|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-248 |
4.21e-165 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 455.99 E-value: 4.21e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVG 89
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEI 248
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
11-220 |
1.97e-142 |
|
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: 397.67 E-value: 1.97e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGM 90
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-245 |
1.26e-108 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 313.66 E-value: 1.26e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 4 SAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS-------- 75
Cdd:COG4598 2 TDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdge 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 76 ---DSSRAIDAVRREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQ 152
Cdd:COG4598 82 lvpADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 153 RAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEF 232
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|...
gi 1150860720 233 FRDPKHQRTRTFL 245
Cdd:COG4598 242 FGNPKSERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-245 |
2.30e-102 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 297.39 E-value: 2.30e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVG 89
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-251 |
5.66e-89 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 263.53 E-value: 5.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEE-----IQEGKITVEGT-TLSDSSRAIDAV 84
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTArSLSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTF 244
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
....*..
gi 1150860720 245 LGEILAH 251
Cdd:PRK11264 244 LEKFLLQ 250
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
11-250 |
7.69e-88 |
|
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: 260.92 E-value: 7.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-----------SSR 79
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 AIDAVRREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARA 159
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKH 238
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|..
gi 1150860720 239 QRTRTFLGEILA 250
Cdd:TIGR03005 241 ERTREFLSKVIA 252
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-218 |
2.49e-87 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 259.18 E-value: 2.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSS----RAIDAVRR 86
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKtpsdKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYM 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
11-218 |
8.36e-87 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 257.63 E-value: 8.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS----DSSRAIDAVRR 86
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYM 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-251 |
2.51e-83 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 252.31 E-value: 2.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY----GAFHALKNVNMTVRKGE--KIVlcGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDA 83
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEifGII--GYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRREVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCME 163
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDtmigLARD-----GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKH 238
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILD----LLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQS 234
|
250
....*....|...
gi 1150860720 239 QRTRTFLGEILAH 251
Cdd:COG1135 235 ELTRRFLPTVLND 247
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-220 |
3.24e-82 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 245.72 E-value: 3.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYG----AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAID 82
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AVRRE-VGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALC 161
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 162 MEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRD 219
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
10-245 |
1.71e-78 |
|
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: 236.81 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEI-----QEGKITVEGTTLSDSSRAIDAV 84
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLvpgvrIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPhKTIMENCTLAPmRVKGL-SKADAEATARKYLERVRILNQ----ADKYPAQLSGGQQQRAAIARA 159
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQ 239
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*.
gi 1150860720 240 RTRTFL 245
Cdd:TIGR00972 238 RTEDYI 243
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-220 |
2.07e-78 |
|
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: 235.46 E-value: 2.07e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA----FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVR 85
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 RE-VGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRD 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-219 |
1.50e-75 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 229.59 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 5 AEQAPLIALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRA 80
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 81 IDAVRREVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVAL-GLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 161 CMEPKAMLFDEPTSALDP----EMVKEVLDTmigLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLS 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
9-220 |
9.35e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 227.25 E-value: 9.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS-DSSRAIDAVRR 86
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENC---------TLAPMRvKGLSKADAEAtARKYLERVRILNQADKYPAQLSGGQQQRAAIA 157
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLL-GLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRD 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-220 |
2.03e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.98 E-value: 2.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRR 86
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENctLA-PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAEN--VAfGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMND 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-220 |
3.74e-74 |
|
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: 225.15 E-value: 3.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYG----AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAV 84
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-220 |
3.71e-73 |
|
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: 222.01 E-value: 3.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGMVF 92
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QSFNLFPHKTIMENctLA-PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:cd03259 79 QDYALFPHLTVAEN--IAfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNE 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-245 |
4.96e-73 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 223.31 E-value: 4.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 18 KWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS---DS--------SRAIDAVRR 86
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKdgqlkvadKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQA-DKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-220 |
3.89e-72 |
|
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: 218.21 E-value: 3.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGM 90
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApmrvkglskadaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
11-250 |
1.00e-71 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 222.75 E-value: 1.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDssRAIDA 83
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSE--KELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRREVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCME 163
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTR 242
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
....*...
gi 1150860720 243 TFLGEILA 250
Cdd:PRK11153 239 EFIQSTLH 246
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-220 |
1.59e-71 |
|
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: 218.36 E-value: 1.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVG 89
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR--ELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQsfN----LFpHKTIMENCTLAPMRvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-220 |
1.88e-71 |
|
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: 218.70 E-value: 1.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVR 85
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFPHKTIMENCTLaPMRV-KGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAF-PLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-220 |
2.40e-71 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 217.61 E-value: 2.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFH-ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVRREV 88
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELED 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-245 |
1.12e-69 |
|
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: 222.47 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWY-----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD 76
Cdd:COG1123 252 PAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 77 -SSRAIDAVRREVGMVFQ----SFNlfPHKTIMEncTLA-PMRV-KGLSKADAEATARKYLERVRI-LNQADKYPAQLSG 148
Cdd:COG1123 332 lSRRSLRELRRRVQMVFQdpysSLN--PRMTVGD--IIAePLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 149 GQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEG 227
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
250
....*....|....*...
gi 1150860720 228 PPEEFFRDPKHQRTRTFL 245
Cdd:COG1123 488 PTEEVFANPQHPYTRALL 505
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-219 |
1.19e-69 |
|
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: 213.49 E-value: 1.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYG----AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRR 86
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 167 MLFDEPTSALDP----EMVKEVLDTmigLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-220 |
8.07e-69 |
|
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: 212.04 E-value: 8.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA-FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTL-SDSSRAIDAVRREV 88
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENC------TLAPMRV--KGLSKADAEAtARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSlfGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKD 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
11-220 |
2.50e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 214.55 E-value: 2.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENctLA-PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:COG3839 80 VFQSYALYPHMTVYEN--IAfPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 170 DEPTSALDP----EMVKEVLDTmigLARDGMTMICVTHEmgfarQV-----ADRVIFMSD 220
Cdd:COG3839 158 DEPLSNLDAklrvEMRAEIKRL---HRRLGTTTIYVTHD-----QVeamtlADRIAVMND 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-220 |
2.61e-66 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 204.62 E-value: 2.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGM 90
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS--LKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNL-FPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-220 |
4.18e-66 |
|
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: 204.72 E-value: 4.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ-----EGKITVEGTTLSDSSRAIDAVR 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFPhKTIMENCTLAPmRVKG-LSKADAEATARKYLERV----RILNQADkyPAQLSGGQQQRAAIARAL 160
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGiKLKEELDERVEEALRKAalwdEVKDRLH--ALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLN 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-218 |
4.85e-66 |
|
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: 204.28 E-value: 4.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVR 85
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 R-EVGMVFQ----SFNlfPHKTIMEncTLA-PMRVKGLSKADAEATARKYLERVRILN---QADKYPAQLSGGQQQRAAI 156
Cdd:cd03257 81 RkEIQMVFQdpmsSLN--PRMTIGE--QIAePLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-242 |
1.75e-65 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 204.12 E-value: 1.75e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ-----EGKITVEGTTLSD 76
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 77 SSRAIDAVRREVGMVFQSFNLFPhKTIMENCTLAPmRVKGL-SKADAEATARKYLERVRILNQA----DKYPAQLSGGQQ 151
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGL-RLHGIkSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 152 QRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEE 231
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
250
....*....|.
gi 1150860720 232 FFRDPKHQRTR 242
Cdd:COG1117 240 IFTNPKDKRTE 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-220 |
6.57e-65 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 201.83 E-value: 6.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidaVRREVGM 90
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE---VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
11-220 |
1.07e-63 |
|
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: 198.61 E-value: 1.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-220 |
2.04e-63 |
|
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: 198.29 E-value: 2.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYG-AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSS-RAIDAVRRE 87
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLAPMRVKG--------LSKADAEaTARKYLERVRILNQADKYPAQLSGGQQQRAAIARA 159
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgrFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKeDGITVIINLHQVDLAKKYADRIVGLKA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-220 |
5.23e-63 |
|
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: 196.95 E-value: 5.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRA-IDAVRREVG 89
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLaPMRVKG-LSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYD 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-252 |
2.98e-62 |
|
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: 195.41 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGA----FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssRAIDAVR 85
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQ----SFNlfPHKTIMEncTLA-PMRVKGLskADAEATARKYLERV----RILnqaDKYPAQLSGGQQQRAAI 156
Cdd:COG1124 79 RRVQMVFQdpyaSLH--PRHTVDR--ILAePLRIHGL--PDREERIAELLEQVglppSFL---DRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRD 235
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
250
....*....|....*..
gi 1150860720 236 PKHQRTRTFLGEILAHH 252
Cdd:COG1124 230 PKHPYTRELLAASLAFE 246
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-220 |
6.22e-62 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 197.68 E-value: 6.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdssRAIDAVRREVGM 90
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENctLA-PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:COG1118 80 VFQHYALFPHMTVAEN--IAfGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 170 DEPTSALD----PEMVKEVLDTmigLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1118 158 DEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQ 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-220 |
7.43e-61 |
|
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: 192.47 E-value: 7.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR-AIDAVRRE-VGMVFQSFNLF 98
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkELRELRRKkISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:cd03294 115 PHRTVLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 179 EMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03294 194 LIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKD 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-247 |
1.14e-59 |
|
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: 188.66 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFH-ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsDSSRAIDAV--RRE 87
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDG----EDIREQDPVelRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRI--LNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTF 244
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 1150860720 245 LGE 247
Cdd:cd03295 236 VGA 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-237 |
3.85e-59 |
|
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: 195.12 E-value: 3.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ---EGKITVEGTTLSDSSRAID 82
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AvrREVGMVFQSF--NLFPHkTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:COG1123 82 G--RRIGMVFQDPmtQLNPV-TVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPK 237
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
11-220 |
2.37e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 187.22 E-value: 2.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAV--RRE 87
Cdd:COG1125 2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD----LDPVelRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLERV----RILnqADKYPAQLSGGQQQRAAIARALCME 163
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVgldpEEY--RDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 164 PKAMLFDEPTSALDPeMVKEVL-DTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1125 155 PPILLMDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMRE 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-220 |
4.70e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 189.16 E-value: 4.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDssRAIDAVRRE-VGMVFQSFNLFPH 100
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGediTKLSK--KELRELRRKkMSMVFQHFALLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP-- 178
Cdd:COG4175 120 RTVLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPli 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 179 --EMVKEVLDtmigL-ARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4175 199 rrEMQDELLE----LqAKLKKTIVFITHDLDEALRLGDRIAIMKD 239
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
10-220 |
2.16e-56 |
|
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: 179.37 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVRRE 87
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 168 LFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
8-218 |
2.38e-56 |
|
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: 183.70 E-value: 2.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidavRRE 87
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ----KRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAYG-LKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 168 LFDEPTSALDPEmVKEVLDTMI-GLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:TIGR03265 157 LLDEPLSALDAR-VREHLRTEIrQLQRRlGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-220 |
3.63e-56 |
|
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: 179.55 E-value: 3.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 1 MPQSAeqAPLIALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TT 73
Cdd:COG4181 1 MSSSS--APIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 74 LSDSSRAidAVRRE-VGMVFQSFNLFPHKTIMENCTLaPMRVKGlsKADAEATARKYLERVRILNQADKYPAQLSGGQQQ 152
Cdd:COG4181 79 LDEDARA--RLRARhVGFVFQSFQLLPTLTALENVML-PLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 153 RAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRA 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-218 |
5.62e-56 |
|
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: 181.79 E-value: 5.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEE---IQEGKITVEGTTLSD-SSRAI 81
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DAVR-REVGMVFQ----SFNlfPHKTI----MEnctlaPMRV-KGLSKADAEATARKYLERVRILN---QADKYPAQLSG 148
Cdd:COG0444 81 RKIRgREIQMIFQdpmtSLN--PVMTVgdqiAE-----PLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 149 GQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVM 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-248 |
2.82e-55 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 181.68 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 1 MPQSAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssra 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 81 IDAVRREVGMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQ 239
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNL 239
|
....*....
