|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
12-250 |
0e+00 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 501.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVG 91
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-225 |
9.14e-148 |
|
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: 411.15 E-value: 9.14e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGM 92
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-252 |
5.41e-121 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 345.25 E-value: 5.41e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 7 QPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN--------- 77
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 --EDIRNIERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQR 155
Cdd:COG4598 83 vpADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 156 VAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFF 235
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*..
gi 16131159 236 AHPKSERTRAFLSQVIH 252
Cdd:COG4598 243 GNPKSERLRQFLSSSLK 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-250 |
7.17e-117 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 333.98 E-value: 7.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVG 91
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
13-251 |
4.23e-99 |
|
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: 289.42 E-value: 4.23e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-----------DIR 81
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 NIERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLAsEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 16131159 241 ERTRAFLSQVI 251
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-249 |
2.99e-98 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 287.03 E-value: 2.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKwygQFH---VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDI------R 81
Cdd:PRK11264 2 SAIEVKNLVK---KFHgqtVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 NIERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSE 241
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
....*...
gi 16131159 242 RTRAFLSQ 249
Cdd:PRK11264 239 RTRQFLEK 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-248 |
2.31e-93 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 274.58 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----EDIRNIERVRQ 88
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPdEFFAHPKSERTRAFLS 248
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-248 |
7.13e-91 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 268.04 E-value: 7.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----EDIRNIERVRQ 88
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEfFAHPKSERTRAFLS 248
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYLS 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-252 |
3.72e-90 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 269.64 E-value: 3.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY----GQFHVLKNINLTVQPGE--RIVlcGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----EDIR 81
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEifGII--GYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 nieRVRQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:COG1135 79 ---AARRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDtmigLAQS-----GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILD----LLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|....*.
gi 16131159 237 HPKSERTRAFLSQVIH 252
Cdd:COG1135 231 NPQSELTRRFLPTVLN 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-230 |
6.59e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.96 E-value: 6.59e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIE---LNEDIRN 82
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDissLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 IERvRQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:COG1136 82 RLR-RRHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARtVADRVIFMDRGEIVEQAA 230
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSDER 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
9-241 |
1.89e-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: 250.40 E-value: 1.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQ 88
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNctLA-PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAEN--VAfGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 168 IMLFDEPTSALDP----EMVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSE 241
Cdd:COG3842 156 VLLLDEPLSALDAklreEMREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATR 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-247 |
3.36e-82 |
|
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: 246.04 E-value: 3.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERV 86
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPkSERTRA 245
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 16131159 246 FL 247
Cdd:COG1127 240 FL 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-248 |
5.28e-82 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 246.42 E-value: 5.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----------- 77
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 EDIRNIERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAH-KFPGQISGGQQQRV 156
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|..
gi 16131159 237 HPKSERTRAFLS 248
Cdd:PRK10619 242 NPQSPRLQQFLK 253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-239 |
3.47e-80 |
|
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: 240.56 E-value: 3.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRNIERV- 86
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-LLSGKELRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 -RQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:cd03258 80 aRRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-234 |
4.12e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 241.11 E-value: 4.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDI-RNIERVRQ 88
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQN--------CTLAPIWVRKMPKKEAEdLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIAR 160
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-252 |
1.51e-79 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 242.78 E-value: 1.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL----NEDIRni 83
Cdd:PRK11153 1 MIELKNISKVFPQggrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 eRVRQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLC 163
Cdd:PRK11153 79 -KARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 164 MKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSER 242
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
250
....*....|
gi 16131159 243 TRAFLSQVIH 252
Cdd:PRK11153 237 TREFIQSTLH 246
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
13-248 |
1.85e-79 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 239.50 E-value: 1.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEE-----HQQGRIVVDGIELNEDIRNIERVR 87
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPhLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEH----AHKFPGQISGGQQQRVAIARSLC 163
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 164 MKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERT 243
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRT 239
|
....*
gi 16131159 244 RAFLS 248
Cdd:TIGR00972 240 EDYIS 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-225 |
9.86e-79 |
|
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: 236.23 E-value: 9.86e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRNIERV-- 86
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS-KLSEKELAaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 -RQEVGMVFQHFNLFPHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTvADRVIFMDRGEI 225
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-245 |
2.16e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.91 E-value: 2.16e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNI 83
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------KPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLC 163
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 164 MKPKIMLFDEPTSALDP----EMVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDR--GEIVEQAAPDefFAH 237
Cdd:COG1116 155 NDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVD--LPR 229
|
....*...
gi 16131159 238 PKSERTRA 245
Cdd:COG1116 230 PRDRELRT 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-239 |
2.04e-77 |
|
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: 233.38 E-value: 2.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVG 91
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK--KNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQhfN----LFpHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-250 |
1.14e-76 |
|
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: 240.58 E-value: 1.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 7 QPANAMITLENVNKWY-----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DI 80
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 RNIERVRQEVGMVFQHFN--LFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRI-AEHAHKFPGQISGGQQQRVA 157
Cdd:COG1123 335 RSLRELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 158 IARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
250
....*....|....
gi 16131159 237 HPKSERTRAFLSQV 250
Cdd:COG1123 495 NPQHPYTRALLAAV 508
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-224 |
4.84e-76 |
|
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: 228.23 E-value: 4.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGM 92
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLApiwvrkmpkkeaedlavhylervriaehahkfpgqISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131159 173 EPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-234 |
2.72e-75 |
|
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: 228.61 E-value: 2.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ-FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIER-VRQEV 90
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTLA-----PIW--VRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLC 163
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrSTWrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 164 MKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-229 |
2.74e-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: 2.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNctLA-PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03259 77 VFQDYALFPHLTVAEN--IAfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQA 229
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-240 |
9.31e-75 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 230.73 E-value: 9.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEV 90
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNctLA-PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG3839 78 AMVFQSYALYPHMTVYEN--IAfPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 170 LFDEPTSALDP----EMVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:COG3839 156 LLDEPLSNLDAklrvEMRAEIKRL---HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
13-250 |
3.38e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 226.57 E-value: 3.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQ-EVG 91
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDLFTNLPPRErRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQN--CTLApiwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG1118 79 FVFQHYALFPHMTVAENiaFGLR---VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 170 LFDEPTSALD----PEMVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRA 245
Cdd:COG1118 156 LLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVAR 232
|
....*
gi 16131159 246 FLSQV 250
Cdd:COG1118 233 FLGCV 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-234 |
4.30e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 222.63 E-value: 4.30e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnedIRNIERVRQEVGM 92
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV---ARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
12-237 |
7.87e-71 |
|
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: 217.17 E-value: 7.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYG-QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL-NEDIRNIERVRQE 89
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLA--------PIWVRKMPKKEAEdLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
12-247 |
2.67e-70 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 218.04 E-value: 2.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIR--NIERVRQ 88
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDG----EDIRdlDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRI--AEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 167 KIMLFDEPTSALDPeMVKEVL-DTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTR 244
Cdd:COG1125 156 PILLMDEPFGALDP-ITREQLqDELLRLqRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
...
gi 16131159 245 AFL 247
Cdd:COG1125 235 DFV 237
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-247 |
3.79e-70 |
|
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: 215.44 E-value: 3.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVR 87
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQH----FNlfPHLTVLQncTLA-PIWVRKMPKKEAEdlAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARS 161
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDR--ILAePLRIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*..
gi 16131159 241 ERTRAFL 247
Cdd:COG1124 233 PYTRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-229 |
5.09e-70 |
|
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: 214.68 E-value: 5.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVR 87
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 -QEVGMVFQH----FNlfPHLTVLQncTLA-PIWVRKMPKKEAEDLAVHYLERVRI---AEHAHKFPGQISGGQQQRVAI 158
Cdd:cd03257 81 rKEIQMVFQDpmssLN--PRMTIGE--QIAePLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQA 229
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-227 |
6.37e-70 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 214.15 E-value: 6.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERVRQE 89
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVE 227
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-246 |
1.64e-69 |
|
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: 213.52 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN-IERVRQEVG 91
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLapiWVR---KMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF---PLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPkSERTRAF 246
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-249 |
6.66e-69 |
|
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: 212.16 E-value: 6.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVG 91
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE--QDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRI--AEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLS 248
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
.
gi 16131159 249 Q 249
Cdd:cd03295 238 A 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-240 |
1.44e-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: 210.94 E-value: 1.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-234 |
1.57e-68 |
|
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: 210.89 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQ-----GRIVVDGIELNEDIRNIERVR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPhLTVLQNCTLAPiWVRKM-PKKEAEDLAVHYLERV----RIAEHAHkfPGQISGGQQQRVAIARSL 162
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAalwdEVKDRLH--ALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-228 |
1.06e-67 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 208.48 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERVRQ 88
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 169 MLFDEPTSALDP----EMVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDR--GEIVEQ 228
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
1.42e-67 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 209.51 E-value: 1.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILlQPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ-----QGRIVVDGIE 75
Cdd:COG1117 1 MTAPA-STLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 76 LNEDIRNIERVRQEVGMVFQHFNLFPHlTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHA----HKFPGQISGG 151
Cdd:COG1117 80 IYDPDVDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 152 QQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAP 231
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPT 237
|
250
....*....|....*..
gi 16131159 232 DEFFAHPKSERTRAFLS 248
Cdd:COG1117 238 EQIFTNPKDKRTEDYIT 254
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-224 |
1.93e-65 |
|
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: 202.31 E-value: 1.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVRQEVGM 92
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKL--SLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNL-FPHLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-240 |
8.30e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 207.45 E-value: 8.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ---QGRIVVDGIEL---NEDIR 81
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 niervRQEVGMVFQHF--NLFPhLTVLQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIA 159
Cdd:COG1123 82 -----GRRIGMVFQDPmtQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
..
gi 16131159 239 KS 240
Cdd:COG1123 235 QA 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-250 |
7.75e-63 |
|
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: 197.87 E-value: 7.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----EDIRNIERvrQEVGMVFQHFN 98
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrKELRELRR--KKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 LFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSAL 178
Cdd:cd03294 113 LLPHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 179 DPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:cd03294 192 DPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
12-247 |
4.16e-62 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 194.59 E-value: 4.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHvlKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVG 91
Cdd:COG3840 1 MLRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----QDLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLApiwVRKMPKKEAEDLA--VHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLG---LRPGLKLTAEQRAqvEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFL 247
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
13-240 |
5.24e-61 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 195.64 E-value: 5.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGG----RDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCT--LAPiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAygLKN---RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 171 FDEPTSALDPEmVKEVLDTMIGLAQS--GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:TIGR03265 158 LDEPLSALDAR-VREHLRTEIRQLQRrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPAT 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-250 |
7.61e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 196.09 E-value: 7.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN----EDIRNIeRvRQEVGMVFQHFNLFPHL 103
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITklskKELREL-R-RKKMSMVFQHFALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 TVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP--- 180
Cdd:COG4175 121 TVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlir 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 181 -EMVKEVLDtmigLaQSGM--TMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:COG4175 200 rEMQDELLE----L-QAKLkkTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-234 |
8.10e-61 |
|
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: 191.11 E-value: 8.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ERVRQE 89
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGLpphERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEdlavhyLERV-----RIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLG-AYARRRAKRKAR------LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
12-252 |
7.68e-60 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 192.40 E-value: 7.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdIRNIERV- 86
Cdd:TIGR02314 1 MIKLSNITKVFHQgtktIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTT-LSNSELTk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 -RQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:TIGR02314 80 aRRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTR 244
Cdd:TIGR02314 159 PKVLLCDEATSALDPATTQSILELLKEInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQ 238
|
....*...
gi 16131159 245 AFLSQVIH 252
Cdd:TIGR02314 239 KFIRSTLH 246
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
12-248 |
1.15e-59 |
|
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: 191.03 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ---QGRIVVDGIEL----NEDI 80
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLlklsEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 RNIeRVRqEVGMVFQH----FNlfPHLTVLQncTLA-PIWV-RKMPKKEAEDLAVHYLERVRI---AEHAHKFPGQISGG 151
Cdd:COG0444 81 RKI-RGR-EIQMIFQDpmtsLN--PVMTVGD--QIAePLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 152 QQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAA 230
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250
....*....|....*...
gi 16131159 231 PDEFFAHPKSERTRAFLS 248
Cdd:COG0444 235 VEELFENPRHPYTRALLS 252
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-247 |
1.26e-59 |
|
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: 188.27 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ERVR 87
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGLpphRIAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPHLTVLQNCTLAPiWVRKMPKKEAEDLavhylERV-----RIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLLGA-YARRDRAEVRADL-----ERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPksER 242
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EV 229
|
....*
gi 16131159 243 TRAFL 247
Cdd:COG0410 230 REAYL 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
15-239 |
2.46e-59 |
|
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: 187.64 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ERVRQEVG 91
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG----EDITGLpphEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLA-------PIWVRKMPKKEAE--DLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAaqartgsGLLLARARREEREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-252 |
9.31e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.45 E-value: 9.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERVR 87
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNL---FPhLTVLQ---NCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:COG1121 75 RRIGYVPQRAEVdwdFP-ITVRDvvlMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGeIVEQAAPDEFFAHPKSE 241
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLS 232
|
250
....*....|.
gi 16131159 242 RTRAFLSQVIH 252
Cdd:COG1121 233 RAYGGPVALLA 243
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-227 |
1.16e-58 |
|
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: 185.15 E-value: 1.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRNIERvrqEVGM 92
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDR---DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEdlavhylERVR-------IAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEID-------ERVRevaellqIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVE 227
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-237 |
1.27e-58 |
|
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: 186.87 E-value: 1.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIE-LNEDirNIERVRQE 89
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEE--NLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQH-FNLFPHLTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFArTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-233 |
1.89e-58 |
|
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: 185.33 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 7 QPANAMITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL---NED 79
Cdd:COG4181 3 SSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 80 IRniERVR-QEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPkkEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAI 158
Cdd:COG4181 83 AR--ARLRaRHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDE 233
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-225 |
2.23e-57 |
|
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: 180.29 E-value: 2.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNediRNIERVRQEVGM 92
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK---KEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNctlapiwvrkmpkkeaedlaVHYlervriaehahkfpgqiSGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03230 78 LPEEPSLYENLTVREN--------------------LKL-----------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
12-233 |
3.04e-57 |
|
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: 182.94 E-value: 3.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRNIERVRQeVG 91
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQncTLA-------PIWVRkmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:COG1120 79 YVPQEPPAPFGLTVRE--LVAlgryphlGLFGR--PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
28-250 |
4.64e-57 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 185.83 E-value: 4.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERV------RQEVGMVFQHFNLFP 101
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDG----ENIMKQSPVelrevrRKKIGMVFQQFALFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTLAPiWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPE 181
Cdd:TIGR01186 85 HMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 182 MVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:TIGR01186 164 IRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-247 |
1.49e-56 |
|
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: 180.61 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLA----PIWVRKmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrvkPRSERP-PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFL 247
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
9-239 |
1.86e-56 |
|
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: 181.00 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ER 85
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITGLpphRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQHFNLFPHLTVLQNCTLA--------------PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGG 151
Cdd:COG0411 77 ARLGIARTFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 152 QQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAA 230
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 16131159 231 PDEFFAHPK 239
Cdd:COG0411 237 PAEVRADPR 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-248 |
2.80e-56 |
|
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: 179.84 E-value: 2.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHvLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 173 EPTSALDPEmVKEVLDTMIGLAQ--SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLS 248
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIRkeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
13-225 |
1.39e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.32 E-value: 1.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGM 92
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHlTVLQNctLAPIWVRKmPKKEAEDLAVHYLERVRIAEHA-HKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:COG4619 79 VPQEPALWGG-TVRDN--LPFPFQLR-ERKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 172 DEPTSALDPEMVKEVLDtMIG--LAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:COG4619 155 DEPTSALDPENTRRVEE-LLReyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-241 |
7.95e-55 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 179.53 E-value: 7.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDI--RNIERvr 87
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG----EDVthRSIQQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSE 241
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
13-239 |
1.03e-54 |
|
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: 177.26 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-EDIRNIERV 86
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQhfnlFPH-----LTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEH-AHKFPGQISGGQQQRVAIAR 160
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-234 |
1.62e-54 |
|
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: 175.43 E-value: 1.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRnieRVRQEVG 91
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR---EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-252 |
4.19e-54 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 177.97 E-value: 4.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNC----TLAPiwVRKMPKKEAEDLAV-HYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIafglTVLP--RRERPNAAAIKAKVtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAF 246
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEF 236
|
....*.
gi 16131159 247 LSQVIH 252
Cdd:PRK10851 237 MGEVNR 242
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
15-220 |
6.43e-53 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 170.10 E-value: 6.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGiELNEDIRNIERV---RQEVG 91
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNG-QETPPLNSKKASkfrREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPIWVRKmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARtVADRVIFM 220
Cdd:TIGR03608 159 DEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
13-239 |
2.67e-52 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 173.98 E-value: 2.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGM 92
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDITHVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPK 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-233 |
3.05e-52 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 180.03 E-value: 3.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIER--VRQ 88
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDPasLRR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFpHLTVLQNCTLApiwvrkmpKKEAEDLAVHY-LERVRIAEHAHKFP-----------GQISGGQQQRV 156
Cdd:COG2274 550 QIGVVLQDVFLF-SGTIRENITLG--------DPDATDEEIIEaARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARtVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEE 695
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-224 |
9.05e-52 |
|
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: 167.43 E-value: 9.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERVRQE 89
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
14-224 |
1.08e-51 |
|
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: 165.50 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMV 93
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 94 FQhfnlfphltvlqnctlapiwvrkmpkkeaedlavhylervriaehahkfpgqISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-250 |
3.97e-51 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 170.79 E-value: 3.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVG 91
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG----VDLSHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 172 DEPTSALDPE----MVKEVLDTmigLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFL 247
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
...
