSGGQKQRVAIARALAMHPD 156
Cdd:PRK10247 85 YCAQTPTLF-GDTVYDNLIFPWQIRNQQpDPAIFLDD----LERFALPDtilTKNI--AELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 157 IILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTH---EMGFAKDV 202
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHdkdEINHADKV 207
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-212 |
3.31e-24 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 100.19 E-value: 3.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsNHKNNLNKLRQKMGMVF 83
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 84 QNFNLFPHKTVLNNIILA--PKLLNKSDLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-228 |
4.82e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.78 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNL---------NKLRQKMGMVFQNF 86
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkvaylpQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 87 ---NLFPHKTVLNNiilapklLNKSDLNQLkQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK10575 106 vaiGRYPWHGALGR-------FGAADREKV-EEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 164 TSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQSPT 228
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
3-195 |
5.31e-24 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 99.95 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNlletptnGRV---IFEGNELSNHKNNLNKLRQKM 79
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIqgnNFTGTILANNRKPTKQILKRT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNNIILA-----PKLLNKSDLNQLKQEALTLLEKVGLEDK--ANVYPSQLSGGQKQRVAIARALA 152
Cdd:PLN03211 143 GFVTQDDILYPHLTVRETLVFCsllrlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEML 222
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:PLN03211 223 INPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-227 |
8.97e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.02 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 14 NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnLNKLRQKMGMVFQNFNLFPhKT 93
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ--LDSWRSRLAVVSQTPFLFS-DT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIILApkllnKSDLNQLKQEALTLLEKVGlEDKANV---YPSQ-------LSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PRK10789 405 VANNIALG-----RPDATQQEIEHVARLASVH-DDILRLpqgYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 164 TSALDPEVVYDVLKVMKDLaKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-219 |
1.09e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNlnkLRQKMG 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA---KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 --MVFQNFNLFPHKTVLNNIILApklLNKSDLNQLKQEAltLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDII 158
Cdd:PRK15439 88 iyLVPQEPLLFPNLSVKENILFG---LPKRQASMQKMKQ--LLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 159 LFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGS 219
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-225 |
5.93e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 93.37 E-value: 5.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLeTPTNGRVIFEGNELSNHknNLNKLRQKMGM------------VFQ 84
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDW--SAAELARHRAYlsqqqsppfampVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 NFNLFphktvlnniilAPKLLNKSDLNQLKQEaltLLEKVGLEDKANVYPSQLSGGQKQRVAIARA-LAMHPDI------ 157
Cdd:COG4138 89 YLALH-----------QPAGASSEAVEQLLAQ---LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVlLQVWPTInpegql 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDpeVVYDV--LKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:COG4138 155 LLLDEPMNSLD--VAQQAalDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-218 |
3.49e-22 |
|
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: 91.24 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 8 NKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKnnlNKLRQKMGMVF-QNF 86
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR---KKFLRRIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 87 NLFPHKTVLNNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSA 166
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 167 LDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-228 |
3.74e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.04 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFG---KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNlletptngrvifegNELSNHKNNLNKLRQK 78
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML--------------GELSHAETSSVVIRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFpHKTVLNNIILAPKLLN------------KSDLNQLKQEALTLLEKVGLedkanvypsQLSGGQKQRVA 146
Cdd:PLN03232 681 VAYVPQVSWIF-NATVRENILFGSDFESerywraidvtalQHDLDLLPGRDLTEIGERGV---------NISGGQKQRVS 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVL-KVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK 828
|
...
gi 515498091 226 SPT 228
Cdd:PLN03232 829 SGS 831
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-221 |
8.34e-22 |
|
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: 93.32 E-value: 8.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 20 INLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFPHktvlnnii 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NREAYRQLFSAVFSDFHLFDR-------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 100 lapkLLNkSDLNQLKQEALTLLEKVGLEDKANVY-----PSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPE---V 171
Cdd:COG4615 421 ----LLG-LDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrV 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515498091 172 VYDVLkvMKDLAKEGMTMVVVTH-EMGFakDVSDKVIFMADGYVIEEGSPQ 221
Cdd:COG4615 496 FYTEL--LPELKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPA 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-194 |
8.48e-22 |
|
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: 88.95 E-value: 8.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 12 GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKN----NLNKLRQKMGMVfqnfn 87
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDepheNILYLGHLPGLK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 88 lfPHKTVLNNIILAPKLLNKSDLNqlkqeALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSAL 167
Cdd:TIGR01189 86 --PELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*...
gi 515498091 168 DPEVVYDVLKVMKD-LAKEGMTmVVVTH 194
Cdd:TIGR01189 159 DKAGVALLAGLLRAhLARGGIV-LLTTH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-194 |
9.65e-22 |
|
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: 87.98 E-value: 9.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIF-EGNELsnhknnlnklrqkmgmvfqnfnLF-PHKT 93
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDL----------------------LFlPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNniilapkllnksdlnqlkqeALTLLEKVgledkanVYPSQ--LSGGQKQRVAIARALAMHPDIILFDEPTSALDPEV 171
Cdd:cd03223 74 YLP--------------------LGTLREQL-------IYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....*.
gi 515498091 172 ---VYDVLKvmkdlaKEGMTMVVVTH 194
Cdd:cd03223 127 edrLYQLLK------ELGITVISVGH 146
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-239 |
1.25e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 89.99 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 20 INLEIKKGEVLAIIGPSGSGKSTLLRCMNLLeTPTNGRVIFEGNELSNHknNLNKLRQKMG-----------M-VFQNFN 87
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW--SAAELARHRAylsqqqtppfaMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 88 LfpHKTVLNNIILAPKLLNKsdlnqlkqealtLLEKVGLEDKANVYPSQLSGGQKQRVAIARA-LAMHPDI------ILF 160
Cdd:PRK03695 92 L--HQPDKTRTEAVASALNE------------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 161 DEPTSALD--PEVVYDVLkvMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFqspthqrTQNFLSR 238
Cdd:PRK03695 158 DEPMNSLDvaQQAALDRL--LSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL-------TPENLAQ 228
|
.
gi 515498091 239 V 239
Cdd:PRK03695 229 V 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-206 |
2.80e-21 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 88.96 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 25 KKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGR---------VI--FEGNELSNHKNNLNKLRQKMGMVFQNFNLFPhKT 93
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILdeFRGSELQNYFTKLLEGDVKVIVKPQYVDLIP-KA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIILapkLLNKSDLNQLKQEALTLLEKVGLEDKaNVypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVY 173
Cdd:cd03236 103 VKGKVGE---LLKKKDERGKLDELVDQLELRHVLDR-NI--DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|...
gi 515498091 174 DVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKV 206
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
3.15e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.15 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF-------G------------KNEV--LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVI 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepGlkgalkglfrreYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 60 FEGNELSNHKnnlNKLRQKMGMVF-QNFNLFPHktvlnniiLAPK---LLNKS----DLNQLKQEALTLLEKVGLEDKAN 131
Cdd:COG4586 81 VLGYVPFKRR---KEFARRIGVVFgQRSQLWWD--------LPAIdsfRLLKAiyriPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 132 VYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMA 210
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVID 229
|
....*....