gi 1150860720 240 RTRTFLGEI 248
Cdd:PRK09452 240 FVARFIGEI 248
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-220 |
3.31e-55 |
|
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: 176.29 E-value: 3.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-219 |
4.19e-55 |
|
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: 177.15 E-value: 4.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD----VPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApMRVK----GLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFG-LRVKprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMS 219
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMN 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-220 |
8.89e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.00 E-value: 8.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGM 90
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP--PPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPhKTIMENCTLaPMRVKGlsKADAEATARKYLERV----RILnqaDKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:COG4619 79 VPQEPALWG-GTVRDNLPF-PFQLRE--RKFDRERALELLERLglppDIL---DKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDtMIG--LARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEE-LLReyLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-220 |
9.93e-53 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 171.38 E-value: 9.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVG 89
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR--ELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQS----FNL----------FPHKTIMEnctlapmrvkGLSKADAEAtARKYLERVRILNQADKYPAQLSGGQQQRAA 155
Cdd:COG1120 79 YVPQEppapFGLtvrelvalgrYPHLGLFG----------RPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 156 IARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-220 |
1.14e-52 |
|
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: 168.34 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREVGM 90
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK---DIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENctlapmrvkglskadaeatarkylervrilnqadkypAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03230 78 LPEEPSLYENLTVREN-------------------------------------LKLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-220 |
3.36e-52 |
|
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: 170.30 E-value: 3.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaIDAVRREV 88
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQS-FNLFPHKTI-------MENctlapmrvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNK 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-220 |
4.69e-52 |
|
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: 170.32 E-value: 4.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA-----FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTL-SDSSRAIDAV 84
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQsfnlFPHK-----TIMENCTLAPMRVkGLSKADAEATARKYLERVRI-LNQADKYPAQLSGGQQQRAAIAR 158
Cdd:TIGR04521 81 RKKVGLVFQ----FPEHqlfeeTVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 159 ALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHK 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-248 |
7.56e-52 |
|
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: 172.34 E-value: 7.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 18 KWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRA--IDAVRREVGMVFQSF 95
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVelREVRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 96 NLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:TIGR01186 81 ALFPHMTILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 176 LDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEI 248
Cdd:TIGR01186 160 LDPLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-218 |
1.00e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRRE 87
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNL---FPhktimenctlapMRV---------------KGLSKADAEAtARKYLERVRILNQADKYPAQLSGG 149
Cdd:COG1121 77 IGYVPQRAEVdwdFP------------ITVrdvvlmgrygrrglfRRPSRADREA-VDEALERVGLEDLADRPIGELSGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 150 QQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-174 |
2.03e-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: 164.36 E-value: 2.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIdaVRREVGMVFQSFNLFPHKTIME 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS--LRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 106 NCTLaPMRVKGLSKADAEATARKYLERVRILNQAD----KYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:pfam00005 79 NLRL-GLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
13-218 |
3.62e-51 |
|
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: 165.87 E-value: 3.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS--DSSRAIDAVRREVGM 90
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPplNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-248 |
6.94e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 169.49 E-value: 6.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRaIDAVRREVGM 90
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSR-LHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENC----TLAPMRvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIafglTVLPRR-ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 1150860720 246 GEI 248
Cdd:PRK10851 238 GEV 240
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
25-220 |
9.14e-51 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 165.28 E-value: 9.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAIdaVRRE-VGMVFQSFNLFPH 100
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGkevTNLSYSQKII--LRRElIGYIFQSFNLIPH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:NF038007 98 LSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 181 VKEVLDTMIGLARDGMTMICVTHEMGfARQVADRVIFMSD 220
Cdd:NF038007 177 ARAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKD 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-247 |
1.45e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 164.93 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHalKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidavRREVGM 90
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----ERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLapmrvkGLS---KADAEATAR--KYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGL------GLRpglKLTAEQRAQveQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTF 244
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
...
gi 1150860720 245 LGE 247
Cdd:COG3840 230 LGI 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
13-220 |
3.07e-50 |
|
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: 161.64 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVF 92
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE--ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QsfnlfphktimenctlapmrvkglskadaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 173 TSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-218 |
5.05e-50 |
|
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: 163.37 E-value: 5.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdSSRAIDAVRREVGMVF 92
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT-GLPPHERARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QSFNLFPHKTIMENCTLApmrVKGLSKADAEATARKYLERVRILNQADKYPA-QLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:cd03224 82 EGRRIFPELTVEENLLLG---AYARRRAKRKARLERVYELFPRLKERRKQLAgTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVL 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-218 |
1.07e-48 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 162.98 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 4 SAEQAPLIALEGVGKWY----GAF-------HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGT 72
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 73 TLSD-SSRAIDAVRREVGMVFQ----SFNlfPHKTIMEncTLA-PMRVKGL-SKADAEATARKYLERVRiLN--QADKYP 143
Cdd:COG4608 81 DITGlSGRELRPLRRRMQMVFQdpyaSLN--PRMTVGD--IIAePLRIHGLaSKAERRERVAELLELVG-LRpeHADRYP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 144 AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-220 |
1.24e-48 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 157.93 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFH--ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREV 88
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL--ESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFpHKTIMENctlapmrvkglskadaeatarkylervrIlnqadkypaqLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03228 79 AYVPQDPFLF-SGTIREN----------------------------I----------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLaRDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDD 169
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-220 |
2.35e-48 |
|
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: 157.60 E-value: 2.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 12 ALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAvrREVGMV 91
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA--RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 92 FQSfnlfphktimenctlapmrvkglskadaeatarkyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:cd03214 79 PQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-220 |
2.86e-48 |
|
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: 159.64 E-value: 2.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREVG 89
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE---DVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMEN----CTLapmrvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:COG4555 78 VLPDERGLYDRLTVRENiryfAEL-----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHK 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-246 |
3.47e-48 |
|
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: 159.04 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHaLKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 171 EPTSALDPEmVKEVLDTMIGLARD--GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLG 246
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-245 |
5.35e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 159.17 E-value: 5.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEgKITVEGTTLSDS----SRAIDAV 84
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNP-EVTITGSIVYNGhniySPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 --RREVGMVFQSFNLFPHkTIMENCTLApMRVKGL-SKADAEATARKYLERVRILNQA-DKYPAQ---LSGGQQQRAAIA 157
Cdd:PRK14239 83 dlRKEIGMVFQQPNPFPM-SIYENVVYG-LRLKGIkDKQVLDEAVEKSLKGASIWDEVkDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLaRDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPK 237
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*...
gi 1150860720 238 HQRTRTFL 245
Cdd:PRK14239 240 HKETEDYI 247
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-218 |
3.11e-47 |
|
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: 157.12 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIdaVRR 86
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRI--ARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLAPMRVKGLS--------------KADAEATARKYLERVRILNQADKYPAQLSGGQQQ 152
Cdd:COG0411 80 GIARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 153 RAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVL 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-226 |
2.68e-46 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 154.13 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIdaVRREVG 89
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEI--ARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLAPMRVKGLS---------KADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAQARTGSGlllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEE 226
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-245 |
3.37e-46 |
|
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: 161.39 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWY-----------GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVE 70
Cdd:COG4172 267 PVPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 71 GTTLSD-SSRAIDAVRREVGMVFQ----SFNlfPHKTIMEncTLA-PMRV--KGLSKADAEATARKYLERVRIL-NQADK 141
Cdd:COG4172 346 GQDLDGlSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQ--IIAeGLRVhgPGLSAAERRARVAEALEEVGLDpAARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 142 YPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4172 422 YPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
250 260
....*....|....*....|....*
gi 1150860720 221 GEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:COG4172 502 GKVVEQGPTEQVFDAPQHPYTRALL 526
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-247 |
8.71e-46 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 156.42 E-value: 8.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 6 EQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDavR 85
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS--IQ--Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTF 244
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
...
gi 1150860720 245 LGE 247
Cdd:PRK11432 237 MGD 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-216 |
9.54e-46 |
|
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: 152.18 E-value: 9.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA-FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVRREV 88
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVI 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-248 |
3.65e-45 |
|
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: 153.80 E-value: 3.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 41 LCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKA 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 121 DAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMI 199
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 200 CVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEI 248
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
8-218 |
4.15e-45 |
|
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: 151.29 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdSSRAIDAVRRE 87
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-GLPPHRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEatarkyLERV---------RILNQAdkypAQLSGGQQQRAAIAR 158
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD------LERVyelfprlkeRRRQRA----GTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 159 ALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVL 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-245 |
1.92e-44 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 156.38 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGV----GKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKS----TLIRCINHLEEIQEGKITVEGTTLSD-SS 78
Cdd:COG4172 4 MPLLSVEDLsvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 79 RAIDAVR-REVGMVFQ----SFNlfPHKTI----MEnctlaPMRV-KGLSKADAEATARKYLERVRILNQA---DKYPAQ 145
Cdd:COG4172 84 RELRRIRgNRIAMIFQepmtSLN--PLHTIgkqiAE-----VLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 146 LSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSDGEII 224
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260
....*....|....*....|.
gi 1150860720 225 EEGPPEEFFRDPKHQRTRTFL 245
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLL 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-215 |
2.13e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 155.56 E-value: 2.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRRE 87
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS-PRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLA--PMRVKGLSKADAEATARKYLERVRI-LNqADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
35-220 |
8.06e-44 |
|
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: 147.06 E-value: 8.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 35 KGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAID--AVRREVGMVFQSFNLFPHKTIMENCTLApm 112
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlpPQQRKIGLVFQQYALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 113 rVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLA 192
Cdd:cd03297 100 -LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIK 178
|
170 180
....*....|....*....|....*....
gi 1150860720 193 RD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03297 179 KNlNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
9.08e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 148.45 E-value: 9.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 19 WYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ-----EGKITVEGTTLSDSSRAIDAVRREVGMVFQ 93
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFNLFPHKTIMENCTLApMRVKGLSKADAEATarkylERVR-----------ILNQADKYPAQLSGGQQQRAAIARALCM 162
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIG-VKLNGLVKSKKELD-----ERVEwalkkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 163 EPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTR 242
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
...
gi 1150860720 243 TFL 245
Cdd:PRK14267 246 KYV 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-216 |
4.46e-43 |
|
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: 145.37 E-value: 4.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRREVGMVFQSFNL-- 97
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 -FPhKTIMENCTLAPMRVKGL----SKADAEAtARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:cd03235 82 dFP-ISVRDVVLMGLYGHKGLfrrlSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 173 TSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVI 216
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
7.04e-43 |
|
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: 153.00 E-value: 7.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVG-KWYGA-FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR 79
Cdd:COG4987 325 PAPAPGGPSLELEDVSfRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 aiDAVRREVGMVFQSFNLFpHKTIMENCTLApmrvkglsKADA-EATARKYLERVRILNQADKYP-----------AQLS 147
Cdd:COG4987 405 --DDLRRRIAVVPQRPHLF-DTTLRENLRLA--------RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLS 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 148 GGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARdGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLED 544
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
25-208 |
7.08e-43 |
|
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: 144.10 E-value: 7.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQSFN--LFpHKT 102
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF-AAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK 182
Cdd:TIGR01166 86 VDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*.
gi 1150860720 183 EVLDTMIGLARDGMTMICVTHEMGFA 208
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-220 |
1.58e-42 |
|
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: 153.45 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFpHKTIM 104
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA--SLRRQIGVVLQDVFLF-SGTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLapmrvkglskADAEATarkyLERVR-----------ILNQADKYP-------AQLSGGQQQRAAIARALCMEPKA 166
Cdd:COG2274 567 ENITL----------GDPDAT----DEEIIeaarlaglhdfIEALPMGYDtvvgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARdGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDK 684
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-219 |
1.64e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 148.44 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQ---APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDss 78
Cdd:PRK11607 8 PQAKTRkalTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 79 raIDAVRREVGMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIAR 158
Cdd:PRK11607 86 --VPPYQRPINMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 159 ALCMEPKAMLFDEPTSALDPE----MVKEVLDTmigLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-216 |
1.82e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 147.87 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVGM 90
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApMRVKGLSKADAEatarKYLERV-RILNQA---DKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFG-LKLAGAKKEEIN----QRVNQVaEVLQLAhllDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 167 MLFDEPTSALDP----EMVKEVLDTMIGLARdgmTMICVTHEMGFARQVADRVI 216
Cdd:PRK11000 155 FLLDEPLSNLDAalrvQMRIEISRLHKRLGR---TMIYVTHDQVEAMTLADKIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-220 |
1.98e-42 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 141.80 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAiDAVRREVGM 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR-DARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQsfnlfphktimenctlapmrvkglskadaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-220 |
2.16e-42 |
|
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: 147.55 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFhALkNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAID--AVRREVGMVFQSFNL 97
Cdd:COG4148 11 RGGF-TL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpPHRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 FPHKTIMENCTLapmrvkGLSKADAEATARKYLERVRILNQA---DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:COG4148 89 FPHLSVRGNLLY------GRKRAPRAERRISFDEVVELLGIGhllDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 175 ALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4148 163 ALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQ 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-220 |
3.07e-42 |
|
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: 143.41 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYG--AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREVGM 90
Cdd:cd03263 3 IRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY---SIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTL-ApmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLaRDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-237 |
5.78e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 144.45 E-value: 5.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQSFN--LFPhKT 102
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDdqLFA-PT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK 182
Cdd:PRK13639 96 VEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 183 EVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPK 237
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-245 |
1.36e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 143.00 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 1 MPQSAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEI-----QEGKITVEGTTLS 75
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 76 DSSRAIDAVRREVGMVFQSFNLFPhKTIMENCTLAPmRVKGLsKADAEATARKYLERVRILNQA-DKYPAQ---LSGGQQ 151
Cdd:PRK14243 81 APDVDPVEVRRRIGMVFQKPNPFP-KSIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVkDKLKQSglsLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 152 QRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSDGEIIEEG---- 227
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMTAFFNVELTEGGGrygy 236
|
250 260
....*....|....*....|...
gi 1150860720 228 -----PPEEFFRDPKHQRTRTFL 245
Cdd:PRK14243 237 lvefdRTEKIFNSPQQQATRDYV 259
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
11-220 |
2.89e-41 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 140.71 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGafHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdssrAIDAVRREVGM 90
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT----AAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApmRVKGL--SKADAEATArKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLG--LSPGLklTAEDRQAIE-VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-219 |
2.93e-41 |
|
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: 143.30 E-value: 2.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 18 KWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREVGMVFQSFNL 97
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGY---DVVREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 FPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:TIGR01188 78 DEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150860720 178 PEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIID 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-218 |
6.89e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.72 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQ--SFNLFpHKT 102
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLF-EET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLAPMRVkGLSKADAEATARKYLERVRILNQ--ADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:PRK13637 101 IEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 181 VKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-220 |
1.35e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 141.38 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 22 AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL--------------EEIQEGKITVE--------GTTLSDSSR 79
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdEKNKKKTKEKEkvleklviQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 AIDAVRREVGMVFQ--SFNLFpHKTIMENCTLAPMRVkGLSKADAEATARKYLERVRI-LNQADKYPAQLSGGQQQRAAI 156
Cdd:PRK13651 99 KIKEIRRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVAL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-215 |
1.40e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 145.55 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 6 EQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS-DSSRaiDAV 84
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPR--DAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENCTLA--PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCM 162
Cdd:COG3845 79 ALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 163 EPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-252 |
1.86e-40 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 142.56 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKnVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAID--AVRREVGMVFQSFNLFPHK 101
Cdd:TIGR02142 12 FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEKRRIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCtlapmrVKGLSKADAEATARKYLERVRILNQA---DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:TIGR02142 91 SVRGNL------RYGMKRARPSERRISFERVIELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 179 EMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDP------KHQRTRTFLGEILAH 251
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlpwlaREDQGSLIEGVVAEH 244
|
.