gi 16131159 248 SQV 250
Cdd:PRK11607 251 GSV 253
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-176 |
4.20e-51 |
|
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: 163.59 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRniERVRQEVGMVFQHFNLFPHLTVLQ 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER--KSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 108 NCTLAPIwVRKMPKKEAEDLAVHYLERVRI----AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTS 176
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-250 |
1.52e-50 |
|
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: 168.06 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 43 LCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKK 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG----EDVTNVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 123 EAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEV---LDTMigLAQSGMT 199
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqleLKTI--QEQLGIT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16131159 200 MLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-233 |
2.94e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.04 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNkwygqFH------VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneD 79
Cdd:COG1132 333 LPPVRGEIEFENVS-----FSypgdrpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----D 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 80 IRNI--ERVRQEVGMVFQHFNLFpHLTVLQNCTLApiwvrkmpKKEAEDLAV-HYLERVRIAEHAHKFPG---------- 146
Cdd:COG1132 404 IRDLtlESLRRQIGVVPQDTFLF-SGTIRENIRYG--------RPDATDEEVeEAAKAAQAHEFIEALPDgydtvvgerg 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 147 -QISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHemgfaR--TV--ADRVIFMD 221
Cdd:COG1132 475 vNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH-----RlsTIrnADRILVLD 548
|
250
....*....|..
gi 16131159 222 RGEIVEQAAPDE 233
Cdd:COG1132 549 DGRIVEQGTHEE 560
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-233 |
6.20e-50 |
|
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: 171.87 E-value: 6.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVN-KWYGQ-FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRniER 85
Cdd:COG4987 329 PGGPSLELEDVSfRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE--DD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQHfnlfPHL---TVLQNCTLApiwvrkmpKKEAED---LAVhyLERVRIAEHAHKFPG-----------QI 148
Cdd:COG4987 407 LRRRIAVVPQR----PHLfdtTLRENLRLA--------RPDATDeelWAA--LERVGLGDWLAALPDgldtwlgeggrRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEM-GFARtvADRVIFMDRGEIVE 227
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLaGLER--MDRILVLEDGRIVE 549
|
....*.
gi 16131159 228 QAAPDE 233
Cdd:COG4987 550 QGTHEE 555
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-224 |
8.69e-50 |
|
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: 161.01 E-value: 8.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVRQEV 90
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFpHLTVLQNctlapiwvrkmpkkeaedlavhylervrIaehahkfpgqISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03228 79 AYVPQDPFLF-SGTIREN----------------------------I----------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARtVADRVIFMDRGE 224
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-247 |
3.35e-49 |
|
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: 169.09 E-value: 3.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL----EEHQQGRIVVDGIELNE-DIRNIERVR-QEVGMVFQH 96
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGlSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 97 ----FNlfPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHK---FPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG4172 101 pmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFL 247
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-223 |
9.38e-49 |
|
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: 159.62 E-value: 9.38e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERVRQEVGMVF 94
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNL---FPhLTVLQ----NCTLAPIWVRKmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:cd03235 75 QRRSIdrdFP-ISVRDvvlmGLYGHKGLFRR-LSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRG 223
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-248 |
2.63e-48 |
|
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: 166.78 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 7 QPANAMITLENVNKWY-----------GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEhQQGRIVVDGIE 75
Cdd:COG4172 270 PDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 76 LNE-DIRNIERVRQEVGMVFQ----HFNlfPHLTVLQncTLA-PIWV--RKMPKKEAEDLAVHYLERVRI-AEHAHKFPG 146
Cdd:COG4172 349 LDGlSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQ--IIAeGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPH 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 147 QISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:COG4172 425 EFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
250 260
....*....|....*....|...
gi 16131159 226 VEQAAPDEFFAHPKSERTRAFLS 248
Cdd:COG4172 505 VEQGPTEQVFDAPQHPYTRALLA 527
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-250 |
4.57e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 161.44 E-value: 4.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILLQpanamitLENVNKWY-----------GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRI 69
Cdd:COG4608 3 MAEPLLE-------VRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 70 VVDGIELNE-DIRNIERVRQEVGMVFQ--HFNLFPHLTVLQncTLA-PIWVRKM-PKKEAEDLAVHYLERVRI-AEHAHK 143
Cdd:COG4608 76 LFDGQDITGlSGRELRPLRRRMQMVFQdpYASLNPRMTVGD--IIAePLRIHGLaSKAERRERVAELLELVGLrPEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 144 FPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDR 222
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLqDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260
....*....|....*....|....*...
gi 16131159 223 GEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:COG4608 234 GKIVEIAPRDELYARPLHPYTQALLSAV 261
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
12-225 |
4.94e-48 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 158.34 E-value: 4.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYG----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRNIERV- 86
Cdd:NF038007 1 MLNMQNAEKCYItktiKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEV-TNLSYSQKIi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 --RQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:NF038007 80 lrRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGfARTVADRVIFMDRGEI 225
Cdd:NF038007 159 NPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-237 |
1.16e-47 |
|
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: 165.70 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 2 SQILLQPANAMITLENVN-KWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDi 80
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 rNIERVRQEVGMVFQHFNLFpHLTVLQNCTLApiwvrkmpKKEAEDLAVHY-LERVRIAEHAHKFPGQI----------- 148
Cdd:COG4988 405 -DPASWRRQIAWVPQNPYLF-AGTIRENLRLG--------RPDASDEELEAaLEAAGLDEFVAALPDGLdtplgeggrgl 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARtVADRVIFMDRGEIVEQ 228
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLA-QADRILVLDDGRIVEQ 552
|
....*....
gi 16131159 229 AAPDEFFAH 237
Cdd:COG4988 553 GTHEELLAK 561
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-228 |
1.65e-47 |
|
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: 156.50 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGqfHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIERVRQEVGM 92
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVhYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 173 EPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQ 228
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-249 |
2.09e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 158.25 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERV 86
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE--TVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQH-FNLFPHLTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAI 158
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVqddvafgLEN--------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
250 260
....*....|....*....|...
gi 16131159 238 -----------PKSERTRAFLSQ 249
Cdd:PRK13635 231 ghmlqeigldvPFSVKLKELLKR 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
14-228 |
2.69e-47 |
|
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: 154.90 E-value: 2.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdIRNIERVRQeVGMV 93
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSPKELARK-IAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 94 FQhfnlfphltvlqnctlapiwvrkmpkkeaedlavhYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQ 228
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-225 |
2.86e-47 |
|
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: 156.03 E-value: 2.86e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHV-LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN-IERVRQEV 90
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-235 |
1.64e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 155.92 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVR 87
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQH-FNLFPHLTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIA 159
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGM-TMLCVTHEMGFArTVADRVIFMDRGEIVEQAAPDEFF 235
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
11-238 |
4.20e-46 |
|
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: 157.18 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLeNVNKWYGQFHVlkNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNI----ERV 86
Cdd:COG4148 1 MMLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIflppHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RqeVGMVFQHFNLFPHLTVLQNCTLApiwVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:COG4148 78 R--IGYVFQEARLFPHLSVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-248 |
5.50e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 154.23 E-value: 5.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQ-----GRIVVDGIEL-NEDIRNIErV 86
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIySPDVDPIE-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQHFNLFPHLTVLQNCTLApIWVRKM--PKKEAEDLAVHYLERVRIAEHA----HKFPGQISGGQQQRVAIAR 160
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLvkSKKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLaQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
....*...
gi 16131159 241 ERTRAFLS 248
Cdd:PRK14267 242 ELTEKYVT 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-239 |
9.00e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 156.73 E-value: 9.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdirnIERVRQEV 90
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCT----LApiwvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSfglkLA-----GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 167 KIMLFDEPTSALDP----EMVKEVLDTMIGLaqsGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:PRK11000 153 SVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-248 |
1.32e-45 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 153.01 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL-----EEHQQGRIVVDGIELNEDIRNIER 85
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQHFNLFPhLTVLQNCTLApIWVRKMPKKEAEDLAVH-YLERVRI----AEHAHKFPGQISGGQQQRVAIAR 160
Cdd:PRK14239 84 LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIKDKQVLDEAVEkSLKGASIwdevKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
....*...
gi 16131159 241 ERTRAFLS 248
Cdd:PRK14239 241 KETEDYIS 248
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-226 |
2.85e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 151.12 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNediRNIERVRQEV 90
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTL-APIwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLaQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-250 |
5.73e-45 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 155.58 E-value: 5.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE--DIRNIERVRQEVGMVFQHFNLFPHLTV 105
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKE 185
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 186 VLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
27-242 |
1.60e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 151.00 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGMVFQHFN--LFPHlT 104
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVK 184
Cdd:PRK13639 96 VEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 185 EVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSER 242
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-233 |
1.76e-44 |
|
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: 151.39 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 20 KWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnedIRNIERVRQEVGMVFQHFNL 99
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV---VREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPHLTVLQNCTL-APIWvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSAL 178
Cdd:TIGR01188 78 DEDLTGRENLEMmGRLY--GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 179 DPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-248 |
1.21e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 147.75 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL-----EEHQQGRIVVDGielnEDI--RNI 83
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDG----QDIfkMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKM-PKKEAEDLAVHYLERVRIAEHAHKF----PGQISGGQQQRVAI 158
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
250
....*....|
gi 16131159 239 KSERTRAFLS 248
Cdd:PRK14247 237 RHELTEKYVT 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-233 |
2.09e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 146.65 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVlkNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVG 91
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTL--AP-IWVRKMPKKEAEDLAvhylERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLglNPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 169 MLFDEPTSALDP----EM---VKEVLDtmiglaQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK10771 151 LLLDEPFSALDPalrqEMltlVSQVCQ------ERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-232 |
3.95e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 146.93 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQF----HVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERV 86
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:COG4525 75 GADRGVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 167 KIMLFDEPTSALDpEMVKEvldTMIGL-----AQSGMTMLCVTHEMGFARTVADRVIFMDR--GEIVEQAAPD 232
Cdd:COG4525 154 RFLLMDEPFGALD-ALTRE---QMQELlldvwQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLELD 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-213 |
4.41e-43 |
|
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: 144.93 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIrniERVRQEV 90
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTL-APIWVRKMPKKEAEDLavhyLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFwAALYGLRADREAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH---EMGFARTV 213
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVL 200
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-237 |
9.32e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 146.43 E-value: 9.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN--IER 85
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQhfnlFPHL-----TVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHA-HKFPGQISGGQQQRVAIA 159
Cdd:PRK13649 83 IRKKVGLVFQ----FPESqlfeeTVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
28-223 |
1.04e-42 |
|
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: 144.92 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERVRQEVGMVFQHFNLFPHLTVLQ 107
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 108 NCTLAPIWV-RKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEV 186
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131159 187 LDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRG 223
Cdd:TIGR01184 154 QEELMQIWEeHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-233 |
2.78e-42 |
|
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: 143.28 E-value: 2.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNierVRQEVGM 92
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE---VRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTL-APIWvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIhARLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 172 DEPTSALDP---EMVKEVLDTMigLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:cd03265 156 DEPTIGLDPqtrAHVWEYIEKL--KEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-234 |
4.06e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNIERVRQ 88
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV--RFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 E-VGMVFQHFNLFPHLTVLQNctlapIWVRKMPK-------KEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIAR 160
Cdd:COG1129 79 AgIAIIHQELNLVPNLSVAEN-----IFLGREPRrgglidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRV-IFMDrGEIVEQAAPDEF 234
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVtVLRD-GRLVGTGPVAEL 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-240 |
4.33e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 146.53 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQE 89
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG----RVVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNctLApiW---VRKMPKKEAEDlavhylervRIAEHA---------HKFPGQISGGQQQRVA 157
Cdd:PRK11650 78 IAMVFQNYALYPHMSVREN--MA--YglkIRGMPKAEIEE---------RVAEAArilelepllDRKPRELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 158 IARSLCMKPKIMLFDEPTSALDP----EMVKEVLDtmigLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIvEQ-AAP 231
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQR----LHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA-EQiGTP 219
|
....*....
gi 16131159 232 DEFFAHPKS 240
Cdd:PRK11650 220 VEVYEKPAS 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-233 |
1.84e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.87 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRN-IERVRQEV 90
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV--RIRSpRDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTLA--PIWVRKMPKKEAedlavhyleRVRIAEHAHKFP---------GQISGGQQQRVAIA 159
Cdd:COG3845 83 GMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAA---------RARIRELSERYGldvdpdakvEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-226 |
1.96e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.33 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-EDIRNI-----ER 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDpEDRRRIgylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 vrqevGmvfqhfnLFPHLTVLQNCT-LAPIwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:COG4152 81 -----G-------LYPKMKVGEQLVyLARL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-236 |
2.17e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 142.95 E-value: 2.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQ---FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVR 87
Cdd:PRK13650 3 NIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQH-FNLFPHLTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIA 159
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGfARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-248 |
2.51e-41 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 141.12 E-value: 2.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDI---RNIERVRQEV 90
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG----EDItklPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTL----APIWVRKMPKkEAEDLaVHYLERVRiaehaHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTglaaLPRRSRKIPD-EIYEL-FPVLKEML-----GRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFfahpKSERTRA 245
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRR 226
|
...
gi 16131159 246 FLS 248
Cdd:TIGR03410 227 YLA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-229 |
3.85e-41 |
|
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: 140.12 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQ---PGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQE--VGMVFQHFNLFPH 102
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQrkIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTVLQNCTLAPIWVRKMPKKEAEDlavHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131159 183 VKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQA 229
Cdd:cd03297 167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-229 |
6.48e-41 |
|
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: 139.66 E-value: 6.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNediRNIERVRQeVGM 92
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ---KNIEALRR-IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQN----CTLAPIwvrkmPKKEAEDLavhyLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:cd03268 77 LIEAPGFYPNLTARENlrllARLLGI-----RKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQA 229
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-235 |
9.52e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 141.38 E-value: 9.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY-----GQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIElNEDIRNI 83
Cdd:PRK13633 2 NEMIKCKNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQH-FNLFPHLTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:PRK13633 81 WDIRNKAGMVFQNpDNQIVATIVEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFArTVADRVIFMDRGEIVEQAAPDEFF 235
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
13-228 |
1.02e-40 |
|
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: 139.25 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGeRIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIervRQEVGM 92
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---RRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQncTLAPI-WVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 172 DEPTSALDPEMvKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQ 228
Cdd:cd03264 155 DEPTAGLDPEE-RIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-234 |
1.03e-40 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 140.92 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL-------EEHQQ--GRIVVDGIELNEDIRn 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksaGSHIEllGRTVQREGRLARDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 ieRVRQEVGMVFQHFNLFPHLTVLQNCTLA-----PIW---VRKMPKKEAEDlAVHYLERVRIAEHAHKFPGQISGGQQQ 154
Cdd:PRK09984 83 --KSRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 16131159 234 F 234
Cdd:PRK09984 240 F 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-238 |
1.52e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 141.91 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 24 QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNED--------------IRNIERVRQE 89
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKknnhelitnpyskkIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQ--HFNLFPHlTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAE-HAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-226 |
1.96e-40 |
|
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: 138.49 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIERV--RQ 88
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLDPAdlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFpHLTVLQNCTLApiwvrkMPkkEAEDLAVhyLERVRIA-------EHAHKFPGQI-------SGGQQQ 154
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLG------AP--LADDERI--LRAAELAgvtdfvnKHPNGLDLQIgergrglSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALD---PEMVKEVLDTMIGlaqsGMTMLCVTHEMGFArTVADRVIFMDRGEIV 226
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDmnsEERLKERLRQLLG----DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-238 |
3.48e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 139.74 E-value: 3.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ-FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRNIERVRQEV 90
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG-DFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNL-FPHLTVLQ-------NCTLAPIWVRKMPkkeaeDLAvhyLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEdlafgpeNLCLPPIEIRKRV-----DRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGfARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-236 |
4.82e-40 |
|
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: 138.13 E-value: 4.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ-FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNI--ERVRQE 89
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVtlDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFpHLTVLQNCTLApiwvrkmpKKEAEDLAVhylERVRIAEHAH----KFPGQ-----------ISGGQQQ 154
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRYG--------RPDATDEEV---IEAAKAAQIHdkimRFPDGydtivgerglkLSGGEKQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMgfaRTV--ADRVIFMDRGEIVEQAAPD 232
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHE 220
|
....
gi 16131159 233 EFFA 236
Cdd:cd03253 221 ELLA 224
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
3-236 |
5.57e-40 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 145.23 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 3 QILLQPANAMITLENVNKWYGQ---FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneD 79
Cdd:TIGR02204 328 KTLPVPLRGEIEFEQVNFAYPArpdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV----D 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 80 IRNIER--VRQEVGMVFQHFNLFPHlTVLQNCtlapiwvrKMPKKEAEDLAVhylERVRIAEHAHKFPGQ---------- 147
Cdd:TIGR02204 404 LRQLDPaeLRARMALVPQDPVLFAA-SVMENI--------RYGRPDATDEEV---EAAARAAHAHEFISAlpegydtylg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 148 -----ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPE---MVKEVLDTMIglaqSGMTMLCVTHEMGfarTV--ADRV 217
Cdd:TIGR02204 472 ergvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAEseqLVQQALETLM----KGRTTLIIAHRLA---TVlkADRI 544
|
250
....*....|....*....
gi 16131159 218 IFMDRGEIVEQAAPDEFFA 236
Cdd:TIGR02204 545 VVMDQGRIVAQGTHAELIA 563
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-235 |
6.68e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.41 E-value: 6.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGMVFQH--FNLFPHlTV 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYpeYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCTLAPIwVRKMPKKEAEDLAVHYLERVRIA--EHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMV 183
Cdd:PRK13637 102 EKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16131159 184 KEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFF 235
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-226 |
8.88e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 139.45 E-value: 8.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ-----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL-------------EEHQQGRIVVDGI 74
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 75 ELNED---------IRNIERVRQEVGMVFQ--HFNLFPHlTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAE-HAH 142
Cdd:PRK13651 83 VLEKLviqktrfkkIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 143 KFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDR 222
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....