gi 515498091 211 DGYVIEEGS 219
Cdd:COG4586 230 HGRIIYDGS 238
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-216 |
3.30e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 91.57 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMGMVFQNFNLFPHktvln 96
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--AEQPEDYRKLFSAVFTDFHLFDQ----- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 97 niILAPKllNKSDLNQLKQ---EALTLLEKVGLEDkANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPE--- 170
Cdd:PRK10522 412 --LLGPE--GKPANPALVEkwlERLKMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrr 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515498091 171 VVYDVLkvMKDLAKEGMTMVVVTHEMGFAkDVSDKVIFMADGYVIE 216
Cdd:PRK10522 487 EFYQVL--LPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-217 |
6.76e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsNHKNNLNKLRQKMG 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILAPKLLNKS---DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVNRFgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-216 |
8.37e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.23 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLLET--PT---NGRVIFEGNELsnhknNLNKLRQ--K 78
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTL---MKVLSGvyPHgsyEGEILFDGEVC-----RFKDIRDseA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVF--QNFNLFPHKTVLNNIILAPKLLNKS--DLNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:NF040905 78 LGIVIihQELALIPYLSIAENIFLGNERAKRGviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIE 216
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-202 |
1.34e-20 |
|
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: 89.99 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKF-GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsnhknnlnklrQKMGMVFQ 84
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG-------------IKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 NFNLFPHKTVLNNIILA----PKLLNK------------SDLNQLKQEALTLLEKV------GLEDK------------- 129
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGvaeiKDALDRfneisakyaepdADFDKLAAEQAELQEIIdaadawDLDSQleiamdalrcppw 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 130 -ANVypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKegmTMVVVTHEMGFAKDV 202
Cdd:TIGR03719 156 dADV--TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-217 |
1.58e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 9 KKFGKnevLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhKNNLNKLRQKMGMVFQN--- 85
Cdd:PRK09700 274 RDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP-RSPLDAVKKGMAYITESrrd 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 86 FNLFPHKTVLNNIILAPK-----------LLNKSDLNQLKQEALTLLEKVGLEDKANVypSQLSGGQKQRVAIARALAMH 154
Cdd:PRK09700 350 NGFFPNFSIAQNMAISRSlkdggykgamgLFHEVDEQRTAENQRELLALKCHSVNQNI--TELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-215 |
2.09e-20 |
|
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: 85.39 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 9 KKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM-NLLETP--TNGRVIFEGNELsnhKNNLNKLRQKMGMVFQN 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNvsVEGDIHYNGIPY---KEFAEKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 86 FNLFPHKTVLNNIILAPKLlnksdlnqlkqealtllekvgledKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:cd03233 92 DVHFPTLTVRETLDFALRC------------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515498091 166 ALDPEVVYDVLKVMKDLAKE-GMT-MVVVTHEMGFAKDVSDKVIFMADGYVI 215
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVlKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-219 |
2.64e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.41 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMnLLETPT--NGRVIfegnelsnhknnlnkLRQKMGMVFQNFNLFpHKTV 94
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAM-LGELPPrsDASVV---------------IRGTVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LNNIILA----PKLLNKS-DLNQLKQEALTL----LEKVGlEDKANVypsqlSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:PLN03130 696 RDNILFGspfdPERYERAiDVTALQHDLDLLpggdLTEIG-ERGVNI-----SGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 166 ALDPEVVYDVL-KVMKDLAKeGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGS 219
Cdd:PLN03130 770 ALDAHVGRQVFdKCIKDELR-GKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGT 822
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
4.26e-20 |
|
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: 85.54 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 23 EIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnHKNNLNKLRQKMgmvfqnfnlfphkTVlnNIILAP 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEG-------------TV--RDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 103 KLLNKSDLNQLKQEALTLLEKVGLEDKaNVypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDL 182
Cdd:cd03237 85 ITKDFYTHPYFKTEIAKPLQIEQILDR-EV--PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180
....*....|....*....|....*.
gi 515498091 183 A-KEGMTMVVVTHEMGFAKDVSDKVI 207
Cdd:cd03237 162 AeNNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-196 |
4.74e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 88.93 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKN-----EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFegNELSNHKN-NLNKLR 76
Cdd:PTZ00265 382 KIQFKNVRFHYDtrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDiNLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 QKMGMVFQNFNLFPHkTVLNNIILA---------------------------------------PKLLNKSDLNQLKQ-- 115
Cdd:PTZ00265 460 SKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlNDMSNTTDSNELIEmr 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 116 ---------EALTLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDV 175
Cdd:PTZ00265 539 knyqtikdsEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|..
gi 515498091 176 LKVMKDL-AKEGMTMVVVTHEM 196
Cdd:PTZ00265 619 QKTINNLkGNENRITIIIAHRL 640
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-196 |
2.42e-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: 86.38 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEV-------LKDINLEI-KKGEVLAIIGPSGSGKSTLLRCM---------NLLETPTNGRVI--FEG 62
Cdd:COG1245 66 ISIVNLPEELEEDPVhrygengFRLYGLPVpKKGKVTGILGPNGIGKSTALKILsgelkpnlgDYDEEPSWDEVLkrFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 63 NELSNHknnLNKLRQKmgmvfqnfNLfphKTVL--NNIILAPK--------LLNKSDlnqLKQEALTLLEKVGLEDKANV 132
Cdd:COG1245 146 TELQDY---FKKLANG--------EI---KVAHkpQYVDLIPKvfkgtvreLLEKVD---ERGKLDELAEKLGLENILDR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 133 YPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDpevVYD---VLKVMKDLAKEGMTMVVVTHEM 196
Cdd:COG1245 209 DISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-226 |
3.53e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.93 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNE-VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNNLnkLRQKMG 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPhKTVLNNIILApkllnksdlNQLKQEAL-TLLEKVGLEDKANVYP-----------SQLSGGQKQRVAIA 148
Cdd:PRK10790 419 MVQQDPVVLA-DTFLANVTLG---------RDISEEQVwQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVYDVLKVMKdLAKEGMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-227 |
4.69e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGnelsnhknnlnKLRqkMG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHK--TVLNNIILAPKLLNKSDLNQLKQ-EALTLLEkvgledkanvYPSQ-LSGGQKQRVAIARALAMHPD 156
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRPGTKKEDILPALKRvQAGHLID----------APMQkLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 157 IILFDEPTSALDPE---VVYDVLKVMKDLAKEGMTMvvVTHEMGFAKDVSDKVIFMaDGYVIEEGSPQQIFQSP 227
Cdd:PRK09544 141 LLVLDEPTQGVDVNgqvALYDLIDQLRRELDCAVLM--VSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHP 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-233 |
4.82e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 84.08 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF----GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLeTPTNGRVI---FEGNELSNHKNNLN 73
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 KLRQKMG----MVFQNFN--LFPHKTVLNNIILA-PKLLNKSD----LNQLKQEALTLLEKVGLEDKANV---YPSQLSG 139
Cdd:PRK15093 82 ERRKLVGhnvsMIFQEPQscLDPSERVGRQLMQNiPGWTYKGRwwqrFGWRKRRAIELLHRVGIKDHKDAmrsFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 140 GQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAK-EGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEG 218
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250
....*....|....*
gi 515498091 219 SPQQIFQSPTHQRTQ 233
Cdd:PRK15093 242 PSKELVTTPHHPYTQ 256
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-195 |
5.45e-19 |
|
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: 81.52 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 5 ENLN----KKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLrcmNLLETPTNGRVIfEGNELSNHKNNLNKLRQKMG 80
Cdd:cd03232 7 KNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLL---DVLAGRKTAGVI-TGEILINGRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVlnniilapkllnksdlnqlkQEALTLlekvgledKANVypSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:cd03232 83 YVEQQDVHSPNLTV--------------------REALRF--------SALL--RGLSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190
....*....|....*....|....*....|....*
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQ 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-223 |
9.02e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLN-KKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHK-NNLNKL----- 75
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 ---RQKMGMVfqnfnlfPHKTVLNNIIL----APKLLNKS--DLNQLKQEALTLLEK-----VGLEDKAnvypSQLSGGQ 141
Cdd:COG3845 339 pedRLGRGLV-------PDMSVAENLILgryrRPPFSRGGflDRKAIRAFAEELIEEfdvrtPGPDTPA----RSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQ 221
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
..