gi 1150860720 252 H 252
Cdd:TIGR02142 245 D 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-220 |
2.08e-40 |
|
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: 138.75 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRREVGMVFQSFNLFPHKTIME 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLAPMRV-KGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150860720 185 LDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-245 |
3.82e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 138.89 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEgKITVEGTTLSDSSRA----IDAVRREVGMVFQSF 95
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYP-EARVSGEVYLDGQDIfkmdVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 96 NLFPHKTIMENCTLAPmRVKGL--SKADAEATARKYLERVR----ILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:PRK14247 92 NPIPNLSIFENVALGL-KLNRLvkSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDgMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-218 |
4.12e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 139.77 E-value: 4.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAID--AVRREVGMVFQsfnlFPH-- 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkPLRKKVGIVFQ----FPEhq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 ---KTIMENCTLAPMRVkGLSKADAEATARKYLERVRiLNQA--DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:PRK13634 98 lfeETVEKDICFGPMNF-GVSEEDAKQKAREMIELVG-LPEEllARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 176 LDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-220 |
4.45e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 145.31 E-value: 4.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREVGMVFQSFNLFpHKTIM 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTL--ESLRRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApmrVKGLSKADAEATARK-YLERVrILNQADKYPAQ-------LSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:COG1132 432 ENIRYG---RPDATDEEVEEAAKAaQAHEF-IEALPDGYDTVvgergvnLSGGQRQRIAIARALLKDPPILILDEATSAL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 177 DPEMVKEVLDTMIGLARdGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG1132 508 DTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDD 549
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
9-220 |
4.58e-40 |
|
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: 137.95 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKwygAF--H--------ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI--NHLeeIQEGKITV----EGT 72
Cdd:COG4778 3 TLLEVENLSK---TFtlHlqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSILVrhdgGWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 73 TLSDSS-RAIDAVRR-EVGMVFQSFNLFPHKT----IMEnctlaPMRVKGLSKADAEATARKYLERVRI---LNQAdkYP 143
Cdd:COG4778 78 DLAQASpREILALRRrTIGYVSQFLRVIPRVSaldvVAE-----PLLERGVDREEARARARELLARLNLperLWDL--PP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 144 AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
26-220 |
6.59e-40 |
|
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: 137.00 E-value: 6.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaidavRREVGMVFQS--FNLFpHKTI 103
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER-----RKSIGYVMQDvdYQLF-TDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLAPMRVkglskADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKE 183
Cdd:cd03226 90 REELLLGLKEL-----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150860720 184 VLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-220 |
6.85e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 144.52 E-value: 6.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVG-KWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRa 80
Cdd:COG4988 328 PLPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 81 iDAVRREVGMVFQSFNLFpHKTIMENCTLApmrvkglsKADA-EATARKYLERVRILNQADKYP-----------AQLSG 148
Cdd:COG4988 407 -ASWRRQIAWVPQNPYLF-AGTIRENLRLG--------RPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSG 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 149 GQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARdGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDD 546
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-220 |
1.02e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAV 84
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET--VWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQS-FNLFPHKTI-------MENCtlapmrvkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAI 156
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVqddvafgLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGM-TMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNK 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-220 |
5.33e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 135.00 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVRRE 87
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 168 LFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-218 |
8.55e-39 |
|
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: 133.95 E-value: 8.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraidAVRREVGM 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI------AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCT-LApmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-220 |
8.76e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.39 E-value: 8.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaidavRR---- 86
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 --EVGmvfqsfnLFPHKTIMENCT-LApmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCME 163
Cdd:COG4152 77 peERG-------LYPKMKVGEQLVyLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
11-218 |
1.11e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 136.03 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA---FH--ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSS--RAIDA 83
Cdd:PRK13649 3 INLQNVSYTYQAgtpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRREVGMVFQsfnlFPH-----KTIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQA-DKYPAQLSGGQQQRAAIA 157
Cdd:PRK13649 83 IRKKVGLVFQ----FPEsqlfeETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVL 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
11-220 |
2.87e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 132.73 E-value: 2.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlSDSSRAIDAVRReVGM 90
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR-IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATarkyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLL-ARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINK 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
11-218 |
3.74e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.51 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAVRREVG 89
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----LEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEataRKYLERVRILNQA---DKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIE---ERVAEAARILELEpllDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 167 MLFDEPTSALDP----EMVKEVLDtmigLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK11650 156 FLFDEPLSNLDAklrvQMRLEIQR----LHRRlKTTSLYVTHDQVEAMTLADRVVVM 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-219 |
6.73e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.45 E-value: 6.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAF----HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRREV 88
Cdd:COG4525 6 VRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 169 FDEPTSALDP---EMVKEVLDTMIGLARDGMTMIcvTHEMGFARQVADRVIFMS 219
Cdd:COG4525 158 MDEPFGALDAltrEQMQELLLDVWQRTGKGVFLI--THSVEEALFLATRLVVMS 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-220 |
1.07e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 133.29 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDaVRREVGMVFQSfnlfPHKTIM 104
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWD-IRNKAGMVFQN----PDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 -----ENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPE 179
Cdd:PRK13633 100 ativeEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150860720 180 MVKEVLDTMIGL-ARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK13633 179 GRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDS 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-220 |
1.82e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.50 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWY---------GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR 79
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 A-IDAVRREVGMVFQ----SFNlfPHKTIMEncTLA-PMR-VKGLSKADAEATARKYLERVRI-LNQADKYPAQLSGGQQ 151
Cdd:PRK10419 82 AqRKAFRRDIQMVFQdsisAVN--PRKTVRE--IIRePLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 152 QRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDN 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-220 |
2.46e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.17 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFN--LFPhK 101
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN--EKWVRSKVGLVFQDPDdqVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:PRK13647 96 TVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 182 KEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-219 |
2.84e-37 |
|
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: 130.57 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlSDSSRAIDAVRREVGM 90
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHA-RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 171 EPTSALDP---EMVKEVLDTMigLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:cd03265 157 EPTIGLDPqtrAHVWEYIEKL--KEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-220 |
2.88e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 131.72 E-value: 2.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLiALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraidaVRREV 88
Cdd:PRK11247 12 PL-LLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-------AREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLapmrvkGLsKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGL------GL-KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEE 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-245 |
3.01e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 135.16 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRA--IDAVRREVGMVFQSFNLFPHKT 102
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK 182
Cdd:PRK10070 123 VLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 183 EVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK10070 202 EMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-220 |
3.32e-37 |
|
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: 129.91 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREV 88
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE---PIRDAREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARkyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFW-AALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTH-EMGFArqvADRVIFMSD 220
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqPLELA---AARVLDLGD 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-219 |
5.09e-37 |
|
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: 129.95 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdSSRAIDAVRREVGMVFQSFNLFP 99
Cdd:TIGR03410 10 YGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-KLPPHERARAGIAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 HKTIMENC-TLAPMRVKGLSKADAEAtarkyLERVRILNQADKYPA-QLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:TIGR03410 89 RLTVEENLlTGLAALPRRSRKIPDEI-----YELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 178 PEMVKEVLDTMIGLA-RDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVME 206
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-220 |
7.02e-37 |
|
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: 129.21 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 30 NMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraidAVRREVGMVFQSFNLFPHKTIMENCTL 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA----PYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 110 A---PMRVKGLSKADAEATARKylerVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLD 186
Cdd:TIGR01277 94 GlhpGLKLNAEQQEKVVDAAQQ----VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1150860720 187 TMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR01277 170 LVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQ 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-245 |
1.19e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 130.17 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTL---SDSSRaIDAV--RREVGMVFQSFNLFPH 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQ-IDAIklRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLaPMRVKGLS-----KADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:PRK14246 105 LSIYDNIAY-PLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 176 LDPeMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK14246 184 IDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-220 |
1.24e-36 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 136.39 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWY----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAID 82
Cdd:PRK10535 2 TALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AVRRE-VGMVFQSFNLFPHKTIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALC 161
Cdd:PRK10535 82 QLRREhFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 162 MEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRD 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-218 |
2.15e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.33 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG--TTLSDSSRAIDAVRREVGMVFQsfnlFPHKTI 103
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTL-----APMRVkGLSKADAEATARKYLERVRILNQ-ADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:PRK13641 99 FENTVLkdvefGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150860720 178 PEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-220 |
2.62e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.16 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 30 NMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidavRREVGMVFQSFNLFPHKTIMENCTL 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS----RRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 110 apmrvkGLS-----KADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEv 184
Cdd:PRK10771 95 ------GLNpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150860720 185 ldtMIGLARD-----GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10771 168 ---MLTLVSQvcqerQLTLLMVSHSLEDAARIAPRSLVVAD 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-218 |
8.02e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 128.18 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaIDAVRREV 88
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK-LQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNL-FPHKTIME-------NCTLAPMRV-KGLSKADAEATARKYLERVrilnqadkyPAQLSGGQQQRAAIARA 159
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEdlafgpeNLCLPPIEIrKRVDRALAEIGLEKYRHRS---------PKTLSGGQGQCVALAGI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGfARQVADRVIFM 218
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVM 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-208 |
1.75e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.05 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAidAVR-REVGMVFQSFNLFPHK 101
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplHQMDEEARA--KLRaKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:PRK10584 104 NALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180
....*....|....*....|....*...
gi 1150860720 182 KEVLDTMIGLARD-GMTMICVTHEMGFA 208
Cdd:PRK10584 183 DKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
10-216 |
2.92e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 126.67 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL---EEIQEGKITVEGTTLSDS---SRAIDA 83
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREgrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRREVGMVFQSFNLFPHKTIMENCTLAPMR--------VKGLSKADAEaTARKYLERVRILNQADKYPAQLSGGQQQRAA 155
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 156 IARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVI 216
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIV 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-220 |
3.27e-35 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 125.42 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFNLFpHKTIME 105
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT--LDSLRRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMRVKGlSKADAEATARKYLERVRILNQADKYPAQ-------LSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:cd03253 94 N--IRYGRPDA-TDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 179 EMVKEVLDTMIGLARdGMTMICVTHEMgfaRQV--ADRVIFMSD 220
Cdd:cd03253 171 HTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKD 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-219 |
4.94e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.26 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQS-FNLFPHKTI 103
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN--LKEIRKKIGIIFQNpDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 -------MENCTLAPMRVKglskadaeATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:PRK13632 102 eddiafgLENKKVPPKKMK--------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 177 DPEMVKEVLDTMIGLARDGM-TMICVTHEMGFARQvADRVIFMS 219
Cdd:PRK13632 174 DPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFS 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
8-249 |
4.99e-35 |
|
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: 125.71 E-value: 4.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKIT--------VEGTTLSDSSR 79
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATyimrsgaeLELYQLSEAER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 AIDAvRREVGMVFQSF--NLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRI-LNQADKYPAQLSGGQQQRAAI 156
Cdd:TIGR02323 81 RRLM-RTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRD 235
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
250
....*....|....