gi 16131159 223 GEIV 226
Cdd:PRK13651 241 GKII 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-223 |
1.01e-39 |
|
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: 137.18 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKwygQF--H--------VLKNINLTVQPGERIVLCGPSGSGKSTTIRCI--NHLEehQQGRIVVDGIELN 77
Cdd:COG4778 2 TTLLEVENLSK---TFtlHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLP--DSGSILVRHDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 EDI-----RNIERVRQ-EVGMVFQHFNLFPHLTVLQnCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEH-AHKFPGQISG 150
Cdd:COG4778 77 VDLaqaspREILALRRrTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 151 GQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRG 223
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
14-226 |
1.23e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 136.23 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVN-KWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQeVGM 92
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKS-IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQH--FNLFPHlTVLQNCTLapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03226 76 VMQDvdYQLFTD-SVREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-247 |
1.82e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 137.49 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG--IELNEDIRNIE--RVRQEVGMVFQHFNLFPH 102
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFQIDaiKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTVLQNCTLaPIWVRKMP-KKEAEDLAVHYLERVRIAEHAHKF----PGQISGGQQQRVAIARSLCMKPKIMLFDEPTSA 177
Cdd:PRK14246 105 LSIYDNIAY-PLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 178 LDPeMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFL 247
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-226 |
2.86e-39 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 133.71 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedIRN-IERVRQEVG 91
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--FASpRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQhfnlfphltvlqnctlapiwvrkmpkkeaedlavhylervriaehahkfpgqISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03216 79 MVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
27-210 |
3.64e-39 |
|
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: 134.47 E-value: 3.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGMVFQHFN--LFpHLT 104
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF-AAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLAPiwvRKMPKKEAEDLAV--HYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:TIGR01166 86 VDQDVAFGP---LNLGLSEAEVERRvrEALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*...
gi 16131159 183 VKEVLDTMIGLAQSGMTMLCVTHEMGFA 210
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-228 |
5.00e-39 |
|
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: 134.99 E-value: 5.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 32 NLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQEVGMVFQHFNLFPHLTVLQNCTL 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND----QSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 112 A---PIWVRKMPKKEAEDLAvhylERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLD 188
Cdd:TIGR01277 94 GlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131159 189 TMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQ 228
Cdd:TIGR01277 170 LVKQLCsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
10-226 |
1.20e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.17 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG---IELNEDIRN 82
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 IERvRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:PRK10535 82 QLR-REHFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 163 CMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFMDRGEIV 226
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
23-244 |
1.92e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 134.96 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNIERVRQEVGMVFQHFN--LF 100
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL--EYGDYKYRCKHIRMIFQDPNtsLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 PHLTVLQncTL-AP-IWVRKMPKKEAEDLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSA 177
Cdd:COG4167 102 PRLNIGQ--ILeEPlRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 178 LDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTR 244
Cdd:COG4167 180 LDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTK 247
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-238 |
2.14e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 135.53 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVV--DGIELNEDIRNIERVRQEVGMVFQhfnlFPHL-- 103
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgeRVITAGKKNKKLKPLRKKVGIVFQ----FPEHql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 ---TVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHA-HKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:PRK13634 99 feeTVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 180 PEMVKEVLDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
27-238 |
2.22e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 135.31 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL---EEHQQGRIVVDGIELNEDirNIERVRQEVGMVFQH-FNLFPH 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAK--TVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPT 175
Cdd:PRK13640 100 ATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 176 SALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFArTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-233 |
2.50e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.47 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRNIERVRQeVG 91
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL-AAWSPWELARR-RA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNL-FPhLTVLQnctlapiwVRKM-------PKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLC 163
Cdd:COG4559 79 VLPQHSSLaFP-FTVEE--------VVALgraphgsSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 164 -------MKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-236 |
3.05e-38 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 133.12 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVG 91
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRD--ISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHlTVLQNCTLApiwvRKMPKKEAEDLAvhyLERVRIAEHAHKFP-----------GQISGGQQQRVAIAR 160
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLG----RPNATDEEVIEA---AKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLaQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
11-233 |
3.42e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 134.13 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRNIERVRQeV 90
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPL-ADWSPAELARR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNL-FPhLTVLQnctlapiwVRKM-------PKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSL 162
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEE--------VVAMgraphglSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 163 C------MKPKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-238 |
4.35e-38 |
|
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: 136.40 E-value: 4.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 17 NVNKWYGQFHVlkNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNI----ERVRqeVGM 92
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppEKRR--IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLA-----PIWVRKMPKKEAEDLAV-HYLERvriaehahkFPGQISGGQQQRVAIARSLCMKP 166
Cdd:TIGR02142 80 VFQEARLFPHLSVRGNLRYGmkrarPSERRISFERVIELLGIgHLLGR---------LPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
13-236 |
5.31e-38 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 133.05 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNkwygqFH--------VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIR--N 82
Cdd:cd03249 1 IEFKNVS-----FRypsrpdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRdlN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 IERVRQEVGMVFQHFNLFPhLTVLQNCTLApiwvrkmpKKEAEDLAVhylERVRIAEHAHKF----P-----------GQ 147
Cdd:cd03249 72 LRWLRSQIGLVSQEPVLFD-GTIAENIRYG--------KPDATDEEV---EEAAKKANIHDFimslPdgydtlvgergSQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 148 ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTmIGLAQSGMTMLCVTHEMGfarTV--ADRVIFMDRGEI 225
Cdd:cd03249 140 LSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEA-LDRAMKGRTTIVIAHRLS---TIrnADLIAVLQNGQV 215
|
250
....*....|.
gi 16131159 226 VEQAAPDEFFA 236
Cdd:cd03249 216 VEQGTHDELMA 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-225 |
8.82e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 132.88 E-value: 8.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdirnierVRQEVGM 92
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-------AREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLAPiwvrkmpKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131159 173 EPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-228 |
9.26e-38 |
|
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: 131.63 E-value: 9.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN-IERVRQEVG 91
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 mvfqhfnLFPHLTVLQNCT-LAPIwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03269 81 -------LYPKMKVIDQLVyLAQL--KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQ 228
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
12-218 |
1.43e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.06 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCIN-HLEEH--QQGRIVVDGIELNEdiRNIERvRQ 88
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTA--LPAEQ-RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 eVGMVFQHFNLFPHLTVLQNCTLA-PiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:COG4136 78 -IGILFQDDLLFPHLSVGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131159 168 IMLFDEPTSALDPEMVKEVLD---TMIglAQSGMTMLCVTHEMGFARtVADRVI 218
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREfvfEQI--RQRGIPALLVTHDEEDAP-AAGRVL 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-231 |
1.95e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.55 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFN--LFPhL 103
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKVGLVFQDPDdqVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 TVLQNCTLAPIWVRkMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMV 183
Cdd:PRK13647 96 TVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131159 184 KEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAP 231
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-239 |
3.68e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 132.26 E-value: 3.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG--IELNEDIRNIER 85
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQhfnlFPHLTVLQNCTLAPiwVRKMPK------KEAEDLAVHYLERVRIAEH-AHKFPGQISGGQQQRVAI 158
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENTVLKD--VEFGPKnfgfseDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
.
gi 16131159 239 K 239
Cdd:PRK13641 237 E 237
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-248 |
5.28e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 136.37 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTT----IRCINhleehQQGRIVVDGIELNE-DIRNIERVRQEVGMVFQHF 97
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 98 N--LFPHLTVLQNCtlapiwvrkmpkkeAEDLAVHYL--------ERVRIA--------EHAHKFPGQISGGQQQRVAIA 159
Cdd:PRK15134 372 NssLNPRLNVLQII--------------EEGLRVHQPtlsaaqreQQVIAVmeevgldpETRHRYPAEFSGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
250
....*....|
gi 16131159 239 KSERTRAFLS 248
Cdd:PRK15134 518 QQEYTRQLLA 527
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
12-232 |
6.27e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.59 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIElnedirnIERVRQEVG 91
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-------VEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 172 DEPTSALDP---EMVKEVLDTMigLAQSGMTMLCVTHEMGFARTVADRVIFM--DRGEIVEQAAPD 232
Cdd:PRK11248 153 DEPFGALDAftrEQMQTLLLKL--WQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPLN 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-236 |
1.13e-36 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 129.27 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIE--RVRQEVGMVFQHFNLFpHLT 104
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVRDYTlaSLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLApiwVRKMPKKEAEDLAvhylervRIAeHAHKF----PG-----------QISGGQQQRVAIARSLCMKPKIM 169
Cdd:cd03251 92 VAENIAYG---RPGATREEVEEAA-------RAA-NAHEFimelPEgydtvigergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-236 |
1.16e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.74 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQ-FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEV 90
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQH--FNLFPhLTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-236 |
1.27e-36 |
|
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: 129.53 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedIRNIERVRQEV 90
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA--LADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFpHLTVLQNCTLAPiwvRKMPKKEAEDLAvhylervRIAEhAHKFPGQ---------------ISGGQQQR 155
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNIALAD---PGMSMERVIEAA-------KLAG-AHDFISElpegydtivgeqgagLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 156 VAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAqSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFF 235
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
.
gi 16131159 236 A 236
Cdd:cd03252 225 A 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
12-226 |
2.06e-36 |
|
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: 128.25 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNierVR 87
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE---AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPHLTVLQNCT-------LApiwvRKMPKKEAEDLAvhylERVRIAEHAHKFPGQISGGQQQRVAIAR 160
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEyfaglygLK----GDELTARLEELA----DRLGMEELLDRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-229 |
2.81e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 128.36 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL---NEDI 80
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 RNIERVrQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIAR 160
Cdd:PRK10584 82 RAKLRA-KHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 161 SLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDrGEIVEQA 229
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEEA 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-233 |
3.12e-36 |
|
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: 135.38 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVN-KWYGQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIER--VRQ 88
Cdd:TIGR03375 464 IEFRNVSfAYPGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGV----DIRQIDPadLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFpHLTVLQNCTLApiwvrkMPKKEAEDLavhyLERVRIA-------EHAHKFPGQI-------SGGQQQ 154
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG------APYADDEEI----LRAAELAgvtefvrRHPDGLDMQIgergrslSGGQRQ 608
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAqSGMTMLCVTHEMGFARTVaDRVIFMDRGEIVEQAAPDE 233
Cdd:TIGR03375 609 AVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQ 685
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-247 |
4.31e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 128.62 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILlqPAnamITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ-----QGRIVVDGIE 75
Cdd:PRK14258 1 MSKLI--PA---IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 76 LNEDIRNIERVRQEVGMVFQHFNLFPhLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERV----RIAEHAHKFPGQISGG 151
Cdd:PRK14258 76 IYERRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 152 QQQRVAIARSLCMKPKIMLFDEPTSALDP--EMVKEVLDTMIGLaQSGMTMLCVTHEMGFARTVADRVIFMDR-----GE 224
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRL-RSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQ 233
|
250 260
....*....|....*....|...
gi 16131159 225 IVEQAAPDEFFAHPKSERTRAFL 247
Cdd:PRK14258 234 LVEFGLTKKIFNSPHDSRTREYV 256
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-238 |
4.67e-36 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 128.28 E-value: 4.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHlEEHQ--QGRIVVDGIEL-NEDIRNIerv 86
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPtyGNDVRLFGERRgGEDVWEL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMV--FQHFNLFPHLTVLQ------NCTLApIWVRkmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAI 158
Cdd:COG1119 77 RKRIGLVspALQLRFPRDETVLDvvlsgfFDSIG-LYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSG-MTMLCVTH---EM--GFartvaDRVIFMDRGEIVEQAAPD 232
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPKE 228
|
250
....*....|....*
gi 16131159 233 E---------FFAHP 238
Cdd:COG1119 229 EvltsenlseAFGLP 243
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
13-236 |
5.02e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 135.08 E-value: 5.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNIERVRQEV 90
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHlTVLQN-CTLAPI-----W-----------VRKMPkkeaedLAVHYLervrIAEHAhkfpGQISGGQQ 153
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFENiAGGAPLtldeaWeaarmaglaedIRAMP------MGMHTV----ISEGG----GTLSGGQR 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 154 QRVAIARSLCMKPKIMLFDEPTSALD---PEMVKEVLDTMiglaqsGMTMLCVTHEMGfarTV--ADRVIFMDRGEIVEQ 228
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDnrtQAIVSESLERL------KVTRIVIAHRLS---TIrnADRIYVLDAGRVVQQ 665
|
....*...
gi 16131159 229 AAPDEFFA 236
Cdd:TIGR03797 666 GTYDELMA 673
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-243 |
6.68e-36 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 127.27 E-value: 6.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ERVRQE 89
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG----QDITKLpmhKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNcTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:cd03218 77 IGYLPQEASIFRKLTVEEN-ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERT 243
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-226 |
8.69e-36 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 125.74 E-value: 8.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 21 WYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCIN--HLEEHQQGRIVVDGIelNEDIRNIervRQEVGMVFQHFN 98
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR--PLDKRSF---RKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 LFPHLTVlqnctlapiwvrkmpkKEAEDLAVHylerVRiaehahkfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSAL 178
Cdd:cd03213 93 LHPTLTV----------------RETLMFAAK----LR----------GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131159 179 DPEMVKEVLDTMIGLAQSGMTMLCVTH----EMgFArtVADRVIFMDRGEIV 226
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHqpssEI-FE--LFDKLLLLSQGRVI 191
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
27-231 |
1.97e-35 |
|
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: 125.68 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNI--ERVRQEVGMVFQHFNLFPHlT 104
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV----DISKIglHDLRSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNctLAPIwvrkmpkKEAEDLAVH-YLERVRIAEHAHKFPGQI-----------SGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03244 94 IRSN--LDPF-------GEYSDEELWqALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 173 EPTSALDPE---MVKEVLDTMIglaqSGMTMLCVTHEMgfaRTVA--DRVIFMDRGEIVEQAAP 231
Cdd:cd03244 165 EATASVDPEtdaLIQKTIREAF----KDCTVLTIAHRL---DTIIdsDRILVLDKGRVVEFDSP 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-248 |
1.18e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 126.62 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIE-LNEDIRNIERVRQEVGMVFQ--HFNL 99
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDlLKADPEAQKLLRQKIQIVFQnpYGSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPHLTVLQncTLA-PIWVR-KMPKKEAEDLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTS 176
Cdd:PRK11308 106 NPRKKVGQ--ILEePLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 177 ALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLS 248
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-239 |
2.29e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 123.60 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFHVLKNINLTVQPGErIV-LCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI---ER 85
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----EDITHLpmhKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQHFNLFPHLTVLQNcTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:COG1137 76 ARLGIGYLPQEASIFRKLTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLcVT----HEmgfarT--VADRVIFMDRGEIVEQAAPDEFFAHPK 239
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVL-ITdhnvRE-----TlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
12-235 |
2.75e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.85 E-value: 2.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN--IE 84
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 85 RVRQEVGMVFQ--HFNLFPHlTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIA-EHAHKFPGQISGGQQQRVAIARS 161
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFF 235
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-248 |
3.20e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 123.74 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 16 ENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEE-----HQQGRIVVDGIELNE-DIRNIErVRQE 89
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYApDVDPVE-VRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHlTVLQNCTLAPiWVRKMpKKEAEDLAVHYLERVRIAEHAH---KFPGQ-ISGGQQQRVAIARSLCMK 165
Cdd:PRK14243 93 IGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKdklKQSGLsLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMGFARTVADRVIFMD---------RGEIVEQAAPDEFFA 236
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFN 248
|
250
....*....|..
gi 16131159 237 HPKSERTRAFLS 248
Cdd:PRK14243 249 SPQQQATRDYVS 260
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-220 |
3.98e-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: 3.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL---NEDIRniervRQ 88
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLadaDADSW-----RD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHlTVLQNCTLApiwvrkmpKKEAEDLAV-HYLERVRIAEHAHKFPGQI-----------SGGQQQRV 156
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLA--------RPDASDAEIrEALERAGLDEFVAALPQGLdtpigeggaglSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARtVADRVIFM 220
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
23-238 |
1.72e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.22 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVRQEVGMVFQHFN--LF 100
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE--NIREVRKFVGLVFQNPDdqIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 PHlTVLQNCTLAPIWVrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:PRK13652 93 SP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 181 EMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
13-236 |
3.91e-33 |
|
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: 126.78 E-value: 3.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ--FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedIRNIERVRQEV 90
Cdd:TIGR01846 456 ITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLA--IADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHlTVLQNCTLA-PiwvrKMPKKE---AEDLA-VH-YLERVR------IAEHAhkfpGQISGGQQQRVAI 158
Cdd:TIGR01846 534 GVVLQENVLFSR-SIRDNIALCnP----GAPFEHvihAAKLAgAHdFISELPqgynteVGEKG----ANLSGGQRQRIAI 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-211 |
4.21e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 119.92 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILLQpanamitLENVNKWY--GQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL 76
Cdd:PRK11629 1 MNKILLQ-------CDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 77 NE-------DIRNiervrQEVGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQIS 149
Cdd:PRK11629 74 SKlssaakaELRN-----QKLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 150 GGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFAR 211
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAK 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-226 |
8.23e-33 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 118.91 E-value: 8.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 18 VNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI-NHLEEHQ--QGRIVVDGIElnediRNIERVRQEVGMVF 94
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQP-----RKPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNLFPHLTVLQNCTLAPIWV--RKMP----KKEAEDLAvhyLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRlpRKSSdairKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMG---FarTVADRVIFMDRGEIV 226
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-228 |
9.69e-33 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 125.32 E-value: 9.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNkwygqFH------VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnED 79
Cdd:COG5265 351 LVVGGGEVRFENVS-----FGydperpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG----QD 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 80 IRNI--ERVRQEVGMVfqhfnlfPHLTVLQNCTLA-------PiwvrkmpkkEAEDLAVHylERVRIAeHAHKF----PG 146
Cdd:COG5265 422 IRDVtqASLRAAIGIV-------PQDTVLFNDTIAyniaygrP---------DASEEEVE--AAARAA-QIHDFieslPD 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 147 QI-----------SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHemgfaR--TV 213
Cdd:COG5265 483 GYdtrvgerglklSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAH-----RlsTI 556
|
250
....*....|....*..