gi 515498091 222 QI 223
Cdd:COG3845 488 EA 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-225 |
1.61e-18 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 84.23 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsnhknnlnklrqkmgmvfqnFNLFPHKTVLN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------------------VAYVPQQAWIQ 711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 97 NIILAPKLLNKSDLNQLKQEALtlLEKVGLEDKANVYPS-----------QLSGGQKQRVAIARALAMHPDIILFDEPTS 165
Cdd:TIGR00957 712 NDSLRENILFGKALNEKYYQQV--LEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 166 ALDPEVVYDVLKvmKDLAKEGM----TMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:TIGR00957 790 AVDAHVGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-212 |
2.63e-18 |
|
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: 83.34 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 19 DINLEIKKGEVLAIIGPSGSGKSTLLRCM-NLLETPTNGRVIFEGNELsNHKNNLNKLRQKMGMVFQN---FNLFPHKTV 94
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDrkrHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LNNIILA--PKLLNKSDLNQLKQEALTLLEKVGLEDKA---NVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDP 169
Cdd:TIGR02633 357 GKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 515498091 170 EVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-196 |
4.06e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEV-------LKDINLEI-KKGEVLAIIGPSGSGKSTLLRCM---------NLLETPTNGRVI--FEG 62
Cdd:PRK13409 66 ISIVNLPEELEEEPVhrygvngFKLYGLPIpKEGKVTGILGPNGIGKTTAVKILsgelipnlgDYEEEPSWDEVLkrFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 63 NELSNHknnLNKLRQKmgmvfqnfNLfphKTVLNN--IILAPK--------LLNKSDLNQLKQEaltLLEKVGLEDKANV 132
Cdd:PRK13409 146 TELQNY---FKKLYNG--------EI---KVVHKPqyVDLIPKvfkgkvreLLKKVDERGKLDE---VVERLGLENILDR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 133 YPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDpevVYD---VLKVMKDLAkEGMTMVVVTHEM 196
Cdd:PRK13409 209 DISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-212 |
2.08e-17 |
|
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: 77.76 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMnLLETPT-NGRVIFEGNELSNHKNNLNKLRQKMGMVFQNfnlfpHKTVL 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-LGEMQTlEGKVHWSNKNESEPSFEATRSRNRYSVAYAA-----QKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 96 NNIILAPKLLNKSDLNQLKQEALTllEKVGLEDKANVYPS-----------QLSGGQKQRVAIARALAMHPDIILFDEPT 164
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVT--DACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515498091 165 SALDPEVVYDVLK--VMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADG 212
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-231 |
2.92e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.39 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNlletptnGRVIFEGNELSNHKNNLNK-LRQKM-GMVFQNFNL---FPh 91
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGKISILGQPTRQaLQKNLvAYVPQSEEVdwsFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 kTVLNNIILAPKLLNKSDLNQLK----QEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSAL 167
Cdd:PRK15056 95 -VLVEDVVMMGRYGHMGWLRRAKkrdrQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 168 DPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIfMADGYVIEEGSPQQIFQSPTHQR 231
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLEL 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-194 |
3.45e-17 |
|
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: 76.76 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 5 ENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhknnlnklrQKMGMVFQ 84
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----------FQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 85 NFNLFPH----KTVLNNIilaPKLLNKSDLNQLKQeALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:cd03231 74 GLLYLGHapgiKTTLSVL---ENLRFWHADHSDEQ-VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 515498091 161 DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTH 194
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-223 |
3.97e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhkNNLNkLRQKMGM 81
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA--GDIA-TRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNNIILAPKL--LNKSDLNQLKQEaltLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARLfhLPAAEIAARVAE---MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 160 FDEPTSALDPeVVYDVL-KVMKDLAKE-GMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQI 223
Cdd:NF033858 421 LDEPTSGVDP-VARDMFwRLLIELSREdGVTIFISTHFMNEAERC-DRISLMHAGRVLASDTPAAL 484
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-219 |
4.15e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.76 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCmnLLETPtnGRVIFEGNELSNHKNNLNK---LRQ 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHP--AYKILEGDILFKGESILDLepeERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 KMG--MVFQNFNLFPHKTVLNNIILA----PKLLNKSDLNQLkqEALTL----LEKVGLEDK---ANVYPSqLSGGQKQR 144
Cdd:CHL00131 83 HLGifLAFQYPIEIPGVSNADFLRLAynskRKFQGLPELDPL--EFLEIinekLKLVGMDPSflsRNVNEG-FSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 145 VAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVS-DKVIFMADGYVIEEGS 219
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGD 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
5.20e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGknevlkDINL-----EIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEgnelsnhknnlNKL 75
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQNFNLfphkTV---LNNIilAPKLlnksDLNQLKQEaltLLEKVGLEDKANVYPSQLSGGQKQRVAIARALA 152
Cdd:PRK13409 403 SYKPQYIKPDYDG----TVedlLRSI--TDDL----GSSYYKSE---IIKPLQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 153 MHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVI 207
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
5.56e-17 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 77.14 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLE--TPTNGRVIFEGNELSNHKNNlNKLRQK 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE-DRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQN-------FNLFPHKTVLNNI--ILAPKLLNKSDLNQLKQEALTLLEKVG--LEDKANVypsQLSGGQKQRVAI 147
Cdd:PRK09580 80 IFMAFQYpveipgvSNQFFLQTALNAVrsYRGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNV---GFSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515498091 148 ARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTH 194
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-194 |
7.95e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.01 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 6 NLNKKFG-KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIF------------------------ 60
Cdd:PRK11819 11 RVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPapgikvgylpqepqldpektvren 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 61 --EG-NELSNHKNNLNKLRQKMGMVFQNFN-LFPHKTVLNNIILApklLNKSDL-NQLKQ--EALTLLEkvgleDKANVy 133
Cdd:PRK11819 91 veEGvAEVKAALDRFNEIYAAYAEPDADFDaLAAEQGELQEIIDA---ADAWDLdSQLEIamDALRCPP-----WDAKV- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515498091 134 pSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEvvyDVLKVMKDLAKEGMTMVVVTH 194
Cdd:PRK11819 162 -TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTH 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-232 |
1.77e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM-NLLETPTNGRVIFEGNELSNhKNNLNKLRQKMGMVFQN---FNLFP 90
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKI-RNPQQAIAQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 HKTVLNNIILA-------PKLLNKSD--------LNQLKQEALTLLEKVGledkanvypsQLSGGQKQRVAIARALAMHP 155
Cdd:PRK13549 355 VMGVGKNITLAaldrftgGSRIDDAAelktilesIQRLKVKTASPELAIA----------RLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADG-----YVIEEGSPQQIFQSPTHQ 230
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGklkgdLINHNLTQEQVMEAALRS 504
|
..
gi 515498091 231 RT 232
Cdd:PRK13549 505 EH 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-195 |
1.90e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 78.23 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 10 KFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCmnLLETPTNGrVIFEGNELSNHKNNLNKLRQKMGMVFQNFNLF 89
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTG-VITGGDRLVNGRPLDSSFQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 PHKTVLNNIILA-----PKLLNKSDLNQLKQEALTLLEkvgLEDKAN----VYPSQLSGGQKQRVAIARALAMHPDIILF 160
Cdd:TIGR00956 849 PTSTVRESLRFSaylrqPKSVSKSEKMEYVEEVIKLLE---MESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLF 925
|
170 180 190
....*....|....*....|....*....|....*.
gi 515498091 161 -DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:TIGR00956 926 lDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-226 |
2.96e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 77.68 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMGMVFQNFNLFPHKTVL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA--KIGLHDLRFKITIIPQDPVLFSGSLRM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 96 NniiLAPkLLNKSDlnqlkQEALTLLEKVGLEDKANVYPSQ-----------LSGGQKQRVAIARALAMHPDIILFDEPT 164
Cdd:TIGR00957 1379 N---LDP-FSQYSD-----EEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 165 SALDPEvVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSdKVIFMADGYVIEEGSPQQIFQS 226
Cdd:TIGR00957 1450 AAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-229 |
5.54e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.86 E-value: 5.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCM--NLLETPT------NGRVIFEGNELSN-HKNN 71
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAprgarvTGDVTLNGEPLAAiDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 LNKLRQKMGMVFQNfnLFPHKTvlNNIILA---PKLLNKSDLNQLKQE-ALTLLEKVGLEDKANVYPSQLSGGQKQRVAI 147
Cdd:PRK13547 81 LARLRAVLPQAAQP--AFAFSA--REIVLLgryPHARRAGALTHRDGEiAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 148 ARALA-MHPD--------IILFDEPTSALDPEVVYDVLKVMKDLAKE-GMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:PRK13547 157 ARVLAqLWPPhdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|..