gi 1150860720 236 PKHQRTRTFLGEIL 249
Cdd:TIGR02323 240 PQHPYTQLLVSSIL 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-179 |
5.05e-35 |
|
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: 124.23 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGeKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlSDSSRAIDAVRREVGM 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG---QDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMEncTLAPM-RVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170
....*....|
gi 1150860720 170 DEPTSALDPE 179
Cdd:cd03264 155 DEPTAGLDPE 164
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-220 |
1.43e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 125.30 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL---EEIQEGKITVEGTTLSdsSRAIDAVRREVGMVFQS-FNLFPH 100
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT--AKTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:PRK13640 100 ATVGDDVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150860720 181 VKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK13640 179 KEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDD 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-216 |
1.81e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.98 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCIN-HLEEI--QEGKITVEGTTLSdssrAIDAVRREVGMVFQSFNLFPHKT 102
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLT----ALPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLA-PmrvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:COG4136 93 VGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150860720 182 KEVLDTMIGLARD-GMTMICVTHEMGfARQVADRVI 216
Cdd:COG4136 170 AQFREFVFEQIRQrGIPALLVTHDEE-DAPAAGRVL 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
26-220 |
3.60e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.07 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQS-FNLFPHKTIM 104
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN--VWDIRHKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:PRK13650 101 DDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 185 LDTMIGLARD-GMTMICVTHEMGfarQVA--DRVIFMSD 220
Cdd:PRK13650 180 IKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKN 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-220 |
1.03e-33 |
|
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: 121.57 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFNLFpHKTIM 104
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT--LASLRRQIGLVSQDVFLF-NDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApmrVKGLSKADAEATARKYLERVRILNQADKYPA-------QLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:cd03251 94 ENIAYG---RPGATREEVEEAARAANAHEFIMELPEGYDTvigergvKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 178 PEMVKEVLDTMIGLARDgMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03251 171 TESERLVQAALERLMKN-RTTFVIAHRLSTIEN-ADRIVVLED 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-220 |
1.37e-33 |
|
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: 121.49 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssRAIDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRD--LNLRWLRSQIGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLapmrvkGLSKA---DAEATARKYLERVRILNQADKYP-------AQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:cd03249 96 NIRY------GKPDAtdeEVEEAAKKANIHDFIMSLPDGYDtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 176 LDPEMVKEVLDTmIGLARDGMTMICVTHEMGfARQVADRVIFMSD 220
Cdd:cd03249 170 LDAESEKLVQEA-LDRAMKGRTTIVIAHRLS-TIRNADLIAVLQN 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
26-220 |
2.44e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.42 E-value: 2.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRRevGMVFQSFNL-FPhktim 104
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR--AVLPQHSSLsFP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 enCT--------LAPMrvkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALC------MEPKAMLFD 170
Cdd:PRK13548 91 --FTveevvamgRAPH---GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-219 |
4.19e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.57 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRREVG 89
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-------KPVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFPHKTIMENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLF 169
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 170 DEPTSALDP---EMVKEVLDTMigLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:PRK11248 153 DEPFGALDAftrEQMQTLLLKL--WQETGKQVLLITHDIEEAVFMATELVLLS 203
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
24-220 |
5.15e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.11 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQS--FNLFPhK 101
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDpdNQLFS-A 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:PRK13636 99 SVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 182 KEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13636 178 SEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKE 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
10-220 |
8.65e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 119.01 E-value: 8.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGA----FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVR 85
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:cd03266 78 RRLGFVSDSTGLYDRLTARENLEYFA-GLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-220 |
1.12e-32 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 118.46 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsdSSRAIDAV--RREVGMVFQSFNLFpHK 101
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLDPAdlRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLApmrvkglskaDAEATARKYLERVRI--LNQ-ADKYP-----------AQLSGGQQQRAAIARALCMEPKAM 167
Cdd:cd03245 93 TLRDNITLG----------APLADDERILRAAELagVTDfVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 168 LFDEPTSALD---PEMVKEVLDTMIGlardGMTMICVTHEMGFArQVADRVIFMSD 220
Cdd:cd03245 163 LLDEPTSAMDmnsEERLKERLRQLLG----DKTLIIITHRPSLL-DLVDRIIVMDS 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-248 |
1.23e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 124.97 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGT---TLSDSsrAIDAVRREVGMVFQS--FNLF 98
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPG--KLQALRRDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKT----IMEnctlaPMRVKGLSKADAEATARKYL-ERVRIL-NQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:PRK10261 416 PRQTvgdsIME-----PLRVHGLLPGKAAAARVAWLlERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 173 TSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEI 248
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-218 |
1.40e-32 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 124.32 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRR 86
Cdd:TIGR02857 319 ASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA--DSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPhKTIMENCTLApmrvkglsKADAEATA-RKYLERVRILN-----------QADKYPAQLSGGQQQRA 154
Cdd:TIGR02857 397 QIAWVPQHPFLFA-GTIAENIRLA--------RPDASDAEiREALERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 155 AIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARdGMTMICVTHEMGFARqVADRVIFM 218
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
23-219 |
1.43e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 120.73 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL----------EEIQEG-KITVEGTTLSDSSRAID---AVRREV 88
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLikskygtiqvGDIYIGdKKNNHELITNPYSKKIKnfkELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQ--SFNLFpHKTIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQ-ADKYPAQLSGGQQQRAAIARALCMEPK 165
Cdd:PRK13631 119 SMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-218 |
1.64e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.22 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 22 AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRA--IDAVRREVGMVFQsfnlFP 99
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeIKPVRKKVGVVFQ----FP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 H-----KTIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQA-DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:PRK13643 94 EsqlfeETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 174 SALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-220 |
2.16e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 118.38 E-value: 2.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVR-REVGMVFQSFNLFPHKTI 103
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLaPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKE 183
Cdd:PRK11629 105 LENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1150860720 184 VLDTMIGL-ARDGMTMICVTHEMGFARQVaDRVIFMSD 220
Cdd:PRK11629 184 IFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRD 220
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-246 |
3.16e-32 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.07 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR-AIDAVRREVGMVFQ----SFNlf 98
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeAQKLLRQKIQIVFQnpygSLN-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMEncTLA-PMRVK-GLSKADAEATARKYLERVRIL-NQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:PRK11308 107 PRKKVGQ--ILEePLLINtSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 176 LDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLG 246
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-245 |
3.36e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.20 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIDAVRREVGMVFQ----SFNlfP 99
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQdplaSLN--P 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 HKTIMEncTLA-PMRV--KGLSKADAEATARKYLERVRIL-NQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:PRK15079 114 RMTIGE--IIAePLRTyhPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 176 LDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALM 262
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-215 |
2.23e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.01 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidaVRREVGM 90
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL---ARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSFNLFPHKTIMENcTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:PRK13536 119 VPQFDNLDLEFTVREN-LLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRL 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-220 |
2.27e-31 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.98 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREV-----GMVFqSFN---- 96
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVlpqhsSLAF-PFTveev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 97 ----LFPHktimenctlapmrvkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALC-------MEPK 165
Cdd:COG4559 96 valgRAPH---------------GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 166 AMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ 215
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-245 |
3.11e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 115.90 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ-----EGKITVEGTTLSDSSRAIDA 83
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRREVGMVFQSFNLFPhKTIMENCTLAPMRVKGLSKADAEATARKYLERV----RILNQADKYPAQLSGGQQQRAAIARA 159
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 160 LCMEPKAMLFDEPTSALDP--EMVKEVLDTMIGLaRDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEG-----PPEEF 232
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRL-RSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQlvefgLTKKI 243
|
250
....*....|...
gi 1150860720 233 FRDPKHQRTRTFL 245
Cdd:PRK14258 244 FNSPHDSRTREYV 256
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
9-203 |
3.13e-31 |
|
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: 115.57 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGK-ITVEGTTLSDSSraIDAVRRE 87
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED--VWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFnlfpHKTIMENCTLAPM----------RVKGLSKADaEATARKYLERVRILNQADKYPAQLSGGQQQRAAIA 157
Cdd:COG1119 80 IGLVSPAL----QLRFPRDETVLDVvlsgffdsigLYREPTDEQ-RERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDG-MTMICVTH 203
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTH 201
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-220 |
5.52e-31 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 115.02 E-value: 5.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEkiVLC--GPSGSGKSTLIRCINHLEEIQEGKIT--VEGTTLSDSSRAIDA 83
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRKGCRDVSFDLYPGE--VLGivGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 VRR-----EVGMVFQSF--NLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRI-LNQADKYPAQLSGGQQQRAA 155
Cdd:PRK11701 82 ERRrllrtEWGFVHQHPrdGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 156 IARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
24-220 |
1.63e-30 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.20 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsdssRAIDA--VRREVGMVFQSFNLFpHK 101
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----RQIDPadLRRNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLapmrvkGLSKADAEATARKyLERVRILNQADKYP-----------AQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:TIGR03375 554 TLRDNIAL------GAPYADDEEILRA-AELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 171 EPTSALD---PEMVKEVLDTMIGlardGMTMICVTHEMGFARQVaDRVIFMSD 220
Cdd:TIGR03375 627 EPTSAMDnrsEERFKDRLKRWLA----GKTLVLVTHRTSLLDLV-DRIIVMDN 674
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-203 |
2.37e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 117.85 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 4 SAEQAPLIALEGVG-KWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiD 82
Cdd:TIGR02868 328 VGLGKPTLELRDLSaGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ--D 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AVRREVGMVFQSFNLFpHKTIMENCTLApmrvkglsKADA-EATARKYLERVRILNQADKYP-----------AQLSGGQ 150
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLF-DTTVRENLRLA--------RPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 151 QQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGlARDGMTMICVTH 203
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
24-220 |
2.66e-30 |
|
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: 112.70 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFPhKTI 103
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK--SLRSMIGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLApmrvKGLSKADAEATARKyleRVRILNQADKYP-----------AQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:cd03254 94 MENIRLG----RPNATDEEVIEAAK---EAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 173 TSALDPEMVKEVLDTMIGLaRDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03254 167 TSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDD 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-220 |
3.35e-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: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWY-----GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVE-GTTLSD-SSRAI 81
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDmTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DA---VRREVGMVFQSFNLFPHKTIMENCT----------LAPMR------VKGLSKADAEAtarkylervrILnqaDKY 142
Cdd:TIGR03269 358 DGrgrAKRYIGILHQEYDLYPHRTVLDNLTeaiglelpdeLARMKavitlkMVGFDEEKAEE----------IL---DKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 143 PAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGlARDGM--TMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK-AREEMeqTFIIVSHDMDFVLDVCDRAALMRD 503
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
11-220 |
4.29e-30 |
|
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: 110.38 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHA--LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREV 88
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP--NELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPhKTIMENCtlapmrvkglskadaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03246 79 GYLPQDDELFS-GSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLED 170
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
5.27e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.97 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFN--LF 98
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN--IREVRKFVGLVFQNPDdqIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PhKTIMENCTLAPMRVkGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:PRK13652 93 S-PTVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150860720 179 EMVKEVLDTMIGLA-RDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13652 171 QGVKELIDFLNDLPeTYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-220 |
5.70e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.70 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVeGTTLsdssraidavrrEV 88
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSF-NLFPHKTIMENctlapmrVKGLSKADAEATARKYLErvRIL---NQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:COG0488 381 GYFDQHQeELDPDKTVLDE-------LRDGAPGGTEQEVRGYLG--RFLfsgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 165 KAMLFDEPTSALDPEMvKEVLDTmiGLAR-DGmTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG0488 452 NVLLLDEPTNHLDIET-LEALEE--ALDDfPG-TVLLVSHDRYFLDRVATRILEFED 504
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-220 |
5.99e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEkIV-LCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRRevGMVF-----QSFNL 97
Cdd:COG1129 266 GVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS-PRDAIRA--GIAYvpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 FPHKTIMENCTLAPMRVKG----LSKADAEATARKYLERVRIlnqadKYP------AQLSGGQQQRAAIARALCMEPKAM 167
Cdd:COG1129 342 VLDLSIRENITLASLDRLSrgglLDRRRERALAEEYIKRLRI-----KTPspeqpvGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 168 LFDEPTSALDpemV---KEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1129 417 ILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMRE 469
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-219 |
9.57e-30 |
|
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: 110.33 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCIN--HLEEIQEGKITVEGTTLSDssraiDAVRREVGMVFQSFNLFPHKTI 103
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK-----RSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MEncTL---APMRvkglskadaeatarkylervrilnqadkypaQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:cd03213 100 RE--TLmfaAKLR-------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 181 VKEVLDTMIGLARDGMTMICVTH----EMgFarQVADRVIFMS 219
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLS 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-218 |
1.01e-29 |
|
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: 111.42 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGA--FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREV 88
Cdd:cd03252 1 ITFEHVRFRYKPdgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA--WLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFpHKTIMENCTLA----PMR--VKGLSKADAEATARKYLERV-RILNQADkypAQLSGGQQQRAAIARALC 161
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNIALAdpgmSMErvIEAAKLAGAHDFISELPEGYdTIVGEQG---AGLSGGQRQRIAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 162 MEPKAMLFDEPTSALDPEMVKEVLDTMIGLArDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVM 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-218 |
1.89e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFpHKTIM 104
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA--SLRRNIAVVFQDAGLF-NRSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENctlapMRVkglSKADA-EATARKYLERVR----ILNQADKYPA-------QLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:PRK13657 427 DN-----IRV---GRPDAtDEEMRAAAERAQahdfIERKPDGYDTvvgergrQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 173 TSALDPEM---VKEVLDTMiglaRDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:PRK13657 499 TSALDVETeakVKAALDEL----MKGRTTFIIAHRLSTVRN-ADRILVF 542
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-246 |
5.17e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 110.57 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEI-----QEGKITVEGTTLSDSsRAID 82
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY-RDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AVRREVGMVFQSFNLFPhKTIMENcTLAPMRV-KGLSKADAEATARKYLERV----RILNQADKYPAQLSGGQQQRAAIA 157
Cdd:PRK14271 98 EFRRRVGMLFQRPNPFP-MSIMDN-VLAGVRAhKLVPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLArDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPK 237
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
....*....
gi 1150860720 238 HQRTRTFLG 246
Cdd:PRK14271 255 HAETARYVA 263
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
26-220 |
7.10e-29 |
|
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: 114.45 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFpHKTIME 105
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA--WLRRQMGVVLQENVLF-SRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLA--PMRVKGLSKADAEATARKYLERVR--ILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:TIGR01846 550 NIALCnpGAPFEHVIHAAKLAGAHDFISELPqgYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE 629
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 182 KEVLDTMIGLARdGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:TIGR01846 630 ALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEK 666
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-218 |
1.72e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 110.73 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 43 GPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAID--AVRREVGMVFQSFNLFPHKTIMENCTLapmrvkGLSKA 120
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClpPEKRRIGYVFQDARLFPHYKVRGNLRY------GMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 121 DAEatarKYLERVRILNQA---DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GM 196
Cdd:PRK11144 105 MVA----QFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNI 180
|
170 180
....*....|....*....|..
gi 1150860720 197 TMICVTHEMGFARQVADRVIFM 218
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVL 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
23-220 |
3.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.56 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAV---RREVGMVFQ--SFNL 97
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 FpHKTIMENCTLAPMRVKglskADAEATARKYLERVRILNQADKY----PAQLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:PRK13645 104 F-QETIEKDIAFGPVNLG----ENKQEAYKKVPELLKLVQLPEDYvkrsPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 174 SALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-220 |
3.94e-28 |
|
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: 105.59 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAiDAVRREVGMV---FQSFNLFPHK 101
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR-DAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLapmrvkglskadaeatarkylervrilnqadkyPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 182 KEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-220 |
4.28e-28 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.47 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssrAIDAVRREVGMVFQSFNLFpHKTI 103
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD---LEKALSSLISVLNQRPYLF-DTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTlapmrvkglskadaeatarkylervrilnqadkypAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKE 183
Cdd:cd03247 92 RNNLG-----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1150860720 184 VLDTMIGLARDgMTMICVTHEM-GFARqvADRVIFMSD 220
Cdd:cd03247 137 LLSLIFEVLKD-KTLIWITHHLtGIEH--MDKILFLEN 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-220 |
4.63e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.48 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAidavrREVGMVFQ--SFNLF 98
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvTKLPEYKRA-----KYIGRVFQdpMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMENCTLAPMRVK------GLSKADAEatarKYLERVRIL-----NQADKYPAQLSGGQQQraaiARALCM----E 163
Cdd:COG1101 95 PSMTIEENLALAYRRGKrrglrrGLTKKRRE----LFRELLATLglgleNRLDTKVGLLSGGQRQ----ALSLLMatltK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLD-TMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-248 |
5.02e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.87 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 1 MPQSAE--QAPLIALEGVGKwygAFH-------ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG 71
Cdd:PRK10261 1 MPHSDEldARDVLAVENLNI---AFMqeqqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 72 TTLSDSSRAI-------DAVRREV-----GMVFQS--FNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILN 137
Cdd:PRK10261 78 MLLRRRSRQVielseqsAAQMRHVrgadmAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 138 QA---DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVAD 213
Cdd:PRK10261 158 AQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIAD 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1150860720 214 RVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEI 248
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAV 272
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-220 |
2.45e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 109.49 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIdAVRREV 88
Cdd:PRK09700 4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL-AAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLAPMRVK---GLSKAD---AEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCM 162
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKkvcGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 163 EPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKD 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-245 |
2.75e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.41 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWY-----------GAFHALKNVNMTVRKGEKIVLCGPSGSGKST----LIRCINhleeiQEGK 66
Cdd:PRK15134 267 PLPEPASPLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 67 ITVEGTTLSD-SSRAIDAVRREVGMVFQSFN--LFPHKTIMEncTLAP-MRV--KGLSKADAEATARKYLERVRiLNQAD 140
Cdd:PRK15134 342 IWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQ--IIEEgLRVhqPTLSAAQREQQVIAVMEEVG-LDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 141 K--YPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIF 217
Cdd:PRK15134 419 RhrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250 260
....*....|....*....|....*...