gi 16131159 214 --ADRVIFMDRGEIVEQ 228
Cdd:COG5265 557 vdADEILVLEAGRIVER 573
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-251 |
1.60e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.41 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERVRQEVGMVFQH----FNlfP 101
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDsisaVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTV-------LQNCTlapiwvrKMPKKEAEDLAVHYLERVRIA-EHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK10419 105 RKTVreiirepLRHLL-------SLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 174 PTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAA--PDEFFAHPKSertRAFLSQV 250
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPvgDKLTFSSPAG---RVLQNAV 254
|
.
gi 16131159 251 I 251
Cdd:PRK10419 255 L 255
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-226 |
1.83e-32 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 118.05 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERVRQE 89
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLaPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-237 |
2.07e-32 |
|
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: 124.06 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRnI 83
Cdd:TIGR02203 324 IERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-ADYT-L 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHlTVLQNCTLAPIwvRKMPKKEAED-LAVHYLERV--RIAEHAHKFPGQ----ISGGQQQRV 156
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFND-TIANNIAYGRT--EQADRAEIERaLAAAYAQDFvdKLPLGLDTPIGEngvlLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEMGfarTV--ADRVIFMDRGEIVEQAAPDEF 234
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLS---TIekADRIVVMDDGRIVERGTHNEL 554
|
...
gi 16131159 235 FAH 237
Cdd:TIGR02203 555 LAR 557
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
30-238 |
6.40e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 6.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 30 NINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIRNIERVRQEVGMVFQHFNLFPHLTVLQNC 109
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQIARMGVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 110 TLA----------------PIWVRKmpKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK11300 102 LVAqhqqlktglfsgllktPAFRRA--ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 174 PTSALDPEMVKEvLDTMIGL--AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK11300 180 PAAGLNPKETKE-LDELIAElrNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-236 |
6.66e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 118.34 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 24 QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRN--IERVRQEVGMVFQhfnlFP 101
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTLAPIWVR----KMPKKEAEDLAVHYLERVRIAEHA-HKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTS 176
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 177 ALDPEMVKEVLdTMIGLAQ--SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK13646 175 GLDPQSKRQVM-RLLKSLQtdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-236 |
7.88e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.89 E-value: 7.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLEN-VNKWYGQFHV--LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERV 86
Cdd:PRK13642 2 NKILEVENlVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQH-FNLFPHLTVLQNCTLApIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-237 |
1.51e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 117.42 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIE--- 84
Cdd:PRK13645 7 IILDNVSYTYAkktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 85 RVRQEVGMVFQ--HFNLFPHlTVLQNCTLAPIWVRKmPKKEAEDLAVHYLERVRIA-EHAHKFPGQISGGQQQRVAIARS 161
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-250 |
1.93e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.89 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 24 QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERVRQEVGMVFQ--HFNLF 100
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQdpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 PHLTVlQNCTLAPIWVRKMPKKEAEDLAVHYL-ERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSAL 178
Cdd:PRK10261 416 PRQTV-GDSIMEPLRVHGLLPGKAAAARVAWLlERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 179 DPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-242 |
2.98e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 115.38 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDgielNEDIRNI---ERVR 87
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDISLLplhARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPHLTVLQNcTLAPIWVRK-MPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKP 166
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDN-LMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 167 KIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSER 242
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-233 |
3.82e-31 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 120.29 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY-----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIV-------VDGIELN 77
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 EDIRNieRVRQEVGMVFQHFNLFPHLTVLQNCTLApIWVrKMPKKEAEDLAVHYLERVRIAEHA-----HKFPGQISGGQ 152
Cdd:TIGR03269 357 PDGRG--RAKRYIGILHQEYDLYPHRTVLDNLTEA-IGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 153 QQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMI-GLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAP 231
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
..
gi 16131159 232 DE 233
Cdd:TIGR03269 513 EE 514
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
13-225 |
4.80e-31 |
|
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: 113.08 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNieRVRQEV 90
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN--ELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHlTVLQNCtlapiwvrkmpkkeaedlavhylervriaehahkfpgqISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFMDRGEI 225
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-205 |
4.94e-31 |
|
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: 119.77 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 21 WYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNieRVRQEVGMVFQHFNLF 100
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD--EVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 pHLTVLQNCTLApiwvrkmpKKEAEDLAVHY-LERVRIAEHAHKFPG-----------QISGGQQQRVAIARSLCMKPKI 168
Cdd:TIGR02868 422 -DTTVRENLRLA--------RPDATDEELWAaLERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGlAQSGMTMLCVTH 205
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-237 |
9.62e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.67 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRnieRVRQEV 90
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR---HARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLTVLQNCTlapIWVR--KMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLL---VFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-248 |
9.96e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 115.19 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 43 LCGPSGSGKSTTIRCINHLEE-----HQQGRIVVDGIELNeDIRNIERVRQEVGMVFQHFNLFPhLTVLQNcTLAPIWVR 117
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIF-NYRDVLEFRRRVGMLFQRPNPFP-MSIMDN-VLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 118 KM-PKKEAEDLAVHYLERV----RIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIG 192
Cdd:PRK14271 129 KLvPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 193 LAQSgMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLS 248
Cdd:PRK14271 209 LADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-251 |
2.67e-30 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 113.39 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINhleehqqGRIVVDGIELNEDIRN-------- 82
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA-------GRLAPDHGTATYIMRSgaelelyq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 ---IER---VRQEVGMVFQHFNLFPHLTVLQNCT----LAPIWVRKMPKKEAEdlAVHYLERVRI-AEHAHKFPGQISGG 151
Cdd:TIGR02323 75 lseAERrrlMRTEWGFVHQNPRDGLRMRVSAGANigerLMAIGARHYGNIRAT--AQDWLEEVEIdPTRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 152 QQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAA 230
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
250 260
....*....|....*....|.
gi 16131159 231 PDEFFAHPKSERTRAFLSQVI 251
Cdd:TIGR02323 233 TDQVLDDPQHPYTQLLVSSIL 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-233 |
3.19e-30 |
|
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: 117.60 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ--QGRIV-------------------- 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 71 -------------VDGIELNEDIRniERVRQEVGMVFQH-FNLFPHLTVLQNCtlapiwVRKMPK-----KEAEDLAVHY 131
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLR--RRIRKRIAIMLQRtFALYGDDTVLDNV------LEALEEigyegKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 132 LERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMI-GLAQSGMTMLCVTHEMGFA 210
Cdd:TIGR03269 153 IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|...
gi 16131159 211 RTVADRVIFMDRGEIVEQAAPDE 233
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDE 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-233 |
3.43e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.87 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE-DIRNIERV---- 86
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRlail 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEvgmvfQHFNL------------FPH----LTvlqnctlapiwvrkmpkkeAEDL-----AVHYLErvrIAEHAHKFP 145
Cdd:COG4604 81 RQE-----NHINSrltvrelvafgrFPYskgrLT-------------------AEDReiideAIAYLD---LEDLADRYL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:COG4604 134 DELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGR 213
|
....*....
gi 16131159 225 IVEQAAPDE 233
Cdd:COG4604 214 VVAQGTPEE 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-247 |
4.34e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.11 E-value: 4.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILLQPANAMITLENVNKwygQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHL-----EEHQQGRIVVDGIE 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQT---VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 76 -LNEDIRNIERVR-QEVGMVFQH--FNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRI---AEHAHKFPGQI 148
Cdd:PRK15134 78 lLHASEQTLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVE 227
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVE 237
|
250 260
....*....|....*....|
gi 16131159 228 QAAPDEFFAHPKSERTRAFL 247
Cdd:PRK15134 238 QNRAATLFSAPTHPYTQKLL 257
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-236 |
4.56e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.62 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNI 83
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD--YSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHlTVLQNCTLApiwvrkmpKKEAEDLA-VHYLERVRIAEHAHKFPG----------QISGGQ 152
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSA-TLRDNLLLA--------APNASDEAlIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 153 QQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHemgfaRTVA----DRVIFMDRGEIVEQ 228
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH-----RLTGleqfDRICVMDNGQIIEQ 554
|
....*...
gi 16131159 229 AAPDEFFA 236
Cdd:PRK11160 555 GTHQELLA 562
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
12-233 |
8.88e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYG-----QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDI------ 80
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVtklpey 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 ---RNIERVRQE--VGMvfqhfnlFPHLTVLQNCTLA------PIWVRKMPKKEAEdlavHYLERVRIA----EHAHKFP 145
Cdd:COG1101 77 kraKYIGRVFQDpmMGT-------APSMTIEENLALAyrrgkrRGLRRGLTKKRRE----LFRELLATLglglENRLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 -GQISGGQQQrvaiARSLCM----KPKIMLFDEPTSALDPEMVKEVLD-TMIGLAQSGMTMLCVTHEMGFARTVADRVIF 219
Cdd:COG1101 146 vGLLSGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIM 221
|
250
....*....|....
gi 16131159 220 MDRGEIVEQAAPDE 233
Cdd:COG1101 222 MHEGRIILDVSGEE 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-233 |
1.30e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY----------------------GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQG 67
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 68 RIVVDGielnedirnieRVRQ--EVGMVFQhfnlfPHLTVLQNCTL-APIWvrKMPKKEAEdlavhylERVR-IAEHA-- 141
Cdd:COG1134 82 RVEVNG-----------RVSAllELGAGFH-----PELTGRENIYLnGRLL--GLSRKEID-------EKFDeIVEFAel 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 142 HKF---P-GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRV 217
Cdd:COG1134 137 GDFidqPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|....*.
gi 16131159 218 IFMDRGEIVEQAAPDE 233
Cdd:COG1134 217 IWLEKGRLVMDGDPEE 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-238 |
1.55e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERV--RQEVGMVFQHFNLFPHlT 104
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG----VPLVQYDHHylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLApiwVRKMPKKEAEDLAVhylervriAEHAHKFPG---------------QISGGQQQRVAIARSLCMKPKIM 169
Cdd:TIGR00958 571 VRENIAYG---LTDTPDEEIMAAAK--------AANAHDFIMefpngydtevgekgsQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMiglAQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:TIGR00958 640 ILDEATSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-250 |
1.60e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.11 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWY----GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG---------- 73
Cdd:PRK10261 8 DARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 74 IELNE-DIRNIERVR-QEVGMVFQH--FNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHA---HKFPG 146
Cdd:PRK10261 88 IELSEqSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 147 QISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDtMIGLAQSGMTM--LCVTHEMGFARTVADRVIFMDRGE 224
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMSMgvIFITHDMGVVAEIADRVLVMYQGE 246
|
250 260
....*....|....*....|....*.
gi 16131159 225 IVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-237 |
2.03e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIER--VRQE 89
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVTRasLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHlTVLQNctlapIWVRKMPKKEAEdlavhYLERVRIAEhAHKF---------------PGQISGGQQQ 154
Cdd:PRK13657 411 IAVVFQDAGLFNR-SIEDN-----IRVGRPDATDEE-----MRAAAERAQ-AHDFierkpdgydtvvgerGRQLSGGERQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEM---VKEVLDTMiglaQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAP 231
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETeakVKAALDEL----MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSF 553
|
....*.
gi 16131159 232 DEFFAH 237
Cdd:PRK13657 554 DELVAR 559
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-226 |
2.14e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 110.35 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRNIERVRQE 89
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAedlavhyLERV-----RIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQER-------IKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-250 |
2.21e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.49 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL----NEDIRNierVRQEVGMVFQH--FNLFPHLT 104
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRA---VRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 V-------LQncTLAPiwvrKMPKKEAED------LAVHYLERVrIAEHAHKFpgqiSGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PRK15079 117 IgeiiaepLR--TYHP----KLSRQEVKDrvkammLKVGLLPNL-INRYPHEF----SGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-250 |
2.29e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.79 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQFHVLKNINLTVQPGEriVLC--GPSGSGKSTTIRCINHLEEHQQGRI--------VVDGIELN 77
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGE--VLGivGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 EDIRnieR--VRQEVGMVFQHF--NLFPHLTVLQNctlapIWVRKMPKKE-----AEDLAVHYLERVRI-AEHAHKFPGQ 147
Cdd:PRK11701 80 EAER---RrlLRTEWGFVHQHPrdGLRMQVSAGGN-----IGERLMAVGArhygdIRATAGDWLERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 148 ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....
gi 16131159 227 EQAAPDEFFAHPKSERTRAFLSQV 250
Cdd:PRK11701 232 ESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-227 |
9.35e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 9.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVdGielnedirniERVRqeVG 91
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G----------ETVK--IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHF-NLFPHLTVLQnctlapiWVRKMPKKEAEDLAVHYLERVRIA-EHAHKFPGQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG0488 382 YFDQHQeELDPDKTVLD-------ELRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 170 LFDEPTSALDPEMvKEVLDTmiGLAQ-SGmTMLCVTHEMGFARTVADRVIFMDRGEIVE 227
Cdd:COG0488 455 LLDEPTNHLDIET-LEALEE--ALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
15-225 |
9.92e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 9.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielneDIRniervrqeVGMVF 94
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----GLR--------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNLFPHLTVLQNCT--LAPIW---------VRKMPKKEAE-----DLAVHY---------------LERVRIAEHAHK 143
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgDAELRaleaeleelEAKLAEPDEDlerlaELQEEFealggweaearaeeiLSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 144 FP-GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVkEVLDTMigLAQSGMTMLCVTHEMGFARTVADRVIFMDR 222
Cdd:COG0488 148 RPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLEEF--LKNYPGTVLVVSHDRYFLDRVATRILELDR 224
|
...
gi 16131159 223 GEI 225
Cdd:COG0488 225 GKL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-234 |
1.53e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGErIV-LCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNI-ERVRQevGMVF-----QHFN 98
Cdd:COG1129 266 GVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPV--RIRSPrDAIRA--GIAYvpedrKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 LFPHLTVLQNCTLAPI-------WVRkmPKKEAEdLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:COG1129 341 LVLDLSIRENITLASLdrlsrggLLD--RRRERA-LAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 171 FDEPTSALDpemV---KEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:COG1129 418 LDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
13-228 |
1.85e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 106.24 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYG--QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIervRQEV 90
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---SSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFpHLTVLQNCTLapiwvrkmpkkeaedlavhylervriaehahkfpgQISGGQQQRVAIARSLCMKPKIML 170
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQsGMTMLCVTHEM-GFARtvADRVIFMDRGEIVEQ 228
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLtGIEH--MDKILFLENGKIIMQ 177
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-251 |
2.96e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 112.45 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKSTTIrciNHLEEHQQGRIVVDG-IELNEDIRNIERVRQEVGMVFQHFNLFPHLT 104
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLA-----PiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQ------ISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:TIGR00955 116 VREHLMFQahlrmP---RRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH-------EMgFartvaDRVIFMDRGEIVEQAAPDE---FFAH-----P 238
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPDQavpFFSDlghpcP 266
|
250
....*....|...
gi 16131159 239 KSERTRAFLSQVI 251
Cdd:TIGR00955 267 ENYNPADFYVQVL 279
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-233 |
2.07e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.61 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRnieRVRQ 88
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR---LARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLAPIWVRkMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK13536 115 RIGVVPQFDNLDLEFTVRENLLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
13-224 |
4.93e-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: 101.76 E-value: 4.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIvvdgielnedirniervrqevgm 92
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 vfqhfnlfphlTVLQNCTLApiwvrkmpkkeaedlavhYLErvriaehahkfpgQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03221 58 -----------TWGSTVKIG------------------YFE-------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQsgmTMLCVTHEMGFARTVADRVIFMDRGE 224
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-218 |
1.41e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.93 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 22 YGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnedirniervRQEVGMVFQHFNL-- 99
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 -FPhLTVLQNCTLApIWVRKMP----KKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEP 174
Cdd:NF040873 69 sLP-LTVRDLVAMG-RWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131159 175 TSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVI 218
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-247 |
1.54e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.82 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQ----FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQqGRIVVDGIELN-EDIRNI-E 84
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNgQDLQRIsE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 85 RVRQ-----EVGMVFQH--FNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHK---FPGQISGGQQQ 154
Cdd:PRK11022 81 KERRnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....
gi 16131159 234 FFAHPKSERTRAFL 247
Cdd:PRK11022 241 IFRAPRHPYTQALL 254
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-240 |
1.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVR 87
Cdd:PRK13648 5 NSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD--NFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQH-FNLFPHLTV-------LQNctlapiwvRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIA 159
Cdd:PRK13648 83 KHIGIVFQNpDNQFVGSIVkydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGL-AQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
..
gi 16131159 239 KS 240
Cdd:PRK13648 234 EE 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-228 |
3.43e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.47 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIrciNHLEEH--QQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFNLFpHLTV 105
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFlpYQGSLKINGIELRE--LDPESWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCTLApiwvrkmpKKEAEDLAVHY-LERVRIAEHAHKFP-----------GQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK11174 440 RDNVLLG--------NPDASDEQLQQaLENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLcVTHEMGFARTVaDRVIFMDRGEIVEQ 228
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQDGQIVQQ 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-206 |
4.32e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI-- 83
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG----EDISTLkp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHlTVLQNCTLaPIWVRKM---PKKEAEDLAvhyleRVRIAEHA-HKFPGQISGGQQQRVAIA 159
Cdd:PRK10247 77 EIYRQQVSYCAQTPTLFGD-TVYDNLIF-PWQIRNQqpdPAIFLDDLE-----RFALPDTIlTKNIAELSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLA-QSGMTMLCVTHE 206
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
12-238 |
7.55e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.42 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLeNVNKWYGQFHVlkNINLTVqPGERIV-LCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNI----ERV 86
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTL-PAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RqeVGMVFQHFNLFPHLTVLQNCTLApiwvrkMPKKEAED-------LAV-HYLERvriaehahkFPGQISGGQQQRVAI 158
Cdd:PRK11144 77 R--IGYVFQDARLFPHYKVRGNLRYG------MAKSMVAQfdkivalLGIePLLDR---------YPGSLSGGEKQRVAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 159 ARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK11144 140 GRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
.