gi 515498091 218 GSPQQIFQsPTH 229
Cdd:PRK13547 237 GAPADVLT-PAH 247
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-227 |
9.42e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLETpTNGRVIFEgnelsnhknnlnklrQKMGMVFQNFNLFpHKT 93
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSlLSQFEI-SEGRVWAE---------------RSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIIL-----APKLLNKSDLNQLkqEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:PTZ00243 737 VRGNILFfdeedAARLADAVRVSQL--EADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 169 PEVVYdvlKVMKDL---AKEGMTMVVVTHEMGFAKdVSDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PTZ00243 815 AHVGE---RVVEECflgALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-212 |
1.52e-15 |
|
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: 71.97 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLrcmnlletptngrviFEGNELSNhKNNLNKLRQKmgmvfqnfnlFPHktvlN 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEGLYASG-KARLISFLPK----------FSR----N 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 97 NIILAPKLLNKSDLNqlkqealtlLEKVGLEDKAnvypSQLSGGQKQRVAIARALA--MHPDIILFDEPTSALDPEVVYD 174
Cdd:cd03238 61 KLIFIDQLQFLIDVG---------LGYLTLGQKL----STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 515498091 175 VLKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMADG 212
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-223 |
1.95e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNnlnKLRQKMGMVF-----QNFNLF 89
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 90 phktvlnniILAPKLLNKSDL--NQL------KQEALTLlEKV--GLEDKANvYPSQ----LSGGQKQRVAIARALAMHP 155
Cdd:PRK15439 354 ---------LDAPLAWNVCALthNRRgfwikpARENAVL-ERYrrALNIKFN-HAEQaartLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-199 |
2.39e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 19 DINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELsnhknnlNKLRQKMgmvFQNFNLFPH----KTV 94
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEY---HQDLLYLGHqpgiKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LN---NIILAPKLLNKSDLNQLKQealtLLEKVGLEDKANVYPSQLSGGQKQRVAIAR-ALAMHPDIILfDEPTSALDPE 170
Cdd:PRK13538 89 LTaleNLRFYQRLHGPGDDEALWE----ALAQVGLAGFEDVPVRQLSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQ 163
|
170 180 190
....*....|....*....|....*....|.
gi 515498091 171 VVYDVLKVMKDLAKEGmTMVVVT--HEMGFA 199
Cdd:PRK13538 164 GVARLEALLAQHAEQG-GMVILTthQDLPVA 193
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-224 |
3.03e-15 |
|
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: 72.63 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKN--EVLKDINLEIKKGEVLAIIGPSGSGKSTL----LRCMNLLEtptnGRVIFEGNELSnhKNNLNKL 75
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDIS--KLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 76 RQKMGMVFQN---------FNLFPHKTVLNNiilapKLLNKSDLNQLKQEALTL---LEKVGLEDKANvypsqLSGGQKQ 143
Cdd:cd03288 94 RSRLSIILQDpilfsgsirFNLDPECKCTDD-----RLWEALEIAQLKNMVKSLpggLDAVVTEGGEN-----FSVGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 144 RVAIARALAMHPDIILFDEPTSALDpEVVYDVLK--VMKDLAKEgmTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQ 221
Cdd:cd03288 164 LFCLARAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPE 239
|
...
gi 515498091 222 QIF 224
Cdd:cd03288 240 NLL 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-207 |
9.37e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVL---------------KDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELS 66
Cdd:PTZ00265 1154 IRIKNKNDIKGKIEIMdvnfryisrpnvpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHT 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 67 NHKNNLNKLR----QKMGM-------------------VFQN-------------FNLFPHKTVLNNIILAPKLLNKSDL 110
Cdd:PTZ00265 1234 NDMTNEQDYQgdeeQNVGMknvnefsltkeggsgedstVFKNsgkilldgvdicdYNLKDLRNLFSIVSQEPMLFNMSIY 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 111 NQLK--QEALTL---------------LEKVGLEDKANV--YPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEV 171
Cdd:PTZ00265 1314 ENIKfgKEDATRedvkrackfaaidefIESLPNKYDTNVgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270
....*....|....*....|....*....|....*..
gi 515498091 172 VYDVLKVMKDLA-KEGMTMVVVTHEMGFAKDvSDKVI 207
Cdd:PTZ00265 1394 EKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIV 1429
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-207 |
2.39e-14 |
|
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: 71.74 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 23 EIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGrVIFEGNELSnHKNNlnKLRQKMGMVFQNFNLFPHKTVLNNIILAP 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-EVDEDLKIS-YKPQ--YISPDYDGTVEEFLRSANTDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 103 KLLNKSDLNQLkqealtlLEKvgledkaNVypSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDL 182
Cdd:COG1245 438 EIIKPLGLEKL-------LDK-------NV--KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180
....*....|....*....|....*.
gi 515498091 183 AKE-GMTMVVVTHEMGFAKDVSDKVI 207
Cdd:COG1245 502 AENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-170 |
3.16e-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: 71.50 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFeGNELsnhknnlnklrqKMGM 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNF-NLFPHKTVL------NNIIlapkLLNKSDLN--------------QLKqealtlleKVGledkanvypsQLSGG 140
Cdd:TIGR03719 390 VDQSRdALDPNKTVWeeisggLDII----KLGKREIPsrayvgrfnfkgsdQQK--------KVG----------QLSGG 447
|
170 180 190
....*....|....*....|....*....|
gi 515498091 141 QKQRVAIARALAMHPDIILFDEPTSALDPE 170
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-212 |
8.83e-14 |
|
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: 69.12 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 14 NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLR-CMNLLEtPTNGRVIFEGN-ELSNHKNNLNKLRQKMGMVFQ-NFNLFP 90
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMlILGELE-PSEGKIKHSGRiSFSSQFSWIMPGTIKENIIFGvSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 91 HKTVLNNIILapkllnKSDLNQLKQEALTLLEKVGLedkanvypsQLSGGQKQRVAIARALAMHPDIILFDEPTSALD-- 168
Cdd:cd03291 129 YKSVVKACQL------EEDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvf 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515498091 169 -PEVVYD--VLKVMKDlakegMTMVVVTHEMGFAKdVSDKVIFMADG 212
Cdd:cd03291 194 tEKEIFEscVCKLMAN-----KTRILVTSKMEHLK-KADKILILHEG 234
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-223 |
1.04e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.38 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLeTPTNGRVIFEgneLSNHKNNLNKLRQKMGM 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*-GPDAGRRPWR---F*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 vfqnfnlfpHKTVL----------NNIILAPKLLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARAL 151
Cdd:NF000106 90 ---------HRPVR*grresfsgrENLYMIGR*LDLSR-KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 152 AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-239 |
2.06e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCmnlLETPTNGRVIFEGNELSNHKNNLNKL-RQKMGMVF---QNFNLFPH 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKT---IASNTDGFHIGVEGVITYDGITPEEIkKHYRGDVVynaETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNIILAPKL-------LNKSDLNQLKQEALTLLEKVGLEDKANV-----YPSQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:TIGR00956 153 LTVGETLDFAARCktpqnrpDGVSREEYAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVT--HEMGFAKDVSDKVIFMADGYVIEEGSPQQI--------FQSPTH 229
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDR 312
|
250
....*....|
gi 515498091 230 QRTQNFLSRV 239
Cdd:TIGR00956 313 QTTADFLTSL 322
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-212 |
2.44e-13 |
|
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: 69.17 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLR-CMNLLEtPTNGRVIFEGN-ELSNHKNNLNKLRQKMGMVFQ-NFNLFPHK 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELE-PSEGKIKHSGRiSFSPQTSWIMPGTIKDNIIFGlSYDEYRYT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNIILapkllnKSDLNQLKQEALTLLEKVGLedkanvypsQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV 172
Cdd:TIGR01271 520 SVIKACQL------EEDIALFPEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515498091 173 YDVLK--VMKDLAKEgmTMVVVTHEMGFAKDvSDKVIFMADG 212
Cdd:TIGR01271 585 KEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
3.31e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsNHKNNLNKLRQKMG 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ---SIKKDLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFNLFPHKTVLNNIILApklLNKSDLNQLKQEALTLLEKVGLEDkanvYP-SQLSGGQKQRVAIARALAMHPDIIL 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYD---IHFSPGAVGITELCRLFSLEHLID----YPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 515498091 160 FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
3.83e-13 |
|
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: 67.19 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKF--GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMnLLETPTNGRVIFEGneLSNHKNNLNKLRQKM 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF-LRLLNTEGDIQIDG--VSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 GMVFQNFNLFPHKTVLNniiLAPKLLNKSdlnqlkQEALTLLEKVGLEDKANVYPSQL-----------SGGQKQRVAIA 148
Cdd:cd03289 80 GVIPQKVFIFSGTFRKN---LDPYGKWSD------EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515498091 149 RALAMHPDIILFDEPTSALDPeVVYDVLKVMKDLAKEGMTMVVVTHEM 196
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-228 |
8.92e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 8.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKF--GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQK 78
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA--KFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 MGMVFQNFNLFPHKTVLNniiLAP-KLLNKSDLnqlkQEALtllEKVGLEDKANVYPSQL-----------SGGQKQRVA 146
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFN---IDPfSEHNDADL----WEAL---ERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLS 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEgMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQS 226
Cdd:PLN03232 1382 LARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS-CTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
..