gi 1150860720 218 MSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK15134 499 LRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
23-237 |
3.88e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 105.63 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR--AIDAVRREVGMVFQsfnlFPH 100
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLAPMRV--KGLSKADAEATARKYlervRIL-------NQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:PRK13646 96 SQLFEDTVEREIIFgpKNFKMNLDEVKNYAH----RLLmdlgfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLA-RDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPK 237
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-215 |
5.72e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidaVRRE 87
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH---ARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENcTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVREN-LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 168 LFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-220 |
1.24e-26 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 100.60 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVegttlsdssraidavrrevgm 90
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 vfqsfnlfphktiMENCTLApmrvkglskadaeatarkYLErvrilnqadkypaQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:cd03221 60 -------------GSTVKIG------------------YFE-------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARdgmTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELED 142
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
11-220 |
1.29e-26 |
|
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: 108.12 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYG--AFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREV 88
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD--VQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPhKTIMEN-CTLAPMRVKglskaDAEATARkyleRVRILNQADKYP-----------AQLSGGQQQRAAI 156
Cdd:TIGR03797 530 GVVLQNGRLMS-GSIFENiAGGAPLTLD-----EAWEAAR----MAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTmigLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRTQAIVSES---LERLKVTRIVIAHRLSTIRN-ADRIYVLDA 659
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-219 |
1.75e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 6 EQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVR 85
Cdd:PRK10247 3 ENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP--EIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFpHKTIMENCTLaPMRVKGlsKADAEATARKYLERVRI-LNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:PRK10247 81 QQVSYCAQTPTLF-GDTVYDNLIF-PWQIRN--QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMS 219
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKDEINH-ADKVITLQ 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-218 |
1.95e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.15 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIdaVR 85
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGHQI--AR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQSFNLFPHKTIMENCTLAPMR------VKGLSK------ADAEATARK--YLERVRILNQADKYPAQLSGGQQ 151
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIENLLVAQHQqlktglFSGLLKtpafrrAESEALDRAatWLERVGLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 152 QRAAIARALCMEPKAMLFDEPTSALDPEMVKEvLDTMIGLARD--GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKE-LDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVV 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-220 |
8.59e-26 |
|
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: 99.91 E-value: 8.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLE--EIQEGKITVEG---TTLSDSSRAidavRREVGMVFQSfnlfph 100
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGediTDLPPEERA----RLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 ktimenctlaPMRVKGLSKADaeatarkYLervRILNQAdkypaqLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:cd03217 86 ----------PPEIPGVKNAD-------FL---RYVNEG------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150860720 181 VKEVLDTMIGLARDGMTMICVTH-EMGFARQVADRVIFMSD 220
Cdd:cd03217 140 LRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYD 180
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-220 |
9.91e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 9.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDS-----SRAIDAVR 85
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTpsrelAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 REVGMVFQ-------SFNLFPHKtimenctlapmrvKG-LSKADAEATARkYLERVRILNQADKYPAQLSGGQQQRAAIA 157
Cdd:COG4604 82 QENHINSRltvrelvAFGRFPYS-------------KGrLTAEDREIIDE-AIAYLDLEDLADRYLDELSGGQRQRAFIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKD 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-216 |
1.20e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTT----LSDSSRAIDA----VRREVGMv 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayVPQRSEVPDSlpltVRDLVAM- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 92 fqsfNLFPHktimenctLAPMRVKGlskADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:NF040873 81 ----GRWAR--------RGLWRRLT---RDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVI 216
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-220 |
1.38e-25 |
|
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: 104.80 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFNLFpHKTIM 104
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT--LASLRRQVALVSQDVVLF-NDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLAPMRvkGLSKADAEATAR-KYLERVrilnqADKYP-----------AQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:TIGR02203 424 NNIAYGRTE--QADRAEIERALAaAYAQDF-----VDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 173 TSALDPEMVKEVLDTMIGLARdGMTMICVTHEMGfARQVADRVIFMSD 220
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ-GRTTLVIAHRLS-TIEKADRIVVMDD 542
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-219 |
1.97e-25 |
|
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: 99.65 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTL---IRCINHLEEIQEGKITVEGttlsdSSRAIDAVRREVGMVFQSFNLFPHKT 102
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNG-----QPRKPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLAP---MRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPE 179
Cdd:cd03234 98 VRETLTYTAilrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 180 MVKEVLDTMIGLARDGMTMICVTHEMG---FarQVADRVIFMS 219
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLS 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-248 |
2.71e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.61 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 4 SAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSR-AID 82
Cdd:PRK11831 1 EQSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsRLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 AVRREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCM 162
Cdd:PRK11831 81 TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 163 EPKAMLFDEPTSALDPeMVKEVLDTMIGLARD--GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEfFRDPKHQR 240
Cdd:PRK11831 161 EPDLIMFDEPFVGQDP-ITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPR 238
|
....*...
gi 1150860720 241 TRTFLGEI 248
Cdd:PRK11831 239 VRQFLDGI 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-218 |
6.93e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.88 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssraIDAV--RREVGMVFQSFNLFpHKTI 103
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ----YDHHylHRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MEN----CTLAPMrvkglskADAEATARKYLERVRILNQADKYP-------AQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:TIGR00958 572 RENiaygLTDTPD-------EEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1150860720 173 TSALDPEMVKEVLDTMiglARDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:TIGR00958 645 TSALDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVL 686
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-220 |
8.30e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 8.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRRE 87
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR--AASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQ----SFNlFPHKTIME-NCTLAPMRVKGLSKADaEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCM 162
Cdd:PRK09536 79 VASVPQdtslSFE-FDVRQVVEmGRTPHRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 163 EPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD 214
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-220 |
8.56e-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: 97.85 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 14 EGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaidavrREVGMVFQ 93
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL------HKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFNLFPHKTIMENctlapMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:TIGR03740 78 SPPLYENLTAREN-----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 174 SALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISE 199
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
9-214 |
1.20e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.03 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAiDAVRREV 88
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA-KIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENctlapmrvkgLSKADAEATARKYLERV--------RILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEEN----------LAMGGFFAERDQFQERIkwvyelfpRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 161 CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADR 214
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-216 |
1.22e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTlsdssraidavrrEVGMVF 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QSFNLFPHKTIMENCTLAPMRVKGLSKA-------------------------------DAEATARKYLERVRI-LNQAD 140
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFpEEDLD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 141 KYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK---EVLdtmigLARDGmTMICVTHEMGFARQVADRVI 216
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFL-----KNYPG-TVLVVSHDRYFLDRVATRIL 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-220 |
2.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.90 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQS-FNLFPHKTI 103
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN--FEKLRKHIGIVFQNpDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 -------MENctlapmrvKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:PRK13648 102 kydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 177 DPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK13648 174 DPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNK 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-203 |
3.13e-24 |
|
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: 101.05 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFpHKTIME 105
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA--SLRAAIGIVPQDTVLF-NDTIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMRVkGLSKADAEATARkyLERVR--ILNQADKYPAQ-------LSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:COG5265 451 N--IAYGRP-DASEEEVEAAAR--AAQIHdfIESLPDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
170 180
....*....|....*....|....*..
gi 1150860720 177 DPEMVKEVLDTMIGLARdGMTMICVTH 203
Cdd:COG5265 526 DSRTERAIQAALREVAR-GRTTLVIAH 551
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-245 |
3.97e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 28 NVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL-----EEIQEGKITVEGTTLSDSS-RAIDAVR-REVGMVFQS--FNLF 98
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASeQTLRGVRgNKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADK---YPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSA 175
Cdd:PRK15134 107 PLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 176 LDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFL 245
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-218 |
4.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 4.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdsSRAIDAVRREVGMVFQS-FNLFPHKTIM 104
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:PRK13642 101 DDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190
....*....|....*....|....*....|....*
gi 1150860720 185 LDTMIGLA-RDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:PRK13642 180 MRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVM 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-203 |
4.82e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 100.28 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 3 QSAEQAPLIALEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRA 80
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 81 idAVRREVGMVFQSFNLFPHkTIMENCTLApmrvkglsKADA-EATARKYLERV---RILNQADKYPA-------QLSGG 149
Cdd:PRK11160 411 --ALRQAISVVSQRVHLFSA-TLRDNLLLA--------APNAsDEALIEVLQQVgleKLLEDDKGLNAwlgeggrQLSGG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 150 QQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDgMTMICVTH 203
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-KTVLMITH 532
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-184 |
9.54e-24 |
|
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: 95.30 E-value: 9.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAidavRRE 87
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqdiTKLPMHKRA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENcTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:cd03218 77 IGYLPQEASIFRKLTVEEN-ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170
....*....|....*..
gi 1150860720 168 LFDEPTSALDPEMVKEV 184
Cdd:cd03218 156 LLDEPFAGVDPIAVQDI 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-219 |
1.59e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 99.04 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIdaVRREVGMVFQSFNLFPhKTIM 104
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT--LRQFINYLPQEPYIFS-GSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLAPMRvkGLSKADAEATarkyLERVRILNQADKYP-----------AQLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:TIGR01193 566 ENLLLGAKE--NVSQDEIWAA----CEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1150860720 174 SALDPEMVKEVLDTMIGLARDgmTMICVTHEMGFARQVaDRVIFMS 219
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLD 682
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-220 |
1.62e-23 |
|
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: 94.07 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCInhLEEIQ--EGKITVEGTtlsdssraidavrreVGMVFQS---FNLfp 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPGS---------------IAYVSQEpwiQNG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 hkTIMEN-CTLAPMrvkglskaDAEatarKYLERVR---------ILNQADKYP-----AQLSGGQQQRAAIARALCMEP 164
Cdd:cd03250 81 --TIRENiLFGKPF--------DEE----RYEKVIKacalepdleILPDGDLTEigekgINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMI-GLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPH-ADQIVVLDN 202
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-220 |
2.13e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaidavrREVGmvfQSFNLFP 99
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS------RQLA---RRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 -HKTIMENCTLAPMRVKG----------LSKADaEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAML 168
Cdd:PRK11231 83 qHHLTPEGITVRELVAYGrspwlslwgrLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 169 FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
26-220 |
3.40e-23 |
|
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: 97.90 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR--EELGRHIGYLPQDVELFD-GTIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctlapmrVKGLSKADAE---ATARkyleRVR----ILNQADKY-------PAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:COG4618 425 N-------IARFGDADPEkvvAAAK----LAGvhemILRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGfARQVADRVIFMSD 220
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRD 541
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
10-220 |
5.17e-23 |
|
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: 97.20 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIR--CINHLEEIQEGKITVEGTTLSDSSRAiDAVRRE 87
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLKASNIR-DTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 88 VGMVFQSFNLFPHKTIMENCTLA-PMRVKGLSKADAEATAR--KYLERVRILNQADKYP-AQLSGGQQQRAAIARALCME 163
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRakNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-245 |
6.30e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 95.19 E-value: 6.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKS----TLIRCINHLEEIQEGKITVEG---TTLSDSSRAiDAVRREVGMVFQ-- 93
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGqdlQRISEKERR-NLVGAEVAMIFQdp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 --SFNlfPHKT----IMEnctlaPMRV-KGLSKADAEATARKYLERVRILNQA---DKYPAQLSGGQQQRAAIARALCME 163
Cdd:PRK11022 99 mtSLN--PCYTvgfqIME-----AIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTR 242
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
...
gi 1150860720 243 TFL 245
Cdd:PRK11022 252 ALL 254
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-250 |
8.00e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 93.61 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 27 KNVNMTVRKGEKIVLCGPSGSGKStlIRCINHLEEIQEGKITVEGTTLSDSSR-AIDAVR-REVGMVFQ----SFNlfPH 100
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPvAPCALRgRKIATIMQnprsAFN--PL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTI----MENCtlapmrvKGLSKADAEATARKYLERV------RILnqaDKYPAQLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:PRK10418 96 HTMhthaRETC-------LALGKPADDATLTAALEAVglenaaRVL---KLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDPKHQRTRTFLGEIL 249
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHL 245
|
.
gi 1150860720 250 A 250
Cdd:PRK10418 246 A 246
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-178 |
1.29e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEkIV-LCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAidav 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHLPMHKRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENcTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:COG1137 77 RLGIGYLPQEASIFRKLTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170
....*....|....