gi 16131159 238 P 238
Cdd:PRK11144 220 S 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
27-225 |
7.62e-26 |
|
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: 101.01 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFNLFPHlTVL 106
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTLAPIWVRKMPKKEAEDLAvhylervriaeHAHKF---------------PGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKA-----------HAHSFiselasgydtevgekGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSgMTMLCVTHEMgfaRTV--ADRVIFMDRGEI 225
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPER-RTVLVIAHRL---STVerADQILVLDGGRI 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
12-250 |
7.62e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-------------- 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmlssrqlarrlall 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 -------EDIRnierVRQEVGmvfqhFNLFPHLTvlqnctlapIWVRKMPKKEAedLAVHYLERVRIAEHAHKFPGQISG 150
Cdd:PRK11231 82 pqhhltpEGIT----VRELVA-----YGRSPWLS---------LWGRLSAEDNA--RVNQAMEQTRINHLADRRLTDLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 151 GQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAA 230
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
250 260
....*....|....*....|
gi 16131159 231 PDEFFahpkserTRAFLSQV 250
Cdd:PRK11231 222 PEEVM-------TPGLLRTV 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-252 |
1.02e-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: 105.21 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIER--VRQEVGMVFQHFNLF---- 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF----SLKDIDRhtLRQFINYLPQEPYIFsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 ---------PHLT---VLQNCTLAPIwvrkmpKKEAEDLAVHYleRVRIAEHAhkfpGQISGGQQQRVAIARSLCMKPKI 168
Cdd:TIGR01193 565 lenlllgakENVSqdeIWAACEIAEI------KDDIENMPLGY--QTELSEEG----SSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSgmTMLCVTHEMGFARTVaDRVIFMDRGEIVEQAAPDEFFAHpksertRAFLS 248
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDR------NGFYA 703
|
....
gi 16131159 249 QVIH 252
Cdd:TIGR01193 704 SLIH 707
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
16-233 |
1.99e-25 |
|
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: 99.78 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 16 ENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-EDIRNIervrqevGMVF 94
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKI-------GSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNLFPHLTVLQN----CTLapiwvRKMPKKEAEDLavhyLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIML 170
Cdd:TIGR03740 77 ESPPLYENLTARENlkvhTTL-----LGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
29-248 |
2.11e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 100.54 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 29 KNINLTVQPGERIVLCGPSGSGKSTTirCINHLE------EHQQGRIVVDGIELN-EDIRNIERVrqevgmvfqhfnlfp 101
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLT--CAAALGilpagvRQTAGRVLLDGKPVApCALRGRKIA--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 hlTVLQNCTLAPIWVRKMP-----------KKEAEDLAVHYLERVRIAEHA---HKFPGQISGGQQQRVAIARSLCMKPK 167
Cdd:PRK10418 83 --TIMQNPRSAFNPLHTMHtharetclalgKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRAF 246
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSL 240
|
..
gi 16131159 247 LS 248
Cdd:PRK10418 241 VS 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-231 |
3.21e-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: 98.64 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQF--HVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNI-- 83
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIpl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFPHlTVLQNCTlapiwvrkmPKKEAEDlaVHYLERVRIAEHAHKFpgqiSGGQQQRVAIARSLC 163
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSG-TIRSNLD---------PFDEYSD--EEIYGALRVSEGGLNL----SQGQRQLLCLARALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 164 MKPKIMLFDEPTSALDPEMVKEVLDTmIGLAQSGMTMLCVTHEMgfaRTVA--DRVIFMDRGEIVEQAAP 231
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKT-IREEFTNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-225 |
3.27e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 97.89 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDiRNIERVRQEVGMV---FQHFNLFPHL 103
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR-SPRDAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 TVLQNCTLApiwvrkmpkkeaedlavHYLervriaehahkfpgqiSGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMV 183
Cdd:cd03215 94 SVAENIALS-----------------SLL----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131159 184 KEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-237 |
4.13e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 103.56 E-value: 4.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNKWY-GQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNI 83
Cdd:PRK11176 335 IERAKGDIEFRNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD--YTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERVRQEVGMVFQHFNLFpHLTVLQNCTLAP--IWVRKMPKKEAEdlAVHYLERVRIAEHA-HKFPGQ----ISGGQQQRV 156
Cdd:PRK11176 413 ASLRNQVALVSQNVHLF-NDTIANNIAYARteQYSREQIEEAAR--MAYAMDFINKMDNGlDTVIGEngvlLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPE---MVKEVLDTMiglaQSGMTMLCVTHEMGfarTV--ADRVIFMDRGEIVEQAAP 231
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTEserAIQAALDEL----QKNRTSLVIAHRLS---TIekADEILVVEDGEIVERGTH 562
|
....*.
gi 16131159 232 DEFFAH 237
Cdd:PRK11176 563 AELLAQ 568
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-248 |
6.14e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.48 E-value: 6.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 5 LLQPANAMITLENVNKWYGQFHV--LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRN 82
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL--HFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 IERVRQEVGMVFQ--HFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIA 159
Cdd:PRK15112 82 YSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
250
....*....|
gi 16131159 239 KSERTRAFLS 248
Cdd:PRK15112 242 LHELTKRLIA 251
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-227 |
2.84e-24 |
|
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: 96.06 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ--QGRIVVDGielnEDIRNI---ERVR 87
Cdd:cd03217 1 LEIKDLHVsvGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKG----EDITDLppeERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNLFPHLTVLqnctlapiwvrkmpkkeaedlavHYLERVRIaehahKFpgqiSGGQQQRVAIARSLCMKPK 167
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNA-----------------------DFLRYVNE-----GF----SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH-EMGFARTVADRVIFMDRGEIVE 227
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVK 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-238 |
3.77e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 30 NINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEhQQGRI----VVDGIE-LNEDIRNIERVR-QEVGMVFQH--FNLFP 101
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsaTFNGREiLNLPEKELNKLRaEQISMIFQDpmTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEhAHK----FPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSA 177
Cdd:PRK09473 113 YMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 178 LDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-237 |
5.57e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.21 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIelneDIRNIERVR--QEVGMVFQHFNLFPHlT 104
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGA----DLSQWDREElgRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNctlapiwVRKMPkkEAEDLAVhyLERVRIAeHAH----KFP-----------GQISGGQQQRVAIARSLCMKPKIM 169
Cdd:COG4618 422 IAEN-------IARFG--DADPEKV--VAAAKLA-GVHemilRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 170 LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARtVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-226 |
1.90e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIErVRQEVG 91
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLA-AQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPIWVRK------MPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMK 165
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-233 |
2.57e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 16 ENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNI--ERVRQEVGMV 93
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG----EHIQHYasKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 94 FQHFNLFPHLTVLQNCTLA-----PIWVRKmpKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK10253 87 AQNATTPGDITVQELVARGryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-236 |
5.31e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 22 YGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGMVFQHfnlfP 101
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTLAPIW--VRKMPKKEAE-----DLAVHYLErvriAEHAHKFPGQ-ISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK13638 87 EQQIFYTDIDSDIAfsLRNLGVPEAEitrrvDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFA 236
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-247 |
6.18e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.06 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 7 QPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIER- 85
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----ENIPAMSRs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 ----VRQEVGMVFQHFNLFPHLTVLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:PRK11831 78 rlytVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPeMVKEVLDTMIGLAQS--GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPk 239
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDP-ITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP- 235
|
....*...
gi 16131159 240 SERTRAFL 247
Cdd:PRK11831 236 DPRVRQFL 243
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-233 |
1.16e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIEL-NEDIRNIER----V 86
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRrvasV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVGMVFQhFNL--------FPHLTvlqnctlapiwvRKMPKKEAEDLAV-HYLERVRIAEHAHKFPGQISGGQQQRVA 157
Cdd:PRK09536 83 PQDTSLSFE-FDVrqvvemgrTPHRS------------RFDTWTETDRAAVeRAMERTGVAQFADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 158 IARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-227 |
2.82e-22 |
|
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: 91.44 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWY----------------------GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIV 70
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 71 VDGielnedirnieRVRQ--EVGMVFQhfnlfPHLTVLQN----CTLAPIWVRKMPKKEAE-----DLAVHYLERVRiae 139
Cdd:cd03220 81 VRG-----------RVSSllGLGGGFN-----PELTGRENiylnGRLLGLSRKEIDEKIDEiiefsELGDFIDLPVK--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 140 hahkfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIF 219
Cdd:cd03220 142 -------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALV 214
|
....*...
gi 16131159 220 MDRGEIVE 227
Cdd:cd03220 215 LEKGKIRF 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
23-237 |
3.53e-22 |
|
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: 94.72 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRniERVRQEVGMVFQHFNLFPH 102
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--ETFGKHIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 lTVLQNctLAPIWVRKMPKK--EAEDLA-VHYLervrIAehahKFP-----------GQISGGQQQRVAIARSLCMKPKI 168
Cdd:TIGR01842 407 -TVAEN--IARFGENADPEKiiEAAKLAgVHEL----IL----RLPdgydtvigpggATLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 169 MLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGfARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
27-224 |
8.02e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 89.45 E-value: 8.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCInhLEE--HQQGRIVVDG----------IeLNEDIR-NI--------ER 85
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEleKLSGSVSVPGsiayvsqepwI-QNGTIReNIlfgkpfdeER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQevgmvfqhfnlfphltVLQNCTLAPiwvrkmpkkeaeDLAVhylervriaehahkFPGQI-----------SGGQQQ 154
Cdd:cd03250 97 YEK----------------VIKACALEP------------DLEI--------------LPDGDlteigekginlSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMI-GLAQSGMTMLCVTHEMGFARTvADRVIFMDRGE 224
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-217 |
1.30e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.07 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 1 MSQILLQpanamitLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEH--QQGRIVVDGIELN- 77
Cdd:PRK13549 1 MMEYLLE-------MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 78 EDIRNIERvrQEVGMVFQHFNLFPHLTVLQNCTLAPIWVR-------KMpKKEAEDLavhyLERVRIAEHAHKFPGQISG 150
Cdd:PRK13549 74 SNIRDTER--AGIAIIHQELALVKELSVLENIFLGNEITPggimdydAM-YLRAQKL----LAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 151 GQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRV 217
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-226 |
2.31e-21 |
|
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: 92.58 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEH--QQGRIVVDGIELN-EDIRNIERvrQ 88
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKaSNIRDTER--A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 EVGMVFQHFNLFPHLTVLQNCTLAPIWVRK---MPKKEAEDLAVHYLERVRIAEHAHKFP-GQISGGQQQRVAIARSLCM 164
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNEITLPggrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-205 |
2.34e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 92.56 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVV-DGIELnedirniervrqevgmvfqhfnLF----P 101
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLqncTLA-----PIWVRKMPKKEAEDLavhyLERVRIAEHAHKFP-----GQI-SGGQQQRVAIARSLCMKPKIML 170
Cdd:COG4178 436 YLPLG---TLReallyPATAEAFSDAELREA----LEAVGLGHLAERLDeeadwDQVlSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*
gi 16131159 171 FDEPTSALDPEMVKEVLdTMIGLAQSGMTMLCVTH 205
Cdd:COG4178 509 LDEATSALDEENEAALY-QLLREELPGTTVISVGH 542
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-227 |
5.16e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.40 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI--NHLEEHQQGRIVVDGIELNEDIRNI 83
Cdd:COG2401 24 SERVAIVLEAFGVELrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 84 ERV--RQEVGMVFQhfnlfphltVLQNCTL--APIWVRKmpkkeaedlavhylervriaehahkfPGQISGGQQQRVAIA 159
Cdd:COG2401 104 DAIgrKGDFKDAVE---------LLNAVGLsdAVLWLRR--------------------------FKELSTGQKFRFRLA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVA-DRVIFMDRGEIVE 227
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-206 |
9.28e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 88.01 E-value: 9.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCInhleehqQGRI---VVDGIELNEDIRNIERVRQEVGMVFQHFNLFPHL 103
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIqgnNFTGTILANNRKPTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 TVLQncTLAPIWVRKMPKKEAEDLAVHYLERVrIAEHA----------HKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PLN03211 156 TVRE--TLVFCSLLRLPKSLTKQEKILVAESV-ISELGltkcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|...
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHE 206
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-231 |
2.77e-19 |
|
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: 86.99 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIR-NIERVRQEVGMVFQHFNLFPHLTVLQNC 109
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIEtNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 110 TL-----APIWVRKMPKKEA--EDLAVHYlervRIAEHAHkfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:TIGR01257 1025 LFyaqlkGRSWEEAQLEMEAmlEDTGLHH----KRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16131159 183 VKEVLDTMIGLaQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAP 231
Cdd:TIGR01257 1097 RRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-239 |
3.10e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.62 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRcinhleehqqgriVVDGIeLNEDIRNIERVRQ-EV 90
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR-------------VVLGL-VAPDEGVIKRNGKlRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPH--LTVLQNCTLAPiwvrkmPKKEAEDLAVhyLERVRiAEHAHKFPGQ-ISGGQQQRVAIARSLCMKPK 167
Cdd:PRK09544 70 GYVPQKLYLDTTlpLTVNRFLRLRP------GTKKEDILPA--LKRVQ-AGHLIDAPMQkLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRgEIVEQAAPDEFFAHPK 239
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPE 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-205 |
4.20e-19 |
|
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: 81.43 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIvvdGIELNEDIrniervrqevgmvfqhfnLFphltvl 106
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDL------------------LF------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 qnctlapiwvrkMPKKEaedlavhYLERVRIAEhahkfpgQI--------SGGQQQRVAIARSLCMKPKIMLFDEPTSAL 178
Cdd:cd03223 69 ------------LPQRP-------YLPLGTLRE-------QLiypwddvlSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*..
gi 16131159 179 DPEMVKEVLDTmigLAQSGMTMLCVTH 205
Cdd:cd03223 123 DEESEDRLYQL---LKELGITVISVGH 146
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-247 |
5.30e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.57 E-value: 5.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI-NHLEEHQQ---GRIVVDGIEL----NEDIRNIerVRQEVGMVF 94
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDNWHvtaDRFRWNGIDLlklsPRERRKI--IGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFN--LFPHLTVLQ-------NCTL-APIWVRKMPKKEAedlAVHYLERVRIAEHAH---KFPGQISGGQQQRVAIARS 161
Cdd:COG4170 96 QEPSscLDPSAKIGDqlieaipSWTFkGKWWQRFKWRKKR---AIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHH 252
|
....*..
gi 16131159 241 ERTRAFL 247
Cdd:COG4170 253 PYTKALL 259
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
27-227 |
6.44e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKST---TIrcINHlEEHQ--QGRIVVDGielnEDIRNI---ERVRQEVGMVFQHFN 98
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTlakVL--MGH-PKYEvtSGSILLDG----EDILELspdERARAGIFLAFQYPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 LFPHLTVLQNCTLAPIWVR--KMPKKEAEDLAVHYLERVRIAE-HAHK-----FpgqiSGGQQQRVAIARSLCMKPKIML 170
Cdd:COG0396 88 EIPGVSVSNFLRTALNARRgeELSAREFLKLLKEKMKELGLDEdFLDRyvnegF----SGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHemgFAR----TVADRVIFMDRGEIVE 227
Cdd:COG0396 164 LDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
27-205 |
6.78e-19 |
|
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: 81.64 E-value: 6.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdirnIERVRQEVGMVFQHFN-LFPHLTV 105
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE----QRDEPHENILYLGHLPgLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCT-LAPIwvrkmpkKEAEDLAVH-YLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMV 183
Cdd:TIGR01189 91 LENLHfWAAI-------HGGAQRTIEdALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|..
gi 16131159 184 KEVLDTMIGLAQSGMTMLCVTH 205
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-227 |
1.23e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.64 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQ--FHVlKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNIERVRQEV 90
Cdd:PRK10522 323 LELRNVTFAYQDngFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV--TAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFNLFPHLtvlqnctLAPiwvrkmPKKEAEDLAV-HYLERVRIAEHAHKFPGQI-----SGGQQQRVAIARSLCM 164
Cdd:PRK10522 400 SAVFTDFHLFDQL-------LGP------EGKPANPALVeKWLERLKMAHKLELEDGRIsnlklSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQ-SGMTMLCVTH-EMGFARtvADRVIFMDRGEIVE 227
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQeMGKTIFAISHdDHYFIH--ADRLLEMRNGQLSE 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-233 |
1.27e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 24 QFHV---LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEhQQGRIVVDGIELNE-DIRNIERVRqevGMVFQHFNL 99
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwSAAELARHR---AYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPHLTVLQNCTLApiwVRKMPKKEAEDLAVHYL-ERVRIAEHAHKFPGQISGGQQQRVAIARSLCM-------KPKIMLF 171
Cdd:COG4138 81 PFAMPVFQYLALH---QPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 172 DEPTSALDpemV--KEVLDTMIG-LAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG4138 158 DEPMNSLD---VaqQAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-205 |
1.78e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGiELNEDIRNIERVRQeVGmvfqHFN-LFPHLTV 105
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-GDIDDPDVAEACHY-LG----HRNaMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCTLapiWVRKmpkKEAEDLAVH-YLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVK 184
Cdd:PRK13539 91 AENLEF---WAAF---LGGEELDIAaALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 16131159 185 EVLDTMIG-LAQSGMtMLCVTH 205
Cdd:PRK13539 165 LFAELIRAhLAQGGI-VIAATH 185
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-226 |
4.67e-18 |
|
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: 80.45 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 18 VNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQeVGMVF-QH 96
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK--RRKKFLRR-IGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 97 FNLFPHLTVLQNCTL-APIWvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPT 175
Cdd:cd03267 104 TQLWWDLPVIDSFYLlAAIY--DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131159 176 SALD---PEMVKEVLDTMIglAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:cd03267 182 IGLDvvaQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-227 |
6.09e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 29 KNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-----EDIRN----IERVRQEVGmvfqhfnL 99
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKgmayITESRRDNG-------F 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPHLTVLQNCTLAP------------IWVRKMPKKEAEDlavhylERVRIAEHAHKFP---GQISGGQQQRVAIARSLCM 164
Cdd:PRK09700 353 FPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAEN------QRELLALKCHSVNqniTELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 165 KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVE 227
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-224 |
1.66e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.13 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVNKWY-GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVvdgieLNEDIRniervrqeVGM 92
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGIK--------VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQHFNLFPHLTVLQNCTLAPIWVRKM-------------PKKEAEDLA--------------VHYLER-VRIAEHAHKF 144
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGVAEIKDAldrfneisakyaePDADFDKLAaeqaelqeiidaadAWDLDSqLEIAMDALRC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 145 P------GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVkEVLDTMigLAQSGMTMLCVTHEMGFARTVADRVI 218
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERH--LQEYPGTVVAVTHDRYFLDNVAGWIL 229
|
....*.