gi 515498091 227 PT 228
Cdd:PLN03232 1460 DT 1461
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-194 |
9.00e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.26 E-value: 9.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 11 FGKNE--VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVifegnELSNHKNNLNKLRQKMGMVFQNFNL 88
Cdd:PRK13543 19 FSRNEepVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-----QIDGKTATRGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 89 FPHKTVLNNIILAPKLLNKSDlNQLKQEALTLlekVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGRRA-KQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180
....*....|....*....|....*.
gi 515498091 169 PEVVYDVLKVMKDLAKEGMTMVVVTH 194
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-214 |
1.09e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKfgKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHKNN--------- 71
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeainhgfal 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 LNKLRQKMGmVFQNFNLFPHKTVLN--NIILAPKLLNKSDLNQLKQEALtllekvgleDKANV-YPSQ------LSGGQK 142
Cdd:PRK10982 328 VTEERRSTG-IYAYLDIGFNSLISNirNYKNKVGLLDNSRMKSDTQWVI---------DSMRVkTPGHrtqigsLSGGNQ 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 143 QRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-177 |
1.21e-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: 66.86 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKF--GKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETpTNGRVIFEGneLSNHKNNLNKLRQKMGM 81
Cdd:TIGR01271 1220 VQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNFNLFPHKTVLNniiLAPKLlNKSDlnqlkQEALTLLEKVGLEDKANVYPSQL-----------SGGQKQRVAIARA 150
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKN---LDPYE-QWSD-----EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARS 1367
|
170 180
....*....|....*....|....*..
gi 515498091 151 LAMHPDIILFDEPTSALDPeVVYDVLK 177
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDP-VTLQIIR 1393
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-207 |
1.28e-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: 64.13 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINlEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNelsnhknnlnklrqkmgm 81
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 vfqnfnlfphktvlnNIILAPKLLNksdlnqlkqealtllekvgledkanvypsqLSGGQKQRVAIARALAMHPDIILFD 161
Cdd:cd03222 62 ---------------TPVYKPQYID------------------------------LSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 515498091 162 EPTSALDPEVVYDVLKVMKDLAKEGM-TMVVVTHEMGFAKDVSDKVI 207
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-225 |
1.39e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhKNNLNKLRQKMGMVFQNFNLFPHKTVL 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDLRKVLGIIPQAPVLFSGTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 96 NniiLAP-KLLNKSDLnqlkQEALtllEKVGLED---------KANVYPS--QLSGGQKQRVAIARALAMHPDIILFDEP 163
Cdd:PLN03130 1332 N---LDPfNEHNDADL----WESL---ERAHLKDvirrnslglDAEVSEAgeNFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 164 TSALDpeVVYDVLkVMKDLAKE--GMTMVVVTHEMGFAKDvSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PLN03130 1402 TAAVD--VRTDAL-IQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-227 |
1.54e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLETpTNGRVIFEGNELSNHknNLNKLRQKMGMVFQNFNLFpHKTV 94
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfMRMVEV-CGGEIRVNGREIGAY--GLRELRRQFSMIPQDPVLF-DGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 95 LNNiiLAPKLLNKSdlnqlkQEALTLLEKVGLEDK---------ANVYP--SQLSGGQKQRVAIARALAMH-PDIILFDE 162
Cdd:PTZ00243 1401 RQN--VDPFLEASS------AEVWAALELVGLRERvasesegidSRVLEggSNYSVGQRQLMCMARALLKKgSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515498091 163 PTSALDPEVVYDV-LKVMKdlAKEGMTMVVVTHEMGFAKDVsDKVIFMADGYVIEEGSPQQIFQSP 227
Cdd:PTZ00243 1473 ATANIDPALDRQIqATVMS--AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-195 |
2.75e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 15 EVLKDINLEIKKGEVLAIIGPSGSGKSTLlrcMNLLETPTNGRVIfEGN-ELSNHKNNLNKLRQKMGMVFQNFNLFPHKT 93
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTL---MDVLAGRKTGGYI-EGDiRISGFPKKQETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 94 VLNNIILA-----PKLLNKSDLNQLKQEALTLLEKVGLEDKANVYP--SQLSGGQKQRVAIARALAMHPDIILFDEPTSA 166
Cdd:PLN03140 970 VRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*....
gi 515498091 167 LDPEVVYDVLKVMKDLAKEGMTMVVVTHE 195
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-225 |
1.07e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNHK-----NN----LNKLRQKMGMVF---- 83
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglANgivyISEDRKRDGLVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 84 -QNFNLfphkTVLNNIILAPKLLNKSDLNQLKQEALTLLekvgledkaNV-YPSQ------LSGGQKQRVAIARALAMHP 155
Cdd:PRK10762 348 kENMSL----TALRYFSRAGGSLKHADEQQAVSDFIRLF---------NIkTPSMeqaiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 156 DIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQ 484
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-225 |
1.64e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 20 INLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSnhknnLNKLRQ--KMGMVF-----QNFNLFPHK 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-----IRSPRDaiRAGIMLcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 93 TVLNNI--------ILAPKLLNKsdlnqlKQEALTLLEKVGledKANV-YPS------QLSGGQKQRVAIARALAMHPDI 157
Cdd:PRK11288 347 SVADNInisarrhhLRAGCLINN------RWEAENADRFIR---SLNIkTPSreqlimNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515498091 158 ILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE----MGfakdVSDKVIFMADGYVI-----EEGSPQQIFQ 225
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAgelarEQATERQALS 490
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
1.92e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFeGNELsnhknnlnklrqKMGM 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------------KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 VFQNF-NLFPHKTVLNNI-----ILapkLLNKSDLN--------------QLKqealtlleKVGledkanvypsQLSGGQ 141
Cdd:PRK11819 392 VDQSRdALDPNKTVWEEIsggldII---KVGNREIPsrayvgrfnfkggdQQK--------KVG----------VLSGGE 450
|
170 180
....*....|....*....|....*....
gi 515498091 142 KQRVAIARALAMHPDIILFDEPTSALDPE 170
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-212 |
2.81e-11 |
|
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: 63.11 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 24 IKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNELSNhknNLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPK 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---NISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 104 LLNKSDlNQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLA 183
Cdd:TIGR01257 2039 LRGVPA-EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 515498091 184 KEGMTMVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-194 |
4.56e-11 |
|
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: 62.07 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVL-KDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIfegnelSNHKNNLNKLRQKm 79
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT------KPAKGKLFYVPQR- 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 80 gmvfqnfnlfPHKTV--LNNIILAP--------KLLNKSDLNQLKQEA-LT-LLEKVGLEDKANVYPSQLSGGQKQRVAI 147
Cdd:TIGR00954 524 ----------PYMTLgtLRDQIIYPdssedmkrRGLSDKDLEQILDNVqLThILEREGGWSAVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 515498091 148 ARALAMHPDIILFDEPTSALDPevvyDVLKVMKDLAKE-GMTMVVVTH 194
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSV----DVEGYMYRLCREfGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
5.44e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRC-MNLLEtPTNGRVIFEGNelsnhkNNLNKLRQKMGMV 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTVKWSEN------ANIGYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQN-FNLFP----HKTVLNNI-----ILAPKLLNKSDLNQlkqealtllekvgledKANVypsqLSGGQKQRVAIARALA 152
Cdd:PRK15064 395 FENdLTLFDwmsqWRQEGDDEqavrgTLGRLLFSQDDIKK----------------SVKV----LSGGEKGRMLFGKLMM 454
|
170
....*....|....*...