gi 1150860720 165 KAMLFDEPTSALDP 178
Cdd:COG1137 156 KFILLDEPFAGVDP 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-220 |
1.46e-22 |
|
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: 96.02 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ--EGKI--------------------- 67
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 68 --TVEGTTL----------SDSSRAidAVRREVGMVFQ-SFNLFPHKTIMENcTLAPMRVKGLSKADAEATARKYLERVR 134
Cdd:TIGR03269 81 pcPVCGGTLepeevdfwnlSDKLRR--RIRKRIAIMLQrTFALYGDDTVLDN-VLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 135 ILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVAD 213
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSD 237
|
....*..
gi 1150860720 214 RVIFMSD 220
Cdd:TIGR03269 238 KAIWLEN 244
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
26-220 |
1.53e-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: 95.88 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--ETFGKHIGYLPQDVELFP-GTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctlapmrvkgLSKADAEATARKYLERVR-------ILNQADKYP-------AQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:TIGR01842 411 N----------IARFGENADPEKIIEAAKlagvhelILRLPDGYDtvigpggATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGfARQVADRVIFMSD 220
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQD 528
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-220 |
1.82e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIALEGVGKWY----------------------GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEG 65
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 66 KITVEGTT---LsdssraidavrrEVGMVFQsfnlfPHKTIMENCTLApMRVKGLSKADAEATAR---------KYLER- 132
Cdd:COG1134 82 RVEVNGRVsalL------------ELGAGFH-----PELTGRENIYLN-GRLLGLSRKEIDEKFDeivefaelgDFIDQp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 133 VRilnqadkypaQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVA 212
Cdd:COG1134 144 VK----------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLC 213
|
....*...
gi 1150860720 213 DRVIFMSD 220
Cdd:COG1134 214 DRAIWLEK 221
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-218 |
2.41e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFH-----ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRreVGMVFQ-- 93
Cdd:PRK15112 19 GWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQR--IRMIFQdp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFNLFPHKTIMENCTLaPMRVK-GLSKADAEATARKYLERVRIL-NQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:PRK15112 97 STSLNPRQRISQILDF-PLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 172 PTSALDPEMVKEVLDTMIGL-ARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVM 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-179 |
3.97e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.70 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSraIDAVRREVGMVFQSFNLFpHKTIM 104
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApmRVKGLSKADAEATARK--YLERVRILNQA-----DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:PRK11176 435 NNIAYA--RTEQYSREQIEEAARMayAMDFINKMDNGldtviGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
..
gi 1150860720 178 PE 179
Cdd:PRK11176 513 TE 514
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-218 |
4.91e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.87 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHL---EEIQEGKITVEGT-TLSDSSRAIDAVRRE-VGMVFQ-- 93
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGReILNLPEKELNKLRAEqISMIFQdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 --SFNlfPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRIlNQADK----YPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:PRK09473 107 mtSLN--PYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 168 LFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-220 |
6.22e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 6.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 27 KNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRREVGMVFQS---FNLFPHKTI 103
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS-PLDAVKKGMAYITESrrdNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLAPM----RVKGLSKADAEATARKYLERVRILNQ-----ADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PRK09700 359 AQNMAISRSlkdgGYKGAMGLFHEVDEQRTAENQRELLAlkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1150860720 175 ALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCE 484
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-218 |
8.61e-22 |
|
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: 90.22 E-value: 8.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIdaVRREVGMVFQSFNLFPhKTIME 105
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY--LHSKVSLVGQEPVLFA-RSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCT--LAPMRVKGLSKADAEATARKYLERVR--ILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:cd03248 107 NIAygLQSCSFECVKEAAQKAHAHSFISELAsgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150860720 182 KEVLDTMIGLARDgMTMICVTHEMGFARQvADRVIFM 218
Cdd:cd03248 187 QQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-220 |
9.33e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 9.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIR--CINHLEEIQEGKITVEGTTLSDSSRAiDAV 84
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvlSGVYPHGTYEGEIIFEGEELQASNIR-DTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATAR--KYLERVRI-LNQADKYpAQLSGGQQQRAAIARALC 161
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRaqKLLAQLKLdINPATPV-GNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 162 MEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRD 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
25-220 |
1.85e-21 |
|
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: 89.09 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREVGMVFQSFNLFPhKTIM 104
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGL--HDLRSRISIIPQDPVLFS-GTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENctLAPmrvkgLSKADaEATARKYLERV----RILNQADKYPA-------QLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:cd03244 96 SN--LDP-----FGEYS-DEELWQALERVglkeFVESLPGGLDTvveeggeNLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 174 SALDPE---MVKEVLDTmiglARDGMTMICVTHE----MGFarqvaDRVIFMSD 220
Cdd:cd03244 168 ASVDPEtdaLIQKTIRE----AFKDCTVLTIAHRldtiIDS-----DRILVLDK 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-203 |
8.80e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITV-EGTTLsdssraidavrrevgmvfqsfnLF-PHKTI 103
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlPQRPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLA-----PmrvkGLSKADAEATARKYLERVRI------LNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:COG4178 437 LPLGTLReallyP----ATAEAFSDAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|.
gi 1150860720 173 TSALDPEMVKEVLdTMIGLARDGMTMICVTH 203
Cdd:COG4178 513 TSALDEENEAALY-QLLREELPGTTVISVGH 542
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-205 |
1.31e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.36 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRR 86
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS-TTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 EVGMVFQSFNLFPHKTIMENCTLA--PMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150860720 165 KAMLFDEPTSALD-PEMvkEVLDTMIG-LARDGMTMICVTHEM 205
Cdd:PRK11288 160 RVIAFDEPTSSLSaREI--EQLFRVIReLRAEGRVILYVSHRM 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-220 |
1.91e-20 |
|
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: 86.43 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY----------------------GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKIT 68
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 69 VEGTtlsdssraIDAVrREVGMVFQsfnlfPHKTIMENCTLApMRVKGLSKADaeatARKYLERVRILNQADKY---P-A 144
Cdd:cd03220 81 VRGR--------VSSL-LGLGGGFN-----PELTGRENIYLN-GRLLGLSRKE----IDEKIDEIIEFSELGDFidlPvK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 145 QLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-220 |
2.20e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.72 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIrciNHLEEIQEGKITVEGTTLSDSsRAIDA--VRREVGMVFQSFNLFPHK 101
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNG-MPIDAkeMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTL-APMRVK-GLSKADAEATARKYLERVRILNQADK---YPAQ---LSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:TIGR00955 115 TVREHLMFqAHLRMPrRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 174 SALDPEMVKEVLDTMIGLARDGMTMICVTH-------EMgFarqvaDRVIFMSD 220
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAE 242
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-219 |
2.55e-20 |
|
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: 90.07 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlSDSSRAIDAVRREVGMVFQSFNLFPHKTIM 104
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENcTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:TIGR01257 1022 EH-ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*
gi 1150860720 185 LDTMIGLaRDGMTMICVTHEMGFARQVADRVIFMS 219
Cdd:TIGR01257 1101 WDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-215 |
3.32e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.08 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LE--GVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCIN--HLEEIQEGKITVEGTT-----LSDSSRaida 83
Cdd:NF040905 2 LEmrGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFDGEVcrfkdIRDSEA---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 vrreVGMVF--QSFNLFPHKTIMENCTLAPMRVKG--LSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARA 159
Cdd:NF040905 78 ----LGIVIihQELALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-220 |
4.40e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIrciNHLEEI--QEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFpHKTI 103
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGFlpYQGSLKINGIELRELDPE--SWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLApmrvkglsKADA-EATARKYLERVRILNQADKYP-----------AQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:PRK11174 440 RDNVLLG--------NPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMIcVTHEMGFARQVaDRVIFMSD 220
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLM-VTHQLEDLAQW-DQIWVMQD 558
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-220 |
1.33e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 20 YGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdsSRAIDAVRREVGMVFQSFNLFP 99
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 HKTIMENCTLA-----PMRVKgLSKADAEATARKyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PRK10253 95 DITVQELVARGryphqPLFTR-WRKEDEEAVTKA-MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 175 ALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALRE 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-220 |
1.85e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI--NHLEEIQEGKITVEGTTLSDSS---RAidavRREVGMVFQSfnlfph 100
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSpdeRA----RAGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 ktimenctlaPMRVKG------------------LSKADAEATARKYLERVRI--------LNqadkypAQLSGGQQQRA 154
Cdd:COG0396 86 ----------PVEIPGvsvsnflrtalnarrgeeLSAREFLKLLKEKMKELGLdedfldryVN------EGFSGGEKKRN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 155 AIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHemgFAR----QVADRVIFMSD 220
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVD 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-247 |
2.53e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.79 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 8 APLIAlEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG---TTLSDSSRAidav 84
Cdd:PRK10895 2 ATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDediSLLPLHARA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEP 164
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSDGEIIEEGPPEEFFRDpkHQRTRTF 244
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD--EHVKRVY 234
|
...
gi 1150860720 245 LGE 247
Cdd:PRK10895 235 LGE 237
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-203 |
3.90e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.70 E-value: 3.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCInhleeiqegkitvegttlsdssraidaVRREVGMVFQSFNLFPHKT 102
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL---------------------------AGALKGTPVAGCVDVPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLapmrVKGLSKADAEATARKYLERVRiLNQADKY---PAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPE 179
Cdd:COG2401 96 FGREASL----IDAIGRKGDFKDAVELLNAVG-LSDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*
gi 1150860720 180 MVKEVLDTMIGLARD-GMTMICVTH 203
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-203 |
4.80e-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: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKItvegttlsdssraidavrrevGMVFQSFNLF-PHKTIM 104
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------GMPEGEDLLFlPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLApmrvkglskadaEATArkylervrilnqadkYP--AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMvk 182
Cdd:cd03223 76 PLGTLR------------EQLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES-- 126
|
170 180
....*....|....*....|..
gi 1150860720 183 evLDTMIGLARD-GMTMICVTH 203
Cdd:cd03223 127 --EDRLYQLLKElGITVISVGH 146
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-215 |
1.42e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 10 LIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDAVRREVG 89
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSfnlfPHKTIME---NCTLApMRVKGLSKADAEATARkyLERVRILNQADKYPAQ----LSGGQQQRAAIARALCM 162
Cdd:PRK13638 81 TVFQD----PEQQIFYtdiDSDIA-FSLRNLGVPEAEITRR--VDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 163 EPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAV 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-219 |
1.47e-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: 81.61 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttLSDSSRAIDAVRReVGMVF-QSFNLFPHKTI 103
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKFLRR-IGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MEncTLAPMR-VKGLSKADAEATARKY---LERVRILNQadkyPA-QLSGGQQQRAAIARALCMEPKAMLFDEPTSALD- 177
Cdd:cd03267 113 ID--SFYLLAaIYDLPPARFKKRLDELselLDLEELLDT----PVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDv 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150860720 178 --PEMVKEVLDTmigLARD-GMTMICVTHEMGFARQVADRVIFMS 219
Cdd:cd03267 187 vaQENIRNFLKE---YNRErGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-218 |
1.64e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.11 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 28 NVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQ-EGKITVEGTTLsDSSRAIDAVRREVGMVFQS---FNLFPHKTI 103
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV-DIRNPAQAIRAGIAMVPEDrkrHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLAPM-RVKGLSKADAEATARKYLERVRILNQADKYP----AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:TIGR02633 357 GKNITLSVLkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
2.51e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 1 MPQS-AEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdssR 79
Cdd:PRK15439 1 MQTSdTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 80 AIDAVRREVG--MVFQSFNLFPHKTIMENCTLapmrvkGLSKAdaEATARKYLERVRILN---QADKYPAQLSGGQQQRA 154
Cdd:PRK15439 78 LTPAKAHQLGiyLVPQEPLLFPNLSVKENILF------GLPKR--QASMQKMKQLLAALGcqlDLDSSAGSLEVADRQIV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 155 AIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRD 215
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-218 |
3.10e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.61 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDssRAIDAVRREVGMVFQSFNLFPhKTIM 104
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLDSWRSRLAVVSQTPFLFS-DTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLA-PmrvkGLSKADAEATARkyLERVR--ILNQADKYPAQ-------LSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PRK10789 407 NNIALGrP----DATQQEIEHVAR--LASVHddILRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 175 ALDPEMVKEVLDTMiGLARDGMTMICVTHEMGfARQVADRVIFM 218
Cdd:PRK10789 481 AVDGRTEHQILHNL-RQWGEGRTVIISAHRLS-ALTEASEILVM 522
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-220 |
3.53e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.24 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRREVGMVF 92
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKS-SKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QSFNLFPHKTIMENCTLAPMRVKGLSkADAEataRKYLERVRILNQAD------KYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMF-VDQD---KMYRDTKAIFDELDididprAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRD 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-220 |
2.04e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEkIV-LCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidaVRREVGMVF-----QSFNLF 98
Cdd:COG3845 273 ALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR---ERRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMENCTL-----APMRVKG-LSKADAEATARKYLERVRILNQADKYPA-QLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:COG3845 349 PDMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-218 |
2.86e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.36 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 28 NVNMTVRKGEKIVLCGPSGSGKSTLIRCI-NHLEEIQEGKITVEGTTLSDSSRAiDAVRREVGMVFQS---FNLFPHKTI 103
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQ-QAIAQGIAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLAPM-RVKGLSKADAEA---TARKYLERVRILNQADKYP-AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:PRK13549 359 GKNITLAALdRFTGGSRIDDAAelkTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK13549 439 GAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-220 |
5.70e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHleEIQEGKITveGTTLSDSSRAIDAVRREVGMVFQSFNLFPHKTIME 105
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGNNFT--GTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 N---CTLapMRV-KGLSKADAEATARKYLERVRILN-----QADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:PLN03211 160 TlvfCSL--LRLpKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 177 DPEMVKEVLDTMIGLARDGMTMICVTHemgfarQVADRVIFMSD 220
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMH------QPSSRVYQMFD 275
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-220 |
9.60e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVEGTTLSDSSRAIDAVRREV---------GM-VFQSF 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYlsqqqsppfAMpVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 96 NLFPHktimenctlapmrvkglSKADAEATARKYLERVRILNQADKYP---AQLSGGQQQRAAIARALCM-------EPK 165
Cdd:COG4138 91 ALHQP-----------------AGASSEAVEQLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLLQvwptinpEGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 166 AMLFDEPTSALDpemV--KEVLDTMIG-LARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:COG4138 154 LLLLDEPMNSLD---VaqQAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-220 |
1.08e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 29 VNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRRevGMVF-----QSFNLFPHKTI 103
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS-PRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MEN----CTLAPMRVKGLSKADAEA-TARKYLERVRIlnqadKYPA------QLSGGQQQRAAIARALCMEPKAMLFDEP 172
Cdd:PRK11288 349 ADNinisARRHHLRAGCLINNRWEAeNADRFIRSLNI-----KTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 173 TSALDPEMVKEVLDTMIGLARDGMTMICVTHE----MGfarqVADRVIFMSD 220
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMRE 471
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-218 |
2.02e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAI 81
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-------QPV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DA----VRREVGMVFQSFNLFPHKTIMENCTL-ApmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAI 156
Cdd:NF033858 331 DAgdiaTRRRVGYMSQAFSLYGELTVRQNLELhA--RLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFArQVADRVIFM 218
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSReDGVTIFISTHFMNEA-ERCDRISLM 470
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-220 |
6.62e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 6.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAI---DAVRREVgMVFQSFNLFPHKT 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWiqnDSLRENI-LFGKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLAPmRVKGLSKADAEATARKYLervrilnqadkypaQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK 182
Cdd:TIGR00957 733 VLEACALLP-DLEILPSGDRTEIGEKGV--------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150860720 183 EVLDTMIG----LArdGMTMICVTHEMGFARQVaDRVIFMSD 220
Cdd:TIGR00957 798 HIFEHVIGpegvLK--NKTRILVTHGISYLPQV-DVIIVMSG 836
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
11-212 |
8.62e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.54 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSG--KSTLIRcinHLEEIQEGKITVEGTTLSDSSRAIdavRREV 88
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPA---HV*GPDAGRRPWRF*TWCANRRAL---RRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMvfqsfnlfpHKTIM----------ENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIAR 158
Cdd:NF000106 88 G*---------HRPVR*grresfsgrENLYMIG-R*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 159 ALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVA 212
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLA 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
25-220 |
1.13e-15 |
|
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: 73.22 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdsSRAIDAVRREVGMVFQSFNLFpHKTIM 104
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIS--TIPLEDLRSSLTIIPQDPTLF-SGTIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENctLAPMRvkglskadaEATARKYLERVRILNQADkypaQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:cd03369 100 SN--LDPFD---------EYSDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1150860720 185 LDTmIGLARDGMTMICVTHEMgfaRQVA--DRVIFMSD 220
Cdd:cd03369 165 QKT-IREEFTNSTILTIAHRL---RTIIdyDKILVMDA 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-220 |
2.17e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.01 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYG--AFhALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAVRREV 88
Cdd:PRK10522 323 LELRNVTFAYQdnGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP--EDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHktimencTLAPmrvKGlsKADAEATARKYLERV-----------RILNqadkypAQLSGGQQQRAAIA 157
Cdd:PRK10522 400 SAVFTDFHLFDQ-------LLGP---EG--KPANPALVEKWLERLkmahkleledgRISN------LKLSKGQKKRLALL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHYFIH-ADRLLEMRN 524
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
9-220 |
3.67e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS-----DSSRAida 83
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 vrrEVGMVFQSFNLFPHKTIMENCTLAPMRVKGLSKADAE---ATARKYLERVRILNQADKYPAQLSGGQQQRAAIARAL 160
Cdd:PRK10762 80 ---GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 161 CMEPKAMLFDEPTSAL-DPEmvKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTE--TESLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRD 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-203 |
5.46e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 5.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG--TTLSDSSRAI------DAVRrevgmvfqsfnl 97
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEAChylghrNAMK------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 fPHKTIMENCTL-ApmRVKGLSKADAEATarkyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:PRK13539 86 -PALTVAENLEFwA--AFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*...