gi 16131159 219 FMDRGE 224
Cdd:TIGR03719 230 ELDRGR 235
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
28-217 |
2.35e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.60 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEH--QQGRIVVDGIELN-EDIRNIERVrqevGMVF--QHFNLFPH 102
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRfKDIRDSEAL----GIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTVLQNctlapIWVRKMPKK-------EAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPT 175
Cdd:NF040905 93 LSIAEN-----IFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16131159 176 SALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRV 217
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-238 |
2.55e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.91 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNeDIRnIERVRQEVGMVFQHFNLFPHlTVL 106
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQ-LDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQ----ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 183 VKEVLDTmigLAQ--SGMTMLCVTHEMGfARTVADRVIFMDRGEIVEQAAPDEFFAHP 238
Cdd:PRK10789 487 EHQILHN---LRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-242 |
6.69e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 9 ANAMITLENVNKWYGQFHV-LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRniervR 87
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-----K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFNL---FPHLT---VLQNCTLAPIWVRKmPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARS 161
Cdd:PRK15056 78 NLVAYVPQSEEVdwsFPVLVedvVMMGRYGHMGWLRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIfMDRGEIVEQAAPDEFFAHPKSE 241
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLE 235
|
.
gi 16131159 242 R 242
Cdd:PRK15056 236 L 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-236 |
1.03e-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: 79.22 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnEDIrNIERVRQEVGMVFQHFNLFP----- 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-AKI-GLHDLRFKITIIPQDPVLFSgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTLAPIWVrkmpkkeAEDLAvhylervriaeHAHKF----PGQI-----------SGGQQQRVAIARSLCMKP 166
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWW-------ALELA-----------HLKTFvsalPDKLdhecaeggenlSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 167 KIMLFDEPTSALDPEmVKEVLDTMIGLAQSGMTMLCVTHEMgfaRTVAD--RVIFMDRGEIVEQAAPDEFFA 236
Cdd:TIGR00957 1441 KILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-217 |
1.24e-16 |
|
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: 75.61 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIERVRQEVGmvfqHFN-LFPHLTV 105
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG----HAPgIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LQNCTlapiWVRKMPKKEAEDLAvhyLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKE 185
Cdd:cd03231 91 LENLR----FWHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 16131159 186 VLDTMIG-LAQSGMTMLCVTHEMGFARTVADRV 217
Cdd:cd03231 164 FAEAMAGhCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-225 |
1.37e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.71 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 30 NINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ-QGRIVVDGIELneDIRN-IERVRQEVGMV---FQHFNLFPHLT 104
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV--DIRNpAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLAPI--WVRKMPKKEAEDLAV--HYLERVRIAEHAHKFP-GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:TIGR02633 356 VGKNITLSVLksFCFKMRIDAAAELQIigSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-227 |
2.09e-16 |
|
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: 77.92 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDirNIERVRQEVGMVFQHFNLFPHLTVLQNCT 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NREAYRQLFSAVFSDFHLFDRLLGLDGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 111 LapiwvrkmpkkeaEDLAVHYLERVRIaehAHKFP---GQI-----SGGQQQRVA-IARSLCMKPkIMLFDEPTSALDP- 180
Cdd:COG4615 429 D-------------PARARELLERLEL---DHKVSvedGRFsttdlSQGQRKRLAlLVALLEDRP-ILVFDEWAADQDPe 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 181 -------EMVKEvldtmigLAQSGMTMLCVTH-EMGFArtVADRVIFMDRGEIVE 227
Cdd:COG4615 492 frrvfytELLPE-------LKARGKTVIAISHdDRYFD--LADRVLKMDYGKLVE 537
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-234 |
2.56e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedirNIERVR-QEV 90
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA----RLTPAKaHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 G--MVFQHFNLFPHLTVLQNctlapIWVRkMPKKEAEDLAVHYLervrIAEHAHKFPGQISGG-----QQQRVAIARSLC 163
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKEN-----ILFG-LPKRQASMQKMKQL----LAALGCQLDLDSSAGslevaDRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 164 MKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-240 |
2.73e-16 |
|
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: 75.72 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQ---------HF 97
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--LPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 98 NLFPHLTvlqnCTLAPIWvrkmpkkEAedlavhyLERVRIAEHAHKFPG-----------QISGGQQQRVAIARSLCMKP 166
Cdd:cd03288 114 NLDPECK----CTDDRLW-------EA-------LEIAQLKNMVKSLPGgldavvteggeNFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 167 KIMLFDEPTSALDpeMVKE-VLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:cd03288 176 SILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-228 |
2.82e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.84 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFH-VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIerVRQEVG 91
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQH-----FNLFPHLTVLQNCTLAPIWvrkmpkkeaedlavHYLERVRIAEHAHKFPGQI-----------SGGQQQR 155
Cdd:PRK10790 419 MVQQDpvvlaDTFLANVTLGRDISEEQVW--------------QALETVQLAELARSLPDGLytplgeqgnnlSVGQKQL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 156 VAIARSLCMKPKIMLFDEPTSALDpEMVKEVLDTMIGLAQSGMTMLCVTHEMGfarTV--ADRVIFMDRGEIVEQ 228
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANID-SGTEQAIQQALAAVREHTTLVVIAHRLS---TIveADTILVLHRGQAVEQ 555
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-207 |
6.13e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 76.69 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNiERVRQEVGMVF 94
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK-EALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNLFPHLTVLQNctlapIWVRKMPKKEA---------------EDLAVHYLERVRIAEhahkfpgqISGGQQQRVAIA 159
Cdd:PRK10982 80 QELNLVLQRSVMDN-----MWLGRYPTKGMfvdqdkmyrdtkaifDELDIDIDPRAKVAT--------LSVSQMQMIEIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEM 207
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKM 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-226 |
6.63e-16 |
|
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: 73.84 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCI-NHLEEHQQ--GRIVVDGIELNEdirNIERVRQEVGMVFQHFNLFPHLT 104
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPYKE---FAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQncTLapiwvrkmpkkeaeDLAVhyleRVRiaehAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVK 184
Cdd:cd03233 100 VRE--TL--------------DFAL----RCK----GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16131159 185 EVLdtmiglaqsgMTMLCVTHEMGFARTVA------------DRVIFMDRGEIV 226
Cdd:cd03233 156 EIL----------KCIRTMADVLKTTTFVSlyqasdeiydlfDKVLVLYEGRQI 199
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-247 |
6.71e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 75.61 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 23 GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEhQQGRIVVDGIELNE-DIRNI---ER---VRQEVGMVFQ 95
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDiDLLRLsprERrklVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 96 HFN--LFPHLTVLQNCTLA-PIWVRKMP--------KKEAEDLavhyLERVRIAEH---AHKFPGQISGGQQQRVAIARS 161
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNiPGWTYKGRwwqrfgwrKRRAIEL----LHRVGIKDHkdaMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQ-SGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHH 252
|
....*..
gi 16131159 241 ERTRAFL 247
Cdd:PRK15093 253 PYTQALI 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-225 |
8.64e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 29 KNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIrniERVRQEVGMVF-----QHFNLFPHL 103
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS---TAQRLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 104 TVLQN-CTLA----PIWVRkmPKKEAedlAVhyLERVRIA-----EHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK15439 357 PLAWNvCALThnrrGFWIK--PAREN---AV--LERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-223 |
8.80e-16 |
|
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: 76.59 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 35 VQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELnedIRNIERVRQEVGMVFQhFNLFPHLTVLQNCTLAPI 114
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISDVHQNMGYCPQ-FDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 115 WVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLA 194
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 16131159 195 QSGMTMLCVTHEMGFARTVADRVIFMDRG 223
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-232 |
1.42e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNediRNIERVRQE- 89
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT---FNGPKSSQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 -VGMVFQHFNLFPHLTVLQNCTLA--------PIWVRKMpKKEAEDLavhyLERVRIAEHAHKFPGQISGGQQQRVAIAR 160
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAENIFLGrefvnrfgRIDWKKM-YAEADKL----LARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 161 SLCMKPKIMLFDEPTSAL-DPEmvKEVLDTMIG-LAQSGMTMLCVTHEMGFARTVADRV-IFMDRGEIVEQAAPD 232
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALtDTE--TESLFRVIReLKSQGRGIVYISHRLKEIFEICDDVtVFRDGQFIAEREVAD 227
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-234 |
1.68e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 119 MPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGM 198
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 16131159 199 TMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEF 234
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-226 |
4.45e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.20 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 22 YGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQeVGMVF-QHFNLF 100
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK--RRKEFARR-IGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 PHLTVLQN-CTLAPIWvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:COG4586 109 WDLPAIDSfRLLKAIY--RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16131159 180 P---EMVKEVLDTMIglAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIV 226
Cdd:COG4586 187 VvskEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-225 |
4.47e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 30 NINLTVQPGERIVLCGPSGSGKSTTIRCI-NHLEEHQQGRIVVDGIELneDIRN-IERVRQEVGMV---FQHFNLFPHLT 104
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV--KIRNpQQAIAQGIAMVpedRKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLAPI---WVRKMPKKEAE-DLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:PRK13549 358 VGKNITLAALdrfTGGSRIDDAAElKTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-223 |
6.31e-15 |
|
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: 70.74 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEE--HQQGRIVVDGIELNEDIRniervrQEVGMVFQHFNLFPHLTV 105
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQ------RSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 LqnctlapiwvrkmpkkeaEDLAVHYLERvriaehahkfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKE 185
Cdd:cd03232 97 R------------------EALRFSALLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131159 186 VLDTMIGLAQSGMTMLCVTHEMGfARTVA--DRVIFMDRG 223
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQPS-ASIFEkfDRLLLLKRG 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-235 |
9.48e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.47 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVN-KWYGQFH--VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVdgielnedirn 82
Cdd:PLN03232 608 LQPGAPAISIKNGYfSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 83 ierVRQEVGMVFQHFNLFpHLTVLQNCTLAPiwvrkmpKKEAEdlavHYLERVRIAEHAHK---FPGQ-----------I 148
Cdd:PLN03232 677 ---IRGSVAYVPQVSWIF-NATVRENILFGS-------DFESE----RYWRAIDVTALQHDldlLPGRdlteigergvnI 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVaDRVIFMDRGEIVEQ 228
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEE 820
|
....*..
gi 16131159 229 AAPDEFF 235
Cdd:PLN03232 821 GTFAELS 827
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-226 |
1.01e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 11 AMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielneDIRnIERVRQ-- 88
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-----DLI-VARLQQdp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 ---EVGMVF-----------QHFNLFPHLTVLqnctLAPIWVRKMPKKEA---EDLAVHYLERV--RIAEH-------AH 142
Cdd:PRK11147 76 prnVEGTVYdfvaegieeqaEYLKRYHDISHL----VETDPSEKNLNELAklqEQLDHHNLWQLenRINEVlaqlgldPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 143 KFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVkEVLDTMIgLAQSGmTMLCVTHEMGFARTVADRVIFMDR 222
Cdd:PRK11147 152 AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGFL-KTFQG-SIIFISHDRSFIRNMATRIVDLDR 228
|
....
gi 16131159 223 GEIV 226
Cdd:PRK11147 229 GKLV 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-237 |
1.27e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.62 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRivvdgIELNEDIRniervrqeVGM 92
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWSENAN--------IGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQ-HFNLFPH-LTVLQnctlapiWVRKMPKKEAEDLAVH-YLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKI 168
Cdd:PRK15064 387 YAQdHAYDFENdLTLFD-------WMSQWRQEGDDEQAVRgTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 169 MLFDEPTSALDPEMVkEVLDtmIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVE-QAAPDEFFAH 237
Cdd:PRK15064 460 LVMDEPTNHMDMESI-ESLN--MALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEYLRS 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-250 |
1.39e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE----DIR 81
Cdd:PLN03232 1230 PSRGSIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 NIERVRQEVGMVFQ---HFNLFPhltvLQNCTLAPIWvRKMPKKEAEDLavhyLERVRIAEHAHKFPG--QISGGQQQRV 156
Cdd:PLN03232 1310 RVLSIIPQSPVLFSgtvRFNIDP----FSEHNDADLW-EALERAHIKDV----IDRNPFGLDAEVSEGgeNFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 157 AIARSLCMKPKIMLFDEPTSALDPEmVKEVLDTMIGLAQSGMTMLCVTHEMgfaRTV--ADRVIFMDRGEIVEQAAPDEF 234
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVR-TDSLIQRTIREEFKSCTMLVIAHRL---NTIidCDKILVLSSGQVLEYDSPQEL 1456
|
250
....*....|....*.
gi 16131159 235 FahpkSERTRAFLSQV 250
Cdd:PLN03232 1457 L----SRDTSAFFRMV 1468
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-233 |
2.58e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 72.08 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVN-KW--YGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRC-INHLEEHQQGRIVVdgielnedir 81
Cdd:PLN03130 608 LEPGLPAISIKNGYfSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVI---------- 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 82 niervRQEVGMVfqhfnlfPHLTVLQNCTlapiwVRKMPKKEAEDLAVHYLERVRIAEHAHKF---PG-----------Q 147
Cdd:PLN03130 678 -----RGTVAYV-------PQVSWIFNAT-----VRDNILFGSPFDPERYERAIDVTALQHDLdllPGgdlteigergvN 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 148 ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVaDRVIFMDRGEIVE 227
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
....*.
gi 16131159 228 QAAPDE 233
Cdd:PLN03130 820 EGTYEE 825
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-233 |
3.81e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGErIV-LCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIE-RVRQEVGMVF-----QHFNL 99
Cdd:COG3845 273 ALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPASGSIRLDG----EDITGLSpRERRRLGVAYipedrLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPHLTVLQNCTLAPIWVRKMPK------KEAEDLAVHYLER--VRIAEHAHKFpGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:COG3845 348 VPDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEfdVRTPGPDTPA-RSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-234 |
8.76e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRN-IERVRQevGMVF-----QHFNLFPHLT 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI--DIRSpRDAIRA--GIMLcpedrKAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTL--------APIWVRkmPKKEAEdLAVHYLERVRI-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPT 175
Cdd:PRK11288 348 VADNINIsarrhhlrAGCLIN--NRWEAE-NADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 176 SALDPEMVKEVLDTMIGLAQSGMTMLCVTHE----MGfartVADRVIFMDRGEIVEQAAPDEF 234
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIAGELAREQA 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-233 |
1.06e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.15 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 22 YGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELneDIRNIErVRQEVGMVFQHFNLFP 101
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV--DAGDIA-TRRRVGYMSQAFSLYG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 102 HLTVLQNCTL-APIWvrKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:NF033858 353 ELTVRQNLELhARLF--HLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 181 EMVKEVLDTMIGLA-QSGMTMLCVTHEMGFA-RtvADRVIFMDRGEIVEQAAPDE 233
Cdd:NF033858 431 VARDMFWRLLIELSrEDGVTIFISTHFMNEAeR--CDRISLMHAGRVLASDTPAA 483
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
30-210 |
2.70e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 30 NINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnediRNIERVRQEVgmvfqHFNLF--------- 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDEY-----HQDLLylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 PHLTVLQNctLApiWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:PRK13538 87 TELTALEN--LR--FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180 190
....*....|....*....|....*....|.
gi 16131159 181 EMVKEVLDTMIG-LAQSGMTMLCVTHEMGFA 210
Cdd:PRK13538 163 QGVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
27-233 |
4.29e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFNLFPHLTVL 106
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QnctLAPI----WVRKMPKKEAEDlavhyleRVRIAEH---------AHKFPGQISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:PRK10575 104 E---LVAIgrypWHGALGRFGAAD-------REKVEEAislvglkplAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 174 PTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-233 |
4.81e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQqGRIVVDGIELNE-DIRNIERVR----QEV----GM-VFQHFNLf 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAwSAAELARHRaylsQQQtppfAMpVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 101 pHLTVLQNctlapiwvrkmpkKEAEDLAVHYL-ERVRIAEHAHKFPGQISGGQQQRVAIA-------RSLCMKPKIMLFD 172
Cdd:PRK03695 93 -HQPDKTR-------------TEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131159 173 EPTSALDPEMVKeVLDTMIG-LAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:PRK03695 159 EPMNSLDVAQQA-ALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-250 |
5.14e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 4 ILLQPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI----NHLEEHQQGRIVVDGIELnED 79
Cdd:TIGR00956 53 ALLKILTRGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITP-EE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 80 IRNieRVRQEVGMVFQHFNLFPHLTVLQncTLAPIWVRKMP-------------KKEAE-DLAVHYLERVRIAEHAHKFP 145
Cdd:TIGR00956 132 IKK--HYRGDVVYNAETDVHFPHLTVGE--TLDFAARCKTPqnrpdgvsreeyaKHIADvYMATYGLSHTRNTKVGNDFV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP----EMVKeVLDTMIGLAQSG--MTMLCVTHEmgfARTVADRVIF 219
Cdd:TIGR00956 208 RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSatalEFIR-ALKTSANILDTTplVAIYQCSQD---AYELFDKVIV 283
|
250 260 270
....*....|....*....|....*....|....*....