gi 515498091 153 MHPDIILFDEPTSALDPE 170
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDME 472
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-225 |
5.45e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.57 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 21 NLEIKKGEVLAIIGPSGSGKSTLLRCMNlletptnGRVIFEGNELSNHKN-----NLNKLRQKMGMVFQNFN---LFPH- 91
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA-------GELPLLSGERQSQFShitrlSFEQLQKLVSDEWQRNNtdmLSPGe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 ----KTVlnniilAPKLLNKSDLNQLKQEaltLLEKVGLEDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSAL 167
Cdd:PRK10938 96 ddtgRTT------AEIIQDEVKDPARCEQ---LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 168 DPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQIFQ 225
Cdd:PRK10938 167 DVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-209 |
8.29e-11 |
|
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: 58.54 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 26 KGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIfegnelsnhknnlnklrqkmgmvfqnfnlfphktvlnniILAPKLL 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 106 NKSDLNQLKQEALtllekvgledkaNVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPE------VVYDVLKVM 179
Cdd:smart00382 42 LEEVLDQLLLIIV------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqealllLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 515498091 180 KDLAKEGMTMVVVTHEMGF-----AKDVSDKVIFM 209
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVL 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-168 |
2.66e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMN---LLEtptNGRVIFEGN-------------- 63
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQDlivarlqqdpprnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 64 -------------ELSNHKNNLNKLRQKMGMVfqnfnlfPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEdkA 130
Cdd:PRK11147 80 egtvydfvaegieEQAEYLKRYHDISHLVETD-------PSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLD--P 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 515498091 131 NVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALD 168
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-220 |
3.31e-10 |
|
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: 58.39 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLL----------RCMNLLETPTNGRVIfEGNElsnhknNLNKLRQ--------- 77
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRI-EGLE------HIDKVIVidqspigrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 78 -------------KMGMVF------QNFN------LFPHKT---VLN-----------NIilaPKLLNKsdlnqlkqeaL 118
Cdd:cd03271 84 prsnpatytgvfdEIRELFcevckgKRYNretlevRYKGKSiadVLDmtveealeffeNI---PKIARK----------L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 119 TLLEKVGLEdkanvY-----PS-QLSGGQKQRVAIARALAM---HPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTM 189
Cdd:cd03271 151 QTLCDVGLG-----YiklgqPAtTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTV 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 515498091 190 VVVTHEMGFAKdVSDKVIFM------ADGYVIEEGSP 220
Cdd:cd03271 226 VVIEHNLDVIK-CADWIIDLgpeggdGGGQVVASGTP 261
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-217 |
3.62e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 4 IENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRViFEGNELS-----NHKNNLNklrqk 78
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKLEvayfdQHRAELD----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 79 mgmvfqnfnlfPHKTVLNNiiLAPkllNKSD--LNQLKQEALTLLEKVGLEDKANVYPSQ-LSGGQKQRVAIARALAMHP 155
Cdd:PRK11147 396 -----------PEKTVMDN--LAE---GKQEvmVNGRPRHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 156 DIILFDEPTSALDPEvvydVLKVMKDL--AKEGmTMVVVTHEMGFAKD-VSDKVIFMADGyVIEE 217
Cdd:PRK11147 460 NLLILDEPTNDLDVE----TLELLEELldSYQG-TVLLVSHDRQFVDNtVTECWIFEGNG-KIGR 518
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-223 |
4.25e-10 |
|
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: 59.26 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 137 LSGGQKQRVAIARAL---AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKdVSDKVIFM---- 209
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeg 908
|
90
....*....|....*.
gi 515498091 210 --ADGYVIEEGSPQQI 223
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-212 |
4.96e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRcmnlletptngrvIFEGNELSNHKNNLN-------- 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS-------------LITGDHPQGYSNDLTlfgrrrgs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 -----KLRQKMGMVFQNFNL-FPHKTVLNNIILAPKLLN------KSD-LNQLKQEALTLLekvGLEDKANVYPSQ-LSG 139
Cdd:PRK10938 328 getiwDIKKHIGYVSSSLHLdYRVSTSVRNVILSGFFDSigiyqaVSDrQQKLAQQWLDIL---GIDKRTADAPFHsLSW 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 140 GQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMT-MVVVTHEmgfAKD----VSDKVIFMADG 212
Cdd:PRK10938 405 GQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHH---AEDapacITHRLEFVPDG 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-219 |
7.55e-10 |
|
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: 56.21 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 26 KGEVLAIIGPSGSGKSTLLRCMNLLETptngrvifegnelsnhknnlnklrqkmgmvFQNFNLFPHKTVLNNIILApkll 105
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIGLALG------------------------------GAQSATRRRSGVKAGCIVA---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 106 nksdlnqlkQEALTLLEKVgledkanvypSQLSGGQKQRVAIARALAMHP----DIILFDEPTSALDPEVVYDVLKVMKD 181
Cdd:cd03227 66 ---------AVSAELIFTR----------LQLSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILE 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 515498091 182 LAKEGMTMVVVTHEMGFAKDvSDKVIFMadGYVIEEGS 219
Cdd:cd03227 127 HLVKGAQVIVITHLPELAEL-ADKLIHI--KKVITGVY 161
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-223 |
8.00e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLL------RCMNlletptNGRVIFEGNELSN--HKNNLN 73
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQ------QGRVEVLGGDMADarHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 74 KlR-----QKMGMvfqnfNLFPHKTVLNNIILAPKL--LNKSdlnQLKQEALTLLEKVGLEDKANVYPSQLSGGQKQRVA 146
Cdd:NF033858 76 P-RiaympQGLGK-----NLYPTLSVFENLDFFGRLfgQDAA---ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 147 IARALAMHPDIILFDEPTSALDP-------EVVYDVLKvmkdlAKEGMTMVVVTHEM----GFakdvsDKVIFMADGYVI 215
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYMeeaeRF-----DWLVAMDAGRVL 216
|
....*...
gi 515498091 216 EEGSPQQI 223
Cdd:NF033858 217 ATGTPAEL 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-202 |
1.50e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.56 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLET---PTNGRVIFEGNE------------LS 66
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILHVEQEvvgddttalqcvLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 67 NHKNNLNKLRQKMGMVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKV--------------GLE---DK 129
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIdaytaearaasilaGLSftpEM 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515498091 130 ANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDpevVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDV 202
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-238 |
1.66e-09 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.53 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 135 SQLSGGQKQRVAIARAL---AMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKdVSDKVIFMA- 210
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELGp 886
|
90 100 110
....*....|....*....|....*....|....*
gi 515498091 211 -----DGYVIEEGSPQQIFQ--SPTHQRTQNFLSR 238
Cdd:PRK00635 887 eggnlGGYLLASCSPEELIHlhTPTAKALRPYLSS 921
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-194 |
3.06e-09 |
|
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: 56.16 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGeVLAIIGPSGSGKSTLLRCMNLLETPTNGRVI---------------------------------FEGN 63
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgddpdlpeieieltfgsllsrllrllLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 64 ELSNHKNNLNKLRQKMGMVFQNFNlfphkTVLNNIILAPKLLNKSDLNQLKQEALTLLE--KVGLEDKANVYPSQLSGGQ 141
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALN-----ELLSEYLKELLDGLDLELELSLDELEDLLKslSLRIEDGKELPLDRLGSGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 142 KQRVAIARALAMH-------PDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTH 194
Cdd:COG3593 168 QRLILLALLSALAelkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-217 |
5.54e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLlrCMNLLE----TPTNGRVIFEGNELSNH------KNNLNKL---RQKMGMV 82
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTEL--AMSVFGrsygRNISGTVFKDGKEVDVStvsdaiDAGLAYVtedRKGYGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 83 FQNfnlfphkTVLNNIILA--PKLLNKSDLNQ-------------LKQEALTLLEKVGledkanvypsQLSGGQKQRVAI 147
Cdd:NF040905 353 LID-------DIKRNITLAnlGKVSRRGVIDEneeikvaeeyrkkMNIKTPSVFQKVG----------NLSGGNQQKVVL 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 148 ARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEE 217
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-218 |