gi 1150860720 177 DPEMVKEVLDTMIG-LARDGMtMICVTH 203
Cdd:PRK13539 159 DAAAVALFAELIRAhLAQGGI-VIAATH 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-177 |
1.29e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssraidavRREV 88
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------KLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPhktimencTLaPMRVK-------GLSKADAEATarkyLERVRILNQADKYPAQLSGGQQQRAAIARALC 161
Cdd:PRK09544 70 GYVPQKLYLDT--------TL-PLTVNrflrlrpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALL 136
|
170
....*....|....*.
gi 1150860720 162 MEPKAMLFDEPTSALD 177
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD 152
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-215 |
1.38e-14 |
|
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: 70.21 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSdssRAIDAVRREVGMVFQSFNLFPHKTIME 105
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD---FQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLapmrvkgLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVL 185
Cdd:cd03231 93 NLRF-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180 190
....*....|....*....|....*....|.
gi 1150860720 186 DTMIG-LARDGMTMICVTHEMGFARQVADRV 215
Cdd:cd03231 166 EAMAGhCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-220 |
3.35e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.96 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 32 TVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVEGTTLSDSSRAIDAVRRE---------VGM-VFQSFNLF-PH 100
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAylsqqqtppFAMpVFQYLTLHqPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTimenctlapmrvkglskadAEATARKYLERV-RILNQADKYP---AQLSGGQQQR---AA----IARALCMEPKAMLF 169
Cdd:PRK03695 97 KT-------------------RTEAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRvrlAAvvlqVWPDINPAGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 170 DEPTSALDPEMVKeVLDTMIG-LARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK03695 158 DEPMNSLDVAQQA-ALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
25-206 |
1.48e-13 |
|
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: 67.38 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTtlsDSSRAIDAVRREVGMVFQSFNLFPHKTIM 104
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT---PLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCT-LAPMRvkglskADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVkE 183
Cdd:TIGR01189 92 ENLHfWAAIH------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV-A 164
|
170 180
....*....|....*....|....*
gi 1150860720 184 VLDTMIG--LARDGMTMICVTHEMG 206
Cdd:TIGR01189 165 LLAGLLRahLARGGIVLLTTHQDLG 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-220 |
1.50e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALE---GVGkwygafhaLKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSS 78
Cdd:PRK15439 260 RQQAAGAPVLTVEdltGEG--------FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 79 RAIdavRREVGMVF-----QSFNLFPHKTIMEN-CTLAPMRVKGLSKADAEataRKYLERVRI-----LNQADKYPAQLS 147
Cdd:PRK15439 332 TAQ---RLARGLVYlpedrQSSGLYLDAPLAWNvCALTHNRRGFWIKPARE---NAVLERYRRalnikFNHAEQAARTLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 148 GGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK15439 406 GGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-216 |
1.54e-13 |
|
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: 68.20 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 18 KWYGAFHaLKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLS--------DSSRAIDAVRREVG 89
Cdd:cd03237 8 KTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFQSFNLFphKT-IMEnctlaPMRVKGLskadaeatarkYLERVRilnqadkypaQLSGGQQQRAAIARALCMEPKAML 168
Cdd:cd03237 87 KDFYTHPYF--KTeIAK-----PLQIEQI-----------LDREVP----------ELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 169 FDEPTSALDPE---MVKEVLDTMIGLARDgmTMICVTHEMGFARQVADRVI 216
Cdd:cd03237 139 LDEPSAYLDVEqrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLI 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-218 |
1.63e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAiDAVRRevGMVFQSFN-----LFPH 100
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQ-DGLAN--GIVYISEDrkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 KTIMENCTLAPMR----VKGLSKADAEATARKylERVRILNQadKYPAQ------LSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:PRK10762 345 MSVKENMSLTALRyfsrAGGSLKHADEQQAVS--DFIRLFNI--KTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-216 |
2.07e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.58 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIdavRREVGMVF----------- 92
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF---ARRIGVVFgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 --QSFNLfpHKTIMEnctlapmrvkgLSKADAEATARKYLErvrILNQADKY--PA-QLSGGQQQRAAIARALCMEPKAM 167
Cdd:COG4586 113 aiDSFRL--LKAIYR-----------IPDAEYKKRLDELVE---LLDLGELLdtPVrQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 168 LFDEPTSALDP---EMVKEVLDTMIglARDGMTMICVTHEMGFARQVADRVI 216
Cdd:COG4586 177 FLDEPTIGLDVvskEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVI 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-213 |
2.91e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 19 WYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaidavRREVGMVFQSFNL- 97
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ-----KNLVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 --FPhkTIMENCTL----APMRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDE 171
Cdd:PRK15056 91 wsFP--VLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVAD 213
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-218 |
3.16e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSsraIDAVRREVGMVFQSFNLFPHKTIM 104
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN---ISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLAPmRVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEV 184
Cdd:TIGR01257 2031 EHLYLYA-RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190
....*....|....*....|....*....|....
gi 1150860720 185 LDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:TIGR01257 2110 WNTIVSIIREGRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-203 |
6.66e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.85 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 30 NMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEgttlsdssraidavrREVGMVFqsfnlFPHKTIMENCTL 109
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------------AKGKLFY-----VPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 110 A-----PMRV-----KGLSKADAEatarKYLERVR---ILNQADKYPA------QLSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:TIGR00954 532 RdqiiyPDSSedmkrRGLSDKDLE----QILDNVQlthILEREGGWSAvqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....
gi 1150860720 171 EPTSALDPEMVkevlDTMIGLARD-GMTMICVTH 203
Cdd:TIGR00954 608 ECTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-220 |
6.68e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.82 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 15 GVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCInhLEEIQ--EGKITVEGTTLSDSSRAIDAVRR------ 86
Cdd:cd03290 6 GYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQtlEGKVHWSNKNESEPSFEATRSRNrysvay 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 87 ------------EVGMVFQS-FNLFPHKTIMENCTLAPmRVKGLSKADAEATARKYLervrilnqadkypaQLSGGQQQR 153
Cdd:cd03290 84 aaqkpwllnatvEENITFGSpFNKQRYKAVTDACSLQP-DIDLLPFGDQTEIGERGI--------------NLSGGQRQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150860720 154 AAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMI--GLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03290 149 ICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGIlkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKD 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-220 |
1.10e-12 |
|
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: 67.13 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWY------GAFHaLKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRaiDAV 84
Cdd:COG4615 328 LELRGVTYRYpgedgdEGFT-LGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR--EAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFPhktimenctlapmRVKGLSKADAEATARKYLERVRIlnqADKYPAQ--------LSGGQQQRAAI 156
Cdd:COG4615 405 RQLFSAVFSDFHLFD-------------RLLGLDGEADPARARELLERLEL---DHKVSVEdgrfsttdLSQGQRKRLAL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 157 ARALcMEPKA-MLFDEPTSALDP--------EMVKEvldtmigLARDGMTMICVTH-EMGFarQVADRVIFMSD 220
Cdd:COG4615 469 LVAL-LEDRPiLVFDEWAADQDPefrrvfytELLPE-------LKARGKTVIAISHdDRYF--DLADRVLKMDY 532
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-218 |
1.32e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVE-----GTTLSDSS----RAIdaVRREVGMV 91
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADrfrwnGIDLLKLSprerRKI--IGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 92 FQ--SFNLFPHKTIMENC--TLAPMRVKGL---SKADAEATARKYLERVRILNQAD---KYPAQLSGGQQQRAAIARALC 161
Cdd:COG4170 95 FQepSSCLDPSAKIGDQLieAIPSWTFKGKwwqRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 162 MEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR-DGMTMICVTHEMGFARQVADRVIFM 218
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-212 |
4.71e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 15 GVGKWYGA-FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKitvegttlsdssrAIDAVRREVGMVFQ 93
Cdd:TIGR03719 9 RVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFNLFPHKTIMENCTLAPMRVKGLSK-------------ADAEATARKYLERVRILNQADKY---------------P-- 143
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEIKDALDrfneisakyaepdADFDKLAAEQAELQEIIDAADAWdldsqleiamdalrcPpw 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 144 ----AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVkEVLDTMigLARDGMTMICVTHEMGFARQVA 212
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERH--LQEYPGTVVAVTHDRYFLDNVA 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-220 |
6.43e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRC-INHLEEIQEGKITVEGTTlsdssraidAVRREVGMVFQSfnlfphkTIM 104
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSV---------AYVPQVSWIFNA-------TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLAPMRVKGLSKADAEATARKY---LERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:PLN03232 697 ENILFGSDFESERYWRAIDVTALQHdldLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150860720 182 KEVLDTMIGLARDGMTMICVTHEMGFARQVaDRVIFMSD 220
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSE 814
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-203 |
7.73e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI-NHLE-EIQEGKITVEGTTLSDssraIDAVRREVGMVFQSFNLfphkti 103
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGHPAyKILEGDILFKGESILD----LEPEERAHLGIFLAFQY------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 menctlaPMRVKGLSKAD----AEATARKYLERVRI------------LNQADKYPAQL--------SGGQQQRAAIARA 159
Cdd:CHL00131 93 -------PIEIPGVSNADflrlAYNSKRKFQGLPELdplefleiinekLKLVGMDPSFLsrnvnegfSGGEKKRNEILQM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150860720 160 LCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTH 203
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-218 |
9.00e-12 |
|
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: 61.96 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRcinhleeiqegkitvEGTTLSDSSRAIDAVRRevgmvfqsfnLFPHKTI 103
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKARLISFLPK----------FSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENcTLAPMRVKGLSkadaeatarkYLERVRILNQadkypaqLSGGQQQRAAIARALCMEPKAMLF--DEPTSALDPEMV 181
Cdd:cd03238 64 FID-QLQFLIDVGLG----------YLTLGQKLST-------LSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150860720 182 KEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-204 |
9.68e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 9.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEE--IQEGKITVEGTTLSDSsraidaVRREVGMVFQSFNLFPHKTI 103
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKN------FQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MEnctlaPMRVKGLSKAdaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKE 183
Cdd:cd03232 97 RE-----ALRFSALLRG-------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 1150860720 184 VLDTMIGLARDGMTMICVTHE 204
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-207 |
9.85e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI---------NHLeeIQEGKITVEGT 72
Cdd:PRK10938 252 HALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDL--TLFGRRRGSGE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 73 TLSDssraidaVRREVGMVFQSFnlfpHKTIMENCTLAPMRVKG------LSKADAEAT---ARKYLERVRILNQADKYP 143
Cdd:PRK10938 330 TIWD-------IKKHIGYVSSSL----HLDYRVSTSVRNVILSGffdsigIYQAVSDRQqklAQQWLDILGIDKRTADAP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 144 AQ-LSGGQQQRAAIARALCMEPKAMLFDEPTSALDP---EMVKEVLDTMIGlarDGMTMI------------CVTHEMGF 207
Cdd:PRK10938 399 FHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETQLlfvshhaedapaCITHRLEF 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-220 |
1.19e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCInhLEEIqegkitvegTTLSDSSRAIdavRREVGMVFQSFNLFpHKTI 103
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGEL---------PPRSDASVVI---RGTVAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTL-APMRVKGLSKADAEATARKYLERV--RILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEM 180
Cdd:PLN03130 696 RDNILFgSPFDPERYERAIDVTALQHDLDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 181 VKEVLDTMIGLARDGMTMICVTHEMGFARQVaDRVIFMSD 220
Cdd:PLN03130 776 GRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHE 814
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-216 |
1.33e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSD-SSRAIdavRREVGMVFQSFNLFPHKTIM 104
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAF---ARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTLAPMRVKG-LSKADAEATAR--KYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMV 181