gi 16131159 220 MDRGEIVEQAAPD---EFFAH-----PKSERTRAFLSQV 250
Cdd:TIGR00956 284 LYEGYQIYFGPADkakQYFEKmgfkcPDRQTTADFLTSL 322
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
27-207 |
5.24e-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: 66.80 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEeHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFNLFPHlTVL 106
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNS--VPLQKWRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTLAPIWVRKMPKKEAEDLAVHYLervriaehAHKFPGQI-----------SGGQQQRVAIARSLCMKPKIMLFDEPT 175
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEVGLKSV--------IEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190
....*....|....*....|....*....|..
gi 16131159 176 SALDPeMVKEVLDTMIGLAQSGMTMLCVTHEM 207
Cdd:cd03289 167 AHLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-225 |
6.51e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELN-----EDIRN----IERVRQEVGMVFQhfn 98
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqDGLANgivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 lfphLTVLQNCTLAPIwvRKMPKK------EAEDLAV-HYLERVRIaehahKFP------GQISGGQQQRVAIARSLCMK 165
Cdd:PRK10762 345 ----MSVKENMSLTAL--RYFSRAggslkhADEQQAVsDFIRLFNI-----KTPsmeqaiGLLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 166 PKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-223 |
6.55e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCinhLEEHQQGRIVVDGIELNEDIRNIERVRQEVGMVFQHFNLFPHLTVL 106
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTLA-----PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQ-ISGGQQQRVAIARSLCMKPKIMLF-DEPTSALD 179
Cdd:TIGR00956 855 ESLRFSaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLD 934
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHE---MGFARTvaDRVIFMDRG 223
Cdd:TIGR00956 935 SQTAWSICKLMRKLADHGQAILCTIHQpsaILFEEF--DRLLLLQKG 979
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-180 |
1.48e-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: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWY--GQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEhQQGRIVVDGIELNEdiRNIER 85
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNS--VTLQT 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQEVGMVFQHFNLFPHlTVLQNCTLAPIWVRKMPKKEAEDLAVHYLervriaehAHKFPGQI-----------SGGQQQ 154
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSG-TFRKNLDPYEQWSDEEIWKVAEEVGLKSV--------IEQFPDKLdfvlvdggyvlSNGHKQ 1360
|
170 180
....*....|....*....|....*.
gi 16131159 155 RVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-224 |
1.57e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 14 TLENVNKWYG-QFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVV-DGI---------ELNE--DI 80
Cdd:PRK11819 8 TMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIkvgylpqepQLDPekTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 81 R-NIERVRQEVGMVFQHFN---------------LFPHLTVLQNctlapiwvrkmpKKEAEDLavHYLE-RVRIAEHAHK 143
Cdd:PRK11819 88 ReNVEEGVAEVKAALDRFNeiyaayaepdadfdaLAAEQGELQE------------IIDAADA--WDLDsQLEIAMDALR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 144 FP------GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVkEVLDTMigLAQSGMTMLCVTHEMGFARTVADRV 217
Cdd:PRK11819 154 CPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQF--LHDYPGTVVAVTHDRYFLDNVAGWI 230
|
....*..
gi 16131159 218 IFMDRGE 224
Cdd:PRK11819 231 LELDRGR 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-207 |
1.69e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedIRNI-ERVRQEVGMVFQHFNLFPHLTVL 106
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTtAALAAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNctlapIWVRKMP-------KKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:PRK11288 98 EN-----LYLGQLPhkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|
gi 16131159 180 -PEMvkEVLDTMIG-LAQSGMTMLCVTHEM 207
Cdd:PRK11288 173 aREI--EQLFRVIReLRAEGRVILYVSHRM 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-205 |
3.16e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnEDIRNIERVRQeVGMVFQHFNLFPHLTVL 106
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSRF-MAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QN----CTLAPIWVRKMPkkeAEDLAVhylerVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:PRK13543 101 ENlhflCGLHGRRAKQMP---GSALAI-----VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|...
gi 16131159 183 VKEVLDTMIGLAQSGMTMLCVTH 205
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTH 195
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-236 |
5.22e-12 |
|
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: 65.35 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 28 LKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG----IELNEDIRNiERVRQEVgmVFQH-FNLFPH 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayVPQQAWIQN-DSLRENI--LFGKaLNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTVLQNCTLAPIwVRKMPKKeaedlavhylERVRIAEHAHkfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEM 182
Cdd:TIGR00957 731 QQVLEACALLPD-LEILPSG----------DRTEIGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 183 VKEVLDTMIGLAQ--SGMTMLCVTHEMGFARTVaDRVIFMDRGEIVEQAAPDEFFA 236
Cdd:TIGR00957 796 GKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-240 |
6.66e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNE----DIRNIERVRQEVGMVFQ---HFNL 99
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGIIPQAPVLFSgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 100 FPhltvLQNCTLAPIWvrkmpkkEAEDLAvHYLERVR---------IAEHAHKFpgqiSGGQQQRVAIARSLCMKPKIML 170
Cdd:PLN03130 1334 DP----FNEHNDADLW-------ESLERA-HLKDVIRrnslgldaeVSEAGENF----SVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 171 FDEPTSALDpemVKEvlDTMIglaQSGM-------TMLCVTHEMgfaRTV--ADRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:PLN03130 1398 LDEATAAVD---VRT--DALI---QKTIreefkscTMLIIAHRL---NTIidCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-206 |
9.18e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIErvrQEVG 91
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ---KQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLAPiwvrkmpKKEAEDLAVHYLERVRIAEHAHKFP-GQISGGQQQRVAIARSLCMKPKIML 170
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDI-------HFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131159 171 FDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHE 206
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-240 |
9.44e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEdiRNIERVRQEVGMVFQHFNLFPHlTVL 106
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA--YGLRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTlapiwvrkmPKKEAEDLAV-HYLERVRIAEHAHKFPGQI-----------SGGQQQRVAIARSLCMK-PKIMLFDE 173
Cdd:PTZ00243 1402 QNVD---------PFLEASSAEVwAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARALLKKgSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 174 PTSALDPEMVKEVLDTMIGlAQSGMTMLCVTHEMgfaRTVA--DRVIFMDRGEIVEQAAPDEFFAHPKS 240
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMS-AFSAYTVITIAHRL---HTVAqyDKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-221 |
9.70e-12 |
|
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: 62.81 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 20 KWYGQFHvlkninLTVQPG-----ERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIRNIE-----RVRQE 89
Cdd:cd03237 8 KTLGEFT------LEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKadyegTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLtvlQNCTLAPIWVRKMPKKEAEDLavhylervriaehahkfpgqiSGGQQQRVAIARSLCMKPKIM 169
Cdd:cd03237 82 LSSITKDFYTHPYF---KTEIAKPLQIEQILDREVPEL---------------------SGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 170 LFDEPTSALDPE---MVKEVLDTMIGLAQSgmTMLCVTHEMGFARTVADRVIFMD 221
Cdd:cd03237 138 LLDEPSAYLDVEqrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
27-231 |
1.60e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCI-NHLEEHQ-------QGRIVVDGIELNE-DIRNIERVRQ------EVG 91
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAiDAPRLARLRAvlpqaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNL-----FPHltvlqnctlapiwVRK--MPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCM 164
Cdd:PRK13547 96 FAFSAREIvllgrYPH-------------ARRagALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 165 ---------KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQS-GMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAP 231
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-209 |
3.13e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 6 LQPANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI---------NHLeeHQQGRIVVDGiel 76
Cdd:PRK10938 254 LPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDL--TLFGRRRGSG--- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 77 nEDIRNIervRQEVGMVFQHFnlfpHLTVLQNCTLA---------PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQ 147
Cdd:PRK10938 329 -ETIWDI---KKHIGYVSSSL----HLDYRVSTSVRnvilsgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFH 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 148 -ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP---EMVKEVLDTMIGlaqSGMTML------------CVTHEMGF 209
Cdd:PRK10938 401 sLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETQLlfvshhaedapaCITHRLEF 475
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-228 |
4.80e-11 |
|
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: 60.73 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKST----TI------RCINHLEE------HQQGRIVVDGIE-----LNEDIRNIE 84
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSlafdTIyaegqrRYVESLSAyarqflGQMDKPDVDSIEglspaIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 85 R-VRQEVGMVFQHFNLfphltvlqnctLAPIWVRKMPKKEAE---DLAVHYLERVRIAehahkfpGQISGGQQQRVAIAR 160
Cdd:cd03270 89 RnPRSTVGTVTEIYDY-----------LRLLFARVGIRERLGflvDVGLGYLTLSRSA-------PTLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 161 SLCMKPK--IMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFM------DRGEIVEQ 228
Cdd:cd03270 151 QIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQ 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-219 |
5.18e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINltvqpgeRIVLCGPSGSGKSTTIRcinhleeHQQGRIVVDGIELNE----DIRNIERVRQEVGMVFqHFNLFPH 102
Cdd:PTZ00265 1251 GMKNVN-------EFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDynlkDLRNLFSIVSQEPMLF-NMSIYEN 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 LTV-LQNCTLAPiwVRKMPKKEAEDLAVHYLERvRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPE 181
Cdd:PTZ00265 1316 IKFgKEDATRED--VKRACKFAAIDEFIESLPN-KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1392
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131159 182 MVKEVLDTMIGLA-QSGMTMLCVTHEMGFARTVADRVIF 219
Cdd:PTZ00265 1393 SEKLIEKTIVDIKdKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-225 |
5.36e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.11 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 10 NAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRI-VVDGIELnedirniervrq 88
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL------------ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 89 evGMVFQH---FnLFPHLTVLQNCT-LAPiwvrkmpkKEAEDLAVHYL-----ERVRIAEHAHKFpgqiSGGQQQRVAIA 159
Cdd:PRK10636 378 --GYFAQHqleF-LRADESPLQHLArLAP--------QELEQKLRDYLggfgfQGDKVTEETRRF----SGGEKARLVLA 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131159 160 RSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSgmtMLCVTHEMGFARTVADRVIFMDRGEI 225
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA---LVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-228 |
6.84e-11 |
|
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: 59.26 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKSTtircinhleehqqgrIVVDGIELNEDIRNIERVRqevgmvfqhfNLFPHLTV 105
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLYASGKARLISFLP----------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 ----LQNCTlapiwvrkmpkkeaeDLAVHYLERVRIAehahkfpGQISGGQQQRVAIARSLCMKPK--IMLFDEPTSALD 179
Cdd:cd03238 64 fidqLQFLI---------------DVGLGYLTLGQKL-------STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFM------DRGEIVEQ 228
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
12-227 |
1.71e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ--QGRIVVDGIELNeDIRNIERVRQE 89
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESIL-DLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLTVLQNCTLAPIWVRK-MPKKEAEDLAVHYL--ERVRIAEHAHKFPGQ-----ISGGQQQRVAIARS 161
Cdd:CHL00131 86 IFLAFQYPIEIPGVSNADFLRLAYNSKRKfQGLPELDPLEFLEIinEKLKLVGMDPSFLSRnvnegFSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 162 LCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHemgFAR----TVADRVIFMDRGEIVE 227
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRlldyIKPDYVHVMQNGKIIK 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-224 |
2.44e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 37 PGERIVLCGPSGSGKSTTIRCI-NHLEEHQQGRIVVDGIELNEDIRNIERVrqevgmvfqhfnlfphltvlqnctlapiw 115
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 116 vrkmpkkeaedlavhylervriaEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLD------T 189
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16131159 190 MIGLAQSGMTMLCVTHEMGF-----ARTVADRVIFMDRGE 224
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-227 |
2.80e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 15 LENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRC-INHLEEhQQGRIVVdGIELnedirniervrqEVGMV 93
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHC-GTKL------------EVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 94 FQH-FNLFPHLTVLQNctLAPiwvrkmPKKEAE-----DLAVHYLE-------RVRIAEHAhkfpgqISGGQQQRVAIAR 160
Cdd:PRK11147 388 DQHrAELDPEKTVMDN--LAE------GKQEVMvngrpRHVLGYLQdflfhpkRAMTPVKA------LSGGERNRLLLAR 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 161 sLCMKP-KIMLFDEPTSALDPEMVkEVLDTMIGLAQSgmTMLCVTHEMGFA-RTVADRVIFMDRGEIVE 227
Cdd:PRK11147 454 -LFLKPsNLLILDEPTNDLDVETL-ELLEELLDSYQG--TVLLVSHDRQFVdNTVTECWIFEGNGKIGR 518
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-192 |
4.04e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNEDIrNIERVRQEVGMVFQHFNLFPH---- 102
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDI-NLKWWRSKIGVVSQDPLLFSNsikn 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 -------------------------------------------LTVLQNCTLAP--IWVRKMPKKEAEDLAVHYLERVRI 137
Cdd:PTZ00265 479 nikyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNelIEMRKNYQTIKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 138 AEHAHKFP-----------GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPE---MVKEVLDTMIG 192
Cdd:PTZ00265 559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG 627
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
12-205 |
8.58e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQ--QGRIVVDGIELNEdIRNIERVRQE 89
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLLE-LSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 90 VGMVFQHFNLFPHLT---VLQNCTLAPIWVRKMPKKEAEDLAVHYLERVRIAehahKFPGQI---------SGGQQQRVA 157
Cdd:PRK09580 80 IFMAFQYPVEIPGVSnqfFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL----KMPEDLltrsvnvgfSGGEKKRND 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16131159 158 IARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH 205
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
146-229 |
3.04e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGE- 224
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLv 469
|
....*..
gi 16131159 225 --IVEQA 229
Cdd:PRK10982 470 agIVDTK 476
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-224 |
5.97e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.25 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG-IELNEDIRNIERVRQEVGMVFQ-HFNLFPHLT 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFSWIMPGTIKENIIFGvSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLApiwvrkmpkkeaEDLAvhylervRIAEHAHKFPGQ----ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:cd03291 132 VVKACQLE------------EDIT-------KFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131159 181 EMVKEVLDTMIGLAQSGMTMLCVTHEMGFARtVADRVIFMDRGE 224
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-237 |
1.21e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.13 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTI------RCInhleehQQGRIVVdgieLNEDIRNiERV 86
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEV----LGGDMAD-ARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 87 RQEVG-----MVfQHF--NLFPHLTVlqnctlapiwvrkmpkkeAEDLAVH-------YLER-VRIAE--HA---HKFP- 145
Cdd:NF033858 71 RRAVCpriayMP-QGLgkNLYPTLSV------------------FENLDFFgrlfgqdAAERrRRIDEllRAtglAPFAd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 ---GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP-------EMVKEvldtmIGLAQSGMTMLCVTHEM----GFar 211
Cdd:NF033858 132 rpaGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDR-----IRAERPGMSVLVATAYMeeaeRF-- 204
|
250 260
....*....|....*....|....*.
gi 16131159 212 tvaDRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:NF033858 205 ---DWLVAMDAGRVLATGTPAELLAR 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
8-251 |
1.59e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 8 PANAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIR-------------C-INHLEEHQQG-RIVVD 72
Cdd:PLN03073 173 PAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipknCqILHVEQEVVGdDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 73 GIELNEDIRNIERVRQEVGMVFQHFNL-FPHLTV-------------LQNCTLAPIWVR--KMPKKEAEDLAVHYLERVR 136
Cdd:PLN03073 253 QCVLNTDIERTQLLEEEAQLVAQQRELeFETETGkgkgankdgvdkdAVSQRLEEIYKRleLIDAYTAEARAASILAGLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 137 I-AEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDpemVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVAD 215
Cdd:PLN03073 333 FtPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 16131159 216 RVIFMDRGEIV-------------EQAAPDEFFAHPKSERTRAFLSQVI 251
Cdd:PLN03073 410 DILHLHGQKLVtykgdydtfertrEEQLKNQQKAFESNERSRSHMQAFI 458
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-223 |
2.99e-08 |
|
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: 52.72 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 21 WYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCInhLEEHQ--QGRI----VVDGIELNEDIRNieRVRQEVGMVF 94
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVhwsnKNESEPSFEATRS--RNRYSVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 95 QHFNLFpHLTVLQNCTLAPIWVRKMPKKEAEDLAVH-------YLERVRIAEHAHkfpgQISGGQQQRVAIARSLCMKPK 167
Cdd:cd03290 86 QKPWLL-NATVEENITFGSPFNKQRYKAVTDACSLQpdidllpFGDQTEIGERGI----NLSGGQRQRICVARALYQNTN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 168 IMLFDEPTSALDPEMVKEVLDTMI--GLAQSGMTMLCVTHEMGFArTVADRVIFMDRG 223
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQEGIlkFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
27-252 |
6.12e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDG-IELNEDIRNIERVRQEVGMVFQ-HFNLFPHLT 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTSWIMPGTIKDNIIFGlSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLApiwvrkmpkkeaEDLAVhylervrIAEHAHKFPGQ----ISGGQQQRVAIARSLCMKPKIMLFDEPTSALDP 180
Cdd:TIGR01271 521 VIKACQLE------------EDIAL-------FPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 181 EMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFMDRGEI--------VEQAAPD--------EFFAHPKSERTR 244
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCyfygtfseLQAKRPDfsslllglEAFDNFSAERRN 660
|
....*...
gi 16131159 245 AFLSQVIH 252
Cdd:TIGR01271 661 SILTETLR 668
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
13-218 |
8.90e-08 |
|
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: 50.65 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINlTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDgielnedirniervrqevgm 92
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 vfqhfnlfphltvlqnctlapiwvrkmpkkeaedlavhyleRVRIAEHAHKFpgQISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:cd03222 60 -----------------------------------------GITPVYKPQYI--DLSGGELQRVAIAAALLRNATFYLFD 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQSGM-TMLCVTHEMGFARTVADRVI 218
Cdd:cd03222 97 EPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-205 |
9.57e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.44 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnedirniervRQEVGMVFQHfnlfPHLTV- 105
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-------------KGKLFYVPQR----PYMTLg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 106 -LQNCTLAPIWVRKMPKKEAEDLA-VHYLERVRIaEHAHKFPG----------QISGGQQQRVAIARSLCMKPKIMLFDE 173
Cdd:TIGR00954 530 tLRDQIIYPDSSEDMKRRGLSDKDlEQILDNVQL-THILEREGgwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 16131159 174 PTSALDPEMVkevlDTMIGLAQS-GMTMLCVTH 205
Cdd:TIGR00954 609 CTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
13-231 |
1.20e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.08 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKwygqfHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI--------NHLEEHQQGRivVDGIELNEDIRNIE 84
Cdd:cd03271 1 LTLKGARE-----NNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalarrLHLKKEQPGN--HDRIEGLEHIDKVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 85 RVRQE-VGM-----------VFQHF-NLFphltvlqnCTlapiwVRKMPKKEAEDLAVHYLERvRIA-------EHAHKF 144
Cdd:cd03271 74 VIDQSpIGRtprsnpatytgVFDEIrELF--------CE-----VCKGKRYNRETLEVRYKGK-SIAdvldmtvEEALEF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 145 ----P-------------------GQ----ISGGQQQRVAIARSLCMK---PKIMLFDEPTSALDPEMVKEVLDTMIGLA 194
Cdd:cd03271 140 feniPkiarklqtlcdvglgyiklGQpattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLV 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 16131159 195 QSGMTMLCVTHEMGFARTvADRVIFM-----DR-GEIVEQAAP 231
Cdd:cd03271 220 DKGNTVVVIEHNLDVIKC-ADWIIDLgpeggDGgGQVVASGTP 261
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
12-205 |
1.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVnKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGIELNedirNIERVRqeVG 91
Cdd:PRK13541 1 MLSLHQL-QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN----NIAKPY--CT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 92 MVFQHFNLFPHLTVLQNCTLapiWVRKMPKKEAEDLAVHYLervRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PRK13541 74 YIGHNLGLKLEMTVFENLKF---WSEIYNSAETLYAAIHYF---KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190
....*....|....*....|....*....|....