5.95e-09 |
|
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: 54.57 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLlrCMNLLETPTNGRVIfegNELSNHknnlnkLRQKMGM--------------- 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL--AFDTIYAEGQRRYV---ESLSAY------ARQFLGQmdkpdvdsieglspa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 82 --VFQN-FNLFPHKTV-----LNNI--ILAPKLLNKSDLNQLKQEALTLLEkvgLEDKANVypsqLSGGQKQRVAIARAL 151
Cdd:cd03270 80 iaIDQKtTSRNPRSTVgtvteIYDYlrLLFARVGIRERLGFLVDVGLGYLT---LSRSAPT----LSGGEAQRIRLATQI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 152 AMHPDIIL--FDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEmgfakdvsDKVIFMADgYVIEEG 218
Cdd:cd03270 153 GSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD--------EDTIRAAD-HVIDIG 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-223 |
7.92e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 3 KIENLNKKFGKNE---VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNE--------LSNHKNN 71
Cdd:PRK13545 23 KLKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAaliaissgLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 72 LNKLRQK---MGMVfqnfnlfphKTVLNNIIlaPKLLNKSDLNQLKQEALtllekvgledkanvypSQLSGGQKQRVAIA 148
Cdd:PRK13545 103 IENIELKglmMGLT---------KEKIKEII--PEIIEFADIGKFIYQPV----------------KTYSSGMKSRLGFA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 149 RALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDVSDKVIFMADGYVIEEGSPQQI 223
Cdd:PRK13545 156 ISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
31-207 |
1.38e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.38 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 31 AIIGPSGSGKSTLLRCMNLL---ETPTNGRVIFEGNELSNHKNNLNKLRqkmgMVFQNFNLFPHK-----TVLNNIILap 102
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVRAQVK----LAFENANGKKYTitrslAILENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 103 kllnksdlnqLKQEALT--LLEKVGledkanvypsQLSGGQKQ------RVAIARALAMHPDIILFDEPTSALDPEVVYD 174
Cdd:cd03240 100 ----------CHQGESNwpLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190
....*....|....*....|....*....|....*
gi 515498091 175 VL-KVMKDLAKEG-MTMVVVTHEMGFaKDVSDKVI 207
Cdd:cd03240 160 SLaEIIEERKSQKnFQLIVITHDEEL-VDAADHIY 193
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-170 |
1.48e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 14 NEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFegnelsnHKNNLNKLRQK-MGMVFQNFNLFPHK 92
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-------KNCNINNIAKPyCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 93 TVLNNIILAPKLLNKSdlnQLKQEALTLLEKVGLEDKaNVYpsQLSGGQKQRVAIARALAMHPDIILFDEPTSALDPE 170
Cdd:PRK13541 86 TVFENLKFWSEIYNSA---ETLYAAIHYFKLHDLLDE-KCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
102-240 |
6.91e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.72 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 102 PKLLNKsdlnqlkqeaLTLLEKVGLEdkanvY-----PS-QLSGGQKQRVAIARALAmHPD----IILFDEPTSALDPEv 171
Cdd:COG0178 801 PKIARK----------LQTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELS-KRStgktLYILDEPTTGLHFH- 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 172 vyDV---LKVMKDLAKEGMTMVVVTHEMgfakDV---SDKVIfmaD---------GYVIEEGSPQQIFQSP-THqrTQNF 235
Cdd:COG0178 864 --DIrklLEVLHRLVDKGNTVVVIEHNL----DViktADWII---DlgpeggdggGEIVAEGTPEEVAKVKaSY--TGRY 932
|
....*
gi 515498091 236 LSRVL 240
Cdd:COG0178 933 LKEYL 937
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-211 |
1.94e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGNElsnhknNLNKLRQKMg 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE------RLGKLRQDQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 81 MVFQNFnlfphkTVLNNIILApkllnKSDLNQLKQE------------------------------------ALTLLEKV 124
Cdd:PRK15064 74 FAFEEF------TVLDTVIMG-----HTELWEVKQErdriyalpemseedgmkvadlevkfaemdgytaearAGELLLGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 125 GL-EDKANVYPSQLSGGQKQRVAIARALAMHPDIILFDEPTSALDpevvYDVLKVMKD-LAKEGMTMVVVTHEMGFAKDV 202
Cdd:PRK15064 143 GIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD----INTIRWLEDvLNERNSTMIIISHDRHFLNSV 218
|
....*....
gi 515498091 203 SDKvifMAD 211
Cdd:PRK15064 219 CTH---MAD 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-214 |
2.61e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRV-IFEGNEL---SNHKnnLNKLR 76
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQ--LEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 77 qkmgmvfqnfnlfPHKTVLNNII-LAPKllnksdlnQLKQEALTLLEKVGLE-DKANVYPSQLSGGQKQRVAIARALAMH 154
Cdd:PRK10636 390 -------------ADESPLQHLArLAPQ--------ELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 155 PDIILFDEPTSALDPEVVYDVLKVMKDLakEGmTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-194 |
2.76e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENlnkkFGKNEVLKDINLEikkGEVLAIIGPSGSGKSTLLRCMNLL-------------------ETPTNGRVIFEG 62
Cdd:COG0419 5 LRLEN----FRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRYAlygkarsrsklrsdlinvgSEEASVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 63 N-----------ELSNHKNNLNKLRQKMgmVFQNFNLFPHKTVLNNI-----ILAPKLLNKSDLNQLKQEALTLLEkvGL 126
Cdd:COG0419 78 GgkryrierrqgEFAEFLEAKPSERKEA--LKRLLGLEIYEELKERLkeleeALESALEELAELQKLKQEILAQLS--GL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 127 EDkanvyPSQLSGGQKQRVAIARALAMhpdiiLFDepTSALDPEVVYDVLKVMKDLAkegmtmvVVTH 194
Cdd:COG0419 154 DP-----IETLSGGERLRLALADLLSL-----ILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
118-240 |
3.04e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.76 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 118 LTLLEKVGLEdkanvY-----PS-QLSGGQKQRVAIARAL---AMHPDIILFDEPTSALDpevVYDV---LKVMKDLAKE 185
Cdd:PRK00349 811 LQTLVDVGLG-----YiklgqPAtTLSGGEAQRVKLAKELskrSTGKTLYILDEPTTGLH---FEDIrklLEVLHRLVDK 882
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 186 GMTMVVVTHEMgfakDvsdkVIFMAD-------------GYVIEEGSPQQIFQSPT-HqrTQNFLSRVL 240
Cdd:PRK00349 883 GNTVVVIEHNL----D----VIKTADwiidlgpeggdggGEIVATGTPEEVAKVEAsY--TGRYLKPVL 941
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
92-194 |
4.67e-06 |
|
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: 46.61 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 92 KTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVgLEDKANVYPSQLSGGQKQ---RVAIARALAMHPDIILFDEPTSALD 168
Cdd:pfam13304 193 KLADLNLSDLGEGIEKSLLVDDRLRERGLILLE-NGGGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLH 271
|
90 100
....*....|....*....|....*.
gi 515498091 169 PEVVYDVLKVMKDLAKEGMTMVVVTH 194
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-207 |
5.41e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 1 MIKIENLNKKFGKNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVIFEGN----------------E 64
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalpqpA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 65 LSNHKNNLNKLRQkmgmVFQNFNLFPHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKANVYP-SQLSGGQKQ 143
Cdd:PRK10636 81 LEYVIDGDREYRQ----LEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515498091 144 RVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKegmTMVVVTHEMGFAKDVSDKVI 207
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKII 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-172 |
8.42e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 16 VLKDINLEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPTNGRVifegnelsnhknnLNKLRQKMGMVFQnfnlfpHKTVL 95
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVRMAVFSQ------HHVDG 584
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515498091 96 NNIILAPKL-LNKSDLNQLKQEALTLLEKVGLEDKANVYPS-QLSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVV 172
Cdd:PLN03073 585 LDLSSNPLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-226 |
1.03e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 135 SQLSGGQKQRVAIARALAM---HPDIILFDEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHEMGFAKDvSDKVIFMA- 210
Cdd:PRK00635 1698 SSLSLSEKIAIKIAKFLYLppkHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGp 1776
|
90 100
....*....|....*....|.
gi 515498091 211 -----DGYVIEEGSPQQIFQS 226
Cdd:PRK00635 1777 gsgktGGKILFSGPPKDISAS 1797
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-236 |
1.42e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 137 LSGGQKQRVAIARALAMHPDIILF--DEPTSALDPEVVYDVLKVMKDLAKEGMTMVVVTHE---MGFAKDVSD----KVI 207
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgAGI 556
|
90 100
....*....|....*....|....*....
gi 515498091 208 FmaDGYVIEEGSPQQiFQSPTHQRTQNFL 236
Cdd:PRK00635 557 F--GGEVLFNGSPRE-FLAKSDSLTAKYL 582
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-227 |
3.27e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 116 EALTLLEKVGLEdkaNVYPSQ----LSGGQKQRVAIARALAMHPDIILF--DEPTSAL---DPEVVYDVLKVMKDLakeG 186
Cdd:TIGR00630 467 ERLGFLIDVGLD---YLSLSRaagtLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLhqrDNRRLINTLKRLRDL---G 540
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 515498091 187 MTMVVVTHEmgfaKD---VSDKVIFMA------DGYVIEEGSPQQIFQSP 227
Cdd:TIGR00630 541 NTLIVVEHD----EDtirAADYVIDIGpgagehGGEVVASGTPEEILANP 586
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
17-43 |
3.44e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 3.44e-05
10 20
....*....|....*....|....*..
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTL 43
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
2-194 |
8.95e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLnkkFGKNEVlkDINLEIKKGeVLAIIGPSGSGKSTLLRCMNLL---------------------ETPTNGRVIF 60
Cdd:COG3950 6 LTIENF---RGFEDL--EIDFDNPPR-LTVLVGENGSGKTTLLEAIALAlsgllsrlddvkfrkllirngEFGDSAKLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 61 ----EGNELSNHKNNLNKLRQKMGMVFQNF-NLFPHKTVLNNII-----LAPKLLNKSD------LNQLKQ---EALTLL 121
Cdd:COG3950 80 yygtSRLLLDGPLKKLERLKEEYFSRLDGYdSLLDEDSNLREFLewlreYLEDLENKLSdeldekLEAVREalnKLLPDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 122 EKVGLEDKAN-----------VYPSQLSGGQKQRVA----IARALAMHPD----------IILFDEPTSALDPEVVYDVL 176
Cdd:COG3950 160 KDIRIDRDPGrlvildkngeeLPLNQLSDGERSLLAlvgdLARRLAELNPalenplegegIVLIDEIDLHLHPKWQRRIL 239
|
250
....*....|....*...
gi 515498091 177 KVMKDLAKEgMTMVVVTH 194
Cdd:COG3950 240 PDLRKIFPN-IQFIVTTH 256
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-67 |
1.06e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515498091 22 LEIKKGEVLAIIGPSGSGKSTLLRCMNLLETPtNGRVIFegNELSN 67
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARF--NKAAN 59
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-43 |
1.89e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.89e-04
10 20
....*....|....*....|....*..
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTL 43
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-212 |
2.28e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 115 QEALTLLEKVGLedkANVYPSQ----LSGGQKQRVAIARALAMH-PDII-LFDEPTSALDPEVVYDVLKVMKDLAKEGMT 188
Cdd:PRK00635 1365 LNRLTFIDKVGL---SYITLGQeqdtLSDGEHYRLHLAKKISSNlTDIIyLLEDPLSGLHPQDAPTLLQLIKELVTNNNT 1441
|
90 100
....*....|....*....|....
gi 515498091 189 mVVVTHEMGFAKDVSDKVIFMADG 212
Cdd:PRK00635 1442 -VIATDRSGSLAEHADHLIHLGPG 1464
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
137-239 |
4.75e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 137 LSGGQKQRVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAK--EGMTMVVVTHEMGFAKDVSDKVIFMADGYV 214
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVLMSLLQPAPETFDLFDDIILLSEGQI 416
|
90 100 110
....*....|....*....|....*....|...
gi 515498091 215 IEEGSPQQI--------FQSPTHQRTQNFLSRV 239
Cdd:PLN03140 417 VYQGPRDHIleffescgFKCPERKGTADFLQEV 449
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-44 |
5.30e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 5.30e-04
10 20
....*....|....*....|....*...
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTLL 44
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
17-43 |
5.91e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 5.91e-04
10 20
....*....|....*....|....*..
gi 515498091 17 LKDINLEIKKGEVLAIIGPSGSGKSTL 43
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
135-181 |
7.04e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 7.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 135 SQLSGGQKQR---VAIARALAMH----------PDIILFDEPTSALDPEVVYDVLKVMKD 181
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-50 |
1.13e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 515498091 2 IKIENLnkkfgKNevLKDINLEIkkGEVLAIIGPSGSGKSTLLRCMNLL 50
Cdd:COG4637 5 IRIKNF-----KS--LRDLELPL--GPLTVLIGANGSGKSNLLDALRFL 44
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
13-45 |
1.34e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.79 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|...
gi 515498091 13 KNEVLKDINLEIKKGEVLAIIGPSGSGKSTLLR 45
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLR 198
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
138-211 |
1.68e-03 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 38.73 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 138 SGGQKQRVAIARALAMHPDIILFDEPTSA--------LDPEVVYD--------VLKVMKDLAKEGMTMVVVTHEMGFAKD 201
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSKdkepitpfVDRVRSLYDDLGVSTILVVGGSGDYLD 238
|
90
....*....|
gi 515498091 202 VSDKVIFMAD 211
Cdd:pfam09818 239 VADTVILMDE 248
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
118-227 |
1.96e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 118 LTLLEKVGLEdkanvY-----PSQ-LSGGQKQRVAIARAL------AMHpdiILfDEPTSALDPEvvyD---VLKVMKDL 182
Cdd:COG0178 466 LGFLVDVGLD-----YltldrSAGtLSGGEAQRIRLATQIgsglvgVLY---VL-DEPSIGLHQR---DndrLIETLKRL 533
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 515498091 183 AKEGMTMVVVTHEmgfaKDvsdkVIFMAD-------------GYVIEEGSPQQIFQSP 227
Cdd:COG0178 534 RDLGNTVIVVEHD----ED----TIRAADyiidigpgagehgGEVVAQGTPEEILKNP 583
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
136-185 |
2.71e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 2.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 515498091 136 QLSGGQKQRVAIARALAMH-----PdIILFDEPTSALDPEVVYDVLKVMKDLAKE 185
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaP-FYLFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
15-47 |
3.40e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 38.15 E-value: 3.40e-03
10 20 30
....*....|....*....|....*....|...
gi 515498091 15 EVLKDInLEIKKGEVLaIIGPSGSGKSTLLRCM 47
Cdd:COG2805 115 PVLKEL-AELPRGLVL-VTGPTGSGKSTTLAAM 145
|
|
| RepA_RSF1010_like |
cd01125 |
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family ... |
27-117 |
3.91e-03 |
|
Hexameric Replicative Helicase RepA of plasmid RSF1010 and related proteins; This family includes the homo-hexameric replicative helicase RepA encoded by plasmid RSF1010. RSF1010 is found in most Gram-negative bacteria and some Gram-positive bacteria . The RepA protein of Plasmid RSF1010 is a 5'-3' DNA helicase which can utilize ATP, dATP, GTP and dGTP (and CTP and dCTP to a lesser extent).
Pssm-ID: 410870 Cd Length: 238 Bit Score: 37.36 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 27 GEVLAIIGPSGSGKSTLLRCM-----------NLLETPTnGRVIFEGNELSNHknnlnKLRQKMGMVFQNFNLFPHKTVL 95
Cdd:cd01125 1 GTLGMLVGPPGSGKSFLALDLavavatgrdwlGERRVKQ-GRVVYLAAEDPRD-----GLRRRLKAIGAHLGDEDAALAE 74
|
90 100
....*....|....*....|....*...
gi 515498091 96 NNII------LAPKLLNKSDLNQLKQEA 117
Cdd:cd01125 75 NLVIenlrgkPVSIDAEAPELERIIEEL 102
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-131 |
5.82e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515498091 2 IKIENLNKkfgknevLKDINLEIKKGEVLaIIGPSGSGKSTLLRCMNLL---ETPTNGRVIFEGNElsNHKNNLNKLRQK 78
Cdd:pfam13476 1 LTIENFRS-------FRDQTIDFSKGLTL-ITGPNGSGKTTILDAIKLAlygKTSRLKRKSGGGFV--KGDIRIGLEGKG 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 515498091 79 MGMVFQNFNLfpHKTVLNNIILAPKLLNKSDLNQLKQEALTLLEKVGLEDKAN 131
Cdd:pfam13476 71 KAYVEITFEN--NDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFIS 121
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
138-198 |
6.58e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 37.72 E-value: 6.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515498091 138 SGGQKQ------RVAIARALAMHPDIILFDEPTSALDPEVVYDVLKVMKDLAKE-----GMTMVVVTHEMGF 198
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqrNFQLLVITHDEDF 1272
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
15-60 |
7.98e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 36.69 E-value: 7.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 515498091 15 EVLKDINLEIKKGE-VLAIIGPSGSGKSTLLRCmnLLET-PTNGRVIF 60
Cdd:COG3267 30 EALARLEYALAQGGgFVVLTGEVGTGKTTLLRR--LLERlPDDVKVAY 75
|
|
| |