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH 205
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-237 |
2.40e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 25 FHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCInhleehqqgrivvdGIELNEDIRNIERvRQEVGMVFQHFNLFPHLT 104
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNII--------------GGSLSPTVGKVDR-NGEVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 105 VLQNCTLapiwvrKM-----PKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:PRK13546 102 GIENIEF------KMlcmgfKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDEFFAH 237
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
12-233 |
3.05e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 12 MITLENVNKwygqfHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINH--LEEHQQGRIVVDG----IELNEDIRNIER 85
Cdd:TIGR00630 613 FLTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYpaLANRLNGAKTVPGrytsIEGLEHLDKVIH 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 86 VRQE-------------VGmVFQHF-NLF---PHLTVL----------------QNCT-----------LAPIWVR---- 117
Cdd:TIGR00630 688 IDQSpigrtprsnpatyTG-VFDEIrELFaetPEAKVRgytpgrfsfnvkggrcEACQgdgvikiemhfLPDVYVPcevc 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 118 KMPKKEAEDLAVHYLERvRIA-------EHAHKF----P-------------------GQ----ISGGQQQRVAIARSLC 163
Cdd:TIGR00630 767 KGKRYNRETLEVKYKGK-NIAdvldmtvEEAYEFfeavPsisrklqtlcdvglgyirlGQpattLSGGEAQRIKLAKELS 845
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131159 164 MK---PKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFM-----DR-GEIVEQAAPDE 233
Cdd:TIGR00630 846 KRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeggDGgGTVVASGTPEE 923
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-231 |
3.43e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 24 QFHVLKNINLTVQPGERIVLCGPSGSGKSTtircinhLEEHQQGRIVVDGIELNEDIRNIERvRQEV-----GMVFQHFN 98
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRKTGGYIEGDIRISGFPK-KQETfarisGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 99 LFPHLTVLQNCTLA-----PIWVRKMPKKEAEDLAVHYLERVRIAEHAHKFPG--QISGGQQQRVAIARSLCMKPKIMLF 171
Cdd:PLN03140 964 HSPQVTVRESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 172 DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVA-DRVIFMDRGEIVEQAAP 231
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGQVIYSGP 1104
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
42-222 |
5.76e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 42 VLCGPSGSGKSTTIRCINH--LEEHQQGRIvvDGIELNEDIRNIErVRQEVGMVFQHFN-----LFPHLTVLQNCtlapI 114
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYalTGELPPNSK--GGAHDPKLIREGE-VRAQVKLAFENANgkkytITRSLAILENV----I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 115 WVRKmpkkeaEDLAVhYLERVRiaehahkfpGQISGGQQQ------RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLD 188
Cdd:cd03240 99 FCHQ------GESNW-PLLDMR---------GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 16131159 189 TMIG--LAQSGMTMLCVTHEMGFaRTVADRVIFMDR 222
Cdd:cd03240 163 EIIEerKSQKNFQLIVITHDEEL-VDAADHIYRVEK 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-252 |
1.44e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 126 DLAVHYLERVRIAehahkfpGQISGGQQQRVAIARSLCMKPKIMLF--DEPTSALDPEMVKEVLDTMIGLAQSGMTMLCV 203
Cdd:TIGR00630 474 DVGLDYLSLSRAA-------GTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVV 546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 204 THEMGFARTvADRVIFMDR------GEIVEQAAPDEFFAHPKSeRTRAFLSQVIH 252
Cdd:TIGR00630 547 EHDEDTIRA-ADYVIDIGPgagehgGEVVASGTPEEILANPDS-LTGQYLSGRKK 599
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-245 |
1.98e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDgielnediRNIERVRQEVGMVfqhfnlfpHLTVL 106
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------RSIAYVPQQAWIM--------NATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 QNCTLapiwvrkMPKKEAEDLAvhylERVRIAE---HAHKFPG-----------QISGGQQQRVAIARSLCMKPKIMLFD 172
Cdd:PTZ00243 739 GNILF-------FDEEDAARLA----DAVRVSQleaDLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 173 EPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFArTVADRVIFMDRGEIVEQAAPDEFFAHPKSERTRA 245
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-181 |
2.36e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.01 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 3 QILLQPA----NAMITLENVNKWYGQFHVLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDgielne 78
Cdd:TIGR03719 309 EIYIPPGprlgDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 79 dirniERVRqeVGMVFQ-HFNLFPHLTVLQNCT--LAPIWV--RKMPKKEaedlavhYLERVRI-AEHAHKFPGQISGGQ 152
Cdd:TIGR03719 383 -----ETVK--LAYVDQsRDALDPNKTVWEEISggLDIIKLgkREIPSRA-------YVGRFNFkGSDQQKKVGQLSGGE 448
|
170 180
....*....|....*....|....*....
gi 16131159 153 QQRVAIARSLCMKPKIMLFDEPTSALDPE 181
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-207 |
3.71e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.98 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 34 TVQPGERIVLCGPSGSGKSTTIRCI--------NHLEEHQQGRIVVD---GIELNEDIRNIERVRQEVGMVFQHFNLFPH 102
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 103 L---TVLQNctlapiwVRKMPKKEAEDLAVHYLERVRIAEHAHKfpgQISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:cd03236 102 AvkgKVGEL-------LKKKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180
....*....|....*....|....*...
gi 16131159 180 PEMVKEVLDTMIGLAQSGMTMLCVTHEM 207
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
149-218 |
4.11e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 4.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDPE---MVKEVLDTMIglAQSGMTMLCVTHEMGFARTVADRVI 218
Cdd:PRK13409 455 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA--EEREATALVVDHDIYMIDYISDRLM 525
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
27-206 |
4.65e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 27 VLKNINLTVQPGERIVLCGPSGSGKSTTIRCINHLEEHQQGRIVVDGielnedirnieRVRqeVGMVFQHfnlfpHLTVL 106
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-----------KVR--MAVFSQH-----HVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 107 qNCTLAPI--WVRKMPKKEAEDLAVHYLERVRIAEHAHKFPGQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVk 184
Cdd:PLN03073 586 -DLSSNPLlyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV- 663
|
170 180
....*....|....*....|..
gi 16131159 185 EVLDTMIGLAQSGMTMlcVTHE 206
Cdd:PLN03073 664 EALIQGLVLFQGGVLM--VSHD 683
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-222 |
9.78e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 31 INLTVQPGERIVLC--GPSGSGKSTTIRCInhleehqqgrivvdgielnedirniervrqEVGMVFQHFNLFPHLTVLQN 108
Cdd:cd03227 12 VPNDVTFGEGSLTIitGPNGSGKSTILDAI------------------------------GLALGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 109 CTlapiwvrkmpkkEAEDLAVHYLERVriaehahkfpgQISGGQQQRVAIA---RSLCMKPK-IMLFDEPTSALDPEMVK 184
Cdd:cd03227 62 CI------------VAAVSAELIFTRL-----------QLSGGEKELSALAlilALASLKPRpLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131159 185 EVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVIFMDR 222
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPELAEL-ADKLIHIKK 155
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
32-251 |
1.29e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.38 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 32 NLTVQPGERI-VLCGPSGSGKSTTIRCI-----------------NHLEEHQQGRIVVDgIELNEDIRNI------ERVR 87
Cdd:COG3593 16 DLSIELSDDLtVLVGENNSGKSSILEALrlllgpsssrkfdeedfYLGDDPDLPEIEIE-LTFGSLLSRLlrlllkEEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHFN--LFPHLTVLQNcTLAPIWVRKMPKKEAeDLAVHYLERVRIAEHA-------HKFP-GQISGGQQQRVA 157
Cdd:COG3593 95 EELEEALEELNeeLKEALKALNE-LLSEYLKELLDGLDL-ELELSLDELEDLLKSLslriedgKELPlDRLGSGFQRLIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 158 IARSLCM-------KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTV-ADRVIFMDRGE----- 224
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRLRRDSggtts 252
|
250 260 270
....*....|....*....|....*....|.
gi 16131159 225 -IVEQAAPDE---FFAHPKSERTRAFLSQVI 251
Cdd:COG3593 253 tKLIDLDDEDlrkLLRYLGVTRSELLFARKV 283
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
146-207 |
2.33e-05 |
|
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: 45.16 E-value: 2.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131159 146 GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDpemVKE---VLDTMIGLAQSGMTMLCVTHEM 207
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-252 |
4.57e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 148 ISGGQQQRVAIARSLCMK-PKIM-LFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFArTVADRVIFMDR--- 222
Cdd:PRK00635 477 LSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgag 555
|
90 100 110
....*....|....*....|....*....|...
gi 16131159 223 ---GEIVEQAAPDEFFAHPKSeRTRAFLSQVIH 252
Cdd:PRK00635 556 ifgGEVLFNGSPREFLAKSDS-LTAKYLRQELT 587
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-218 |
6.47e-05 |
|
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: 43.62 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 20 KWYGQFHvlkninLTVQPG-----ERIVLCGPSGSGKSTTIRCINhleehqqGRIVVDGIELNEDIRnI----ERVRQEV 90
Cdd:COG1245 349 KSYGGFS------LEVEGGeiregEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEVDEDLK-IsykpQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 91 GMVFQHFnLFPHLTV------LQNCTLAPIWVRKMPKKEAEDLavhylervriaehahkfpgqiSGGQQQRVAIARSLCM 164
Cdd:COG1245 415 DGTVEEF-LRSANTDdfgssyYKTEIIKPLGLEKLLDKNVKDL---------------------SGGELQRVAIAACLSR 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 165 KPKIMLFDEPTSALDPE---MVKEVLDTMIglAQSGMTMLCVTHEMGFARTVADRVI 218
Cdd:COG1245 473 DADLYLLDEPSAHLDVEqrlAVAKAIRRFA--ENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
148-218 |
7.77e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131159 148 ISGGQQQRVAIARSLCM---KPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARtVADRVI 218
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-55 |
1.08e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKST----TI 55
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSlafdTI 47
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
13-194 |
1.09e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 13 ITLENVNKWYGQFHVLKNINLTVqpgerivLCGPSGSGKSTTIRCINHLEEHQQGRivvdGIELNEDIRNIERVRQEVGM 92
Cdd:COG0419 5 LRLENFRSYRDTETIDFDDGLNL-------IVGPNGAGKSTILEAIRYALYGKARS----RSKLRSDLINVGSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 93 VFQH-------------FNLFP-------------------------HLTVLQnctlAPIWVRKMPKKEAEDLAVHYLER 134
Cdd:COG0419 74 EFEHggkryrierrqgeFAEFLeakpserkealkrllgleiyeelkeRLKELE----EALESALEELAELQKLKQEILAQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 135 VRIAEHAHkfpgQISGGQQQRVAIARSLcmkpkIMLFDepTSALDPEMVKEVLDTMIGLA 194
Cdd:COG0419 150 LSGLDPIE----TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
147-179 |
1.14e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.14e-04
10 20 30
....*....|....*....|....*....|...
gi 16131159 147 QISGGQQQRVAIARSLCMKPKIMLFDEPTSALD 179
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-233 |
2.64e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKSTTIRCI-------NHleehqQGRIVVDGIELneDIRNIERV-----------R 87
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrNI-----SGTVFKDGKEV--DVSTVSDAidaglayvtedR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 88 QEVGMVFQHfnlfphlTVLQNCTLAPIwvRKMPKK----EAEDLAV--HYLERVRIaehahKFP------GQISGGQQQR 155
Cdd:NF040905 347 KGYGLNLID-------DIKRNITLANL--GKVSRRgvidENEEIKVaeEYRKKMNI-----KTPsvfqkvGNLSGGNQQK 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 156 VAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTVADRVIFMDRGEIVEQAAPDE 233
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE 490
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
41-92 |
3.26e-04 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 40.60 E-value: 3.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 41 IVLCGPSGSGKSTTIRC-INHLEEHQQGRIVV--DGIE-LNEDIRNIerVRQ-EVGM 92
Cdd:cd01131 24 VLVTGPTGSGKSTTLAAmIDYINETRSKHIITieDPIEfVHKHKKSL--INQrEVGR 78
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
139-205 |
5.03e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 5.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131159 139 EHAHKFP-GQISGGQQQ---RVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTH 205
Cdd:pfam13304 227 GGGGELPaFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
124-225 |
6.93e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 124 AEDLAVHYLERVRIAEHAHKFP-GQISGGQQQRVAIARSLCMKPKIMLFDEPTSALDPEMVKEVLDTmigLAQSGMTMLC 202
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
90 100
....*....|....*....|....*..
gi 16131159 203 VTHEMGFARTV----ADrvifMDRGEI 225
Cdd:PRK15064 208 ISHDRHFLNSVcthmAD----LDYGEL 230
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
41-72 |
1.12e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 38.27 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|..
gi 16131159 41 IVLCGPSGSGKSTTIRcinhleEHQQGRIVVD 72
Cdd:COG4639 5 VVLIGLPGSGKSTFAR------RLFAPTEVVS 30
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-53 |
1.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.32e-03
10 20
....*....|....*....|....*...
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKST 53
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSS 37
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-250 |
1.44e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 146 GQ----ISGGQQQRVAIARSLCMKPK---IMLFDEPTSALDPEMVKEVLDTMIGLAQSGMTMLCVTHEMGFARTvADRVI 218
Cdd:PRK00349 825 GQpattLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWII 903
|
90 100 110
....*....|....*....|....*....|....*...
gi 16131159 219 FM-----DR-GEIVEQAAPDEFFAHPKSeRTRAFLSQV 250
Cdd:PRK00349 904 DLgpeggDGgGEIVATGTPEEVAKVEAS-YTGRYLKPV 940
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
149-227 |
2.41e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131159 149 SGGQQQRVAIARSLCMKPKIMLFDEPTSALDpemvkevLDTMIGLAQ-----SGmTMLCVTHEMGFARTVADRVIFMDRG 223
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksyQG-TLILISHDRDFLDPIVDKIIHIEQQ 222
|
....
gi 16131159 224 EIVE 227
Cdd:PRK10636 223 SLFE 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
26-55 |
2.67e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.67e-03
10 20 30
....*....|....*....|....*....|....
gi 16131159 26 HVLKNINLTVQPGERIVLCGPSGSGKST----TI 55
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSlafdTI 47
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
41-67 |
4.12e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 36.36 E-value: 4.12e-03
10 20
....*....|....*....|....*..
gi 16131159 41 IVLCGPSGSGKSTTIRCInhLEEHQQG 67
Cdd:cd00071 2 IVLSGPSGVGKSTLLKRL--LEEFDPN 26
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
41-83 |
5.39e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 36.86 E-value: 5.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 16131159 41 IVLCGPSGSGKSTTIRCI-NHLEehQQGRIVV-----DGIELNEDIRNI 83
Cdd:cd01672 3 IVFEGIDGAGKTTLIELLaERLE--ARGYEVVltrepGGTPIGEAIREL 49
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
41-72 |
6.16e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 36.13 E-value: 6.16e-03
10 20 30
....*....|....*....|....*....|..
gi 16131159 41 IVLCGPSGSGKSTTIRciNHLEEHqqGRIVVD 72
Cdd:pfam13671 2 ILLVGLPGSGKSTLAR--RLLEEL--GAVRLS 29
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
13-58 |
6.61e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.71 E-value: 6.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16131159 13 ITLENVNKWYGQ-FHVLKNINLtvqpgerivLCGPSGSGKSTTIRCI 58
Cdd:pfam13476 1 LTIENFRSFRDQtIDFSKGLTL---------ITGPNGSGKTTILDAI 38
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
41-92 |
8.10e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 36.99 E-value: 8.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131159 41 IVLCGPSGSGKSTTIRC-INHLEEHQQGRIVV--DGIE-LNEDIRNIerVRQ-EVGM 92
Cdd:COG2805 128 VLVTGPTGSGKSTTLAAmIDYINETRAKHIITieDPIEfVHKHKKSL--INQrEVGR 182
|
|
| COG4185 |
COG4185 |
Predicted ABC-type ATPase or kinase [General function prediction only]; |
41-96 |
9.27e-03 |
|
Predicted ABC-type ATPase or kinase [General function prediction only];
Pssm-ID: 443339 Cd Length: 197 Bit Score: 36.02 E-value: 9.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131159 41 IVLCGPSGSGKSTTIRciNHLEEHQQGRIVV--DGIELNEDIRNIERVRQEVGMVFQH 96
Cdd:COG4185 7 YIIAGPNGAGKSTFAR--TILPEELGGLEFVnaDLIARGLSPFNPETAAYEAGRLALE 62
|
|
| |