Cdd:PRK10575 104 ELVAIGRYPWHGaLGRFGAADREKveEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150860720 182 KEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVI 216
Cdd:PRK10575 184 VDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLV 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-213 |
2.62e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCInhLEEIQ--EGKITVeGTTLS----DSSRAIdavrrevgmvfqsfnLFP 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQadSGRIHC-GTKLEvayfDQHRAE---------------LDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 HKTIMENctLAPmrvkglSKADAEATARK-----YLE-------RVRILNQAdkypaqLSGGQQQRAAIARaLCMEPKAM 167
Cdd:PRK11147 397 EKTVMDN--LAE------GKQEVMVNGRPrhvlgYLQdflfhpkRAMTPVKA------LSGGERNRLLLAR-LFLKPSNL 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 168 L-FDEPTSALDP---EMVKEVLDTMIGlardgmTMICVTHEmgfaRQVAD 213
Cdd:PRK11147 462 LiLDEPTNDLDVetlELLEELLDSYQG------TVLLVSHD----RQFVD 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-216 |
4.42e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEgTTLSDSSRAIDAVRREVGMVF---------QSFN 96
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQDPPRNVEGTVYdfvaegieeQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 97 LFPHKTIMENCTLAPMRvKGLSKAdaeATARKYLE---------RVR-ILNQ----ADKYPAQLSGGQQQRAAIARALCM 162
Cdd:PRK11147 98 LKRYHDISHLVETDPSE-KNLNEL---AKLQEQLDhhnlwqlenRINeVLAQlgldPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 163 EPKAMLFDEPTSALDPEMVkEVLDTMIgLARDGmTMICVTHEMGFARQVADRVI 216
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETI-EWLEGFL-KTFQG-SIIFISHDRSFIRNMATRIV 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-220 |
6.20e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 25 ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSrAIDAVRREVGMVFQ---SFNLFPHK 101
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN-ANEAINHGFALVTEerrSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTLAPMR-----VKGLSKADAEATARKYLERVRIlnqadKYPAQ------LSGGQQQRAAIARALCMEPKAMLFD 170
Cdd:PRK10982 342 DIGFNSLISNIRnyknkVGLLDNSRMKSDTQWVIDSMRV-----KTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150860720 171 EPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 466
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-204 |
6.98e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINhlEEIQEGKITvEGTTLSDsSRAIDA-VRREVGMVFQSFNLFPHKTIM 104
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVN-GRPLDSsFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 ENCTL-APMRV-KGLSKADAEatarKYLERVRILNQADKYPAQLSG--------GQQQRAAIARALCMEPKAMLF-DEPT 173
Cdd:TIGR00956 855 ESLRFsAYLRQpKSVSKSEKM----EYVEEVIKLLEMESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLFlDEPT 930
|
170 180 190
....*....|....*....|....*....|.
gi 1150860720 174 SALDPEMVKEVLDTMIGLARDGMTMICVTHE 204
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQ 961
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-217 |
9.03e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.58 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 65 GKITVEGTTLSDSSraIDAVRREVGMVFQS---FNLFPHKTIM---ENCTLAPMRvkglsKADAEATARKYLERVRilNQ 138
Cdd:PTZ00265 1277 GKILLDGVDICDYN--LKDLRNLFSIVSQEpmlFNMSIYENIKfgkEDATREDVK-----RACKFAAIDEFIESLP--NK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 139 ADK----YPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLA-RDGMTMICVTHEMGFARQVAD 213
Cdd:PTZ00265 1348 YDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKRSDK 1427
|
....
gi 1150860720 214 RVIF 217
Cdd:PTZ00265 1428 IVVF 1431
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-177 |
9.55e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 9.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI-NHLEeiqeGKITVEGTTLSDSSRAIDAV---RREVGMVFQSFNLFPHK 101
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTE----GNVSVEGDIHYNGIPYKEFAekyPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 102 TIMEncTLapmrvkglskadaeatarkyleRVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:cd03233 99 TVRE--TL----------------------DFALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-220 |
1.52e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI--NHLEEIQEGKITVEGTTLSDSS--RAIDA---VRREVGMVFQSFNLF 98
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGARVTGDVTLNGEplAAIDAprlARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 P---HKTIMENCTLAPMRVKGLSKADAEaTARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCM---------EPKA 166
Cdd:PRK13547 97 AfsaREIVLLGRYPHARRAGALTHRDGE-IAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 167 MLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLAD 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-205 |
1.66e-10 |
|
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: 60.57 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 32 TVRKGEKIVLCGPSGSGKSTLIRCI------------------------------NHLEEIQEGKITVegttlSDSSRAI 81
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevlkrfrgtelqDYFKKLANGEIKV-----AHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DavrrevgmvfqsfnlfphktimenctLAPMRVKG-----LSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAI 156
Cdd:COG1245 170 D--------------------------LIPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAI 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 157 ARALCMEPKAMLFDEPTSALDpemVKE---VLDTMIGLARDGMTMICVTHEM 205
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-220 |
1.95e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 13 LEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKItvegtTLSDSSRaidavrreVGMVF 92
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSENAN--------IGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 Q-SFNLFPH-KTIMEncTLAPMRVKGlskaDAEATARKYLErvRILNQAD---KYPAQLSGGQQQRAAIARALCMEPKAM 167
Cdd:PRK15064 389 QdHAYDFENdLTLFD--WMSQWRQEG----DDEQAVRGTLG--RLLFSQDdikKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150860720 168 LFDEPTSALDPEMVkEVLDtmIGLARDGMTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK15064 461 VMDEPTNHMDMESI-ESLN--MALEKYEGTLIFVSHDREFVSSLATRIIEITP 510
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-218 |
2.20e-10 |
|
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: 60.69 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG--TTLSDSSRAIDAVRREVGMVFQSFNLFPHKTI 103
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGriSFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLApmrvkglskadaeatarkylERVRILNQADKYP-----AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:TIGR01271 522 IKACQLE--------------------EDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLL 620
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-205 |
2.21e-10 |
|
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: 60.73 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSsrAIDAVRREVGMVFQSFNLFPHKTIMe 105
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI--GLHDLRFKITIIPQDPVLFSGSLRM- 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 ncTLAPMRvkglSKADAEATARKYLERVR--ILNQADKYPAQ-------LSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:TIGR00957 1379 --NLDPFS----QYSDEEVWWALELAHLKtfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180
....*....|....*....|....*....
gi 1150860720 177 DPEmVKEVLDTMIGLARDGMTMICVTHEM 205
Cdd:TIGR00957 1453 DLE-TDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-178 |
2.22e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSsraidAVRREVG- 89
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA-----RHRRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 ----MVfQSF--NLFPHKTIMENctLAPM-RVKGLSKADAEATARKYLERVRILNQADKyPA-QLSGGQQQRAAIARALC 161
Cdd:NF033858 77 riayMP-QGLgkNLYPTLSVFEN--LDFFgRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALI 152
|
170
....*....|....*..
gi 1150860720 162 MEPKAMLFDEPTSALDP 178
Cdd:NF033858 153 HDPDLLILDEPTTGVDP 169
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
26-218 |
3.52e-10 |
|
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: 58.71 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEG--TTLSDSSRAIDAVRREVGMVFQSFNLFPHKTI 103
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGriSFSSQFSWIMPGTIKENIIFGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 104 MENCTLapmrvkglskadaEATARKYLERvrilnqaDKYP-----AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:cd03291 133 VKACQL-------------EEDITKFPEK-------DNTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFM 218
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILIL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
9-179 |
5.43e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidavrREV 88
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-----RFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQSFNLFPHKTIMENCTLapmrVKGLSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARaLCMEPKAM- 167
Cdd:PRK13543 85 AYLGHLPGLKADLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLw 159
|
170
....*....|..
gi 1150860720 168 LFDEPTSALDPE 179
Cdd:PRK13543 160 LLDEPYANLDLE 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-236 |
6.01e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 27 KNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGT-TLSDSSraIDAVRREVGMVFQSFNLFPHkTIME 105
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDIN--LKWWRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLAPMRVKGL------SKADAEAT--------------------------------ARKYLERVR------------- 134
Cdd:PTZ00265 479 NIKYSLYSLKDLealsnyYNEDGNDSqenknkrnscrakcagdlndmsnttdsnelieMRKNYQTIKdsevvdvskkvli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 135 ---ILNQADKY-------PAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPE---MVKEVLDTMIGlaRDGMTMICV 201
Cdd:PTZ00265 559 hdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG--NENRITIII 636
|
250 260 270
....*....|....*....|....*....|....*
gi 1150860720 202 THEMGFARqVADRVIFMSDGEIIEEGPPEEFFRDP 236
Cdd:PTZ00265 637 AHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
26-204 |
7.33e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsDSSRAidAVRREVGMVFQSFNLFPHKTIME 105
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLC--TYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCtlapmrvkgLSKADAEATARKYLERVRI--LNQADKYP-AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDpEMVK 182
Cdd:PRK13540 94 NC---------LYDIHFSPGAVGITELCRLfsLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD-ELSL 163
|
170 180
....*....|....*....|...
gi 1150860720 183 EVLDTMIGLAR-DGMTMICVTHE 204
Cdd:PRK13540 164 LTIITKIQEHRaKGGAVLLTSHQ 186
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-208 |
7.40e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALknvNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssRAIDAVRREvgmvFQSfNLF---- 98
Cdd:PRK13538 17 FSGL---SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDE----YHQ-DLLylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 -----PHKTIMENCTLApMRVKGLSKADAEATArkyLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPT 173
Cdd:PRK13538 82 qpgikTELTALENLRFY-QRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150860720 174 SALDPEMVKEVLDTMIG-LARDGMTMICVTHEMGFA 208
Cdd:PRK13538 158 TAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-177 |
1.18e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI----NHLEEIQEGKITVEGTTLSDSSRAIdavRREVGMVFQSFNLF 98
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHY---RGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 99 PHKTIMEN------CTLAPMRVKGLSKAD-----AEATARKY-LERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:TIGR00956 151 PHLTVGETldfaarCKTPQNRPDGVSREEyakhiADVYMATYgLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 1150860720 167 MLFDEPTSALD 177
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-205 |
1.19e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAidAVRREVGMVFQSFNLFPhKTIME 105
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS--VLRQGVAMVQQDPVVLA-DTFLA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTLApmrvKGLSkadaEATARKYLERVRILNQADKYPA-----------QLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PRK10790 434 NVTLG----RDIS----EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190
....*....|....*....|....*....|.
gi 1150860720 175 ALDpEMVKEVLDTMIGLARDGMTMICVTHEM 205
Cdd:PRK10790 506 NID-SGTEQAIQQALAAVREHTTLVVIAHRL 535
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-179 |
1.23e-09 |
|
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: 58.02 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVeGTTLsdssraidavrrEVGM 90
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 VFQSF-NLFPHKTIMENCT--LAPMRVkglskADAEATARKYLERVRILNQA-DKYPAQLSGGQQQRAAIARALCMEPKA 166
Cdd:TIGR03719 390 VDQSRdALDPNKTVWEEISggLDIIKL-----GKREIPSRAYVGRFNFKGSDqQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|...
gi 1150860720 167 MLFDEPTSALDPE 179
Cdd:TIGR03719 465 LLLDEPTNDLDVE 477
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-220 |
1.86e-09 |
|
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: 56.46 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsdSSRAIDAVRREVGMVFQS---------FN 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDI--SKLPLHTLRSRLSIILQDpilfsgsirFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 97 LFPHKTimenCTlapmrvkglskadaEATARKYLERVRILNQADKYPAQL-----------SGGQQQRAAIARALCMEPK 165
Cdd:cd03288 115 LDPECK----CT--------------DDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 166 AMLFDEPTSALDpeMVKE-VLDTMIGLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:cd03288 177 ILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSR 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-218 |
3.94e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVEGTTLSD------SSRAI-DAVRREVGMVFQ 93
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDidllrlSPRERrKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFN--LFPHKTIMENCTLA--PMRVKGLSKADAEATARKYLE---RVRILNQAD---KYPAQLSGGQQQRAAIARALCME 163
Cdd:PRK15093 97 EPQscLDPSERVGRQLMQNipGWTYKGRWWQRFGWRKRRAIEllhRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 164 PKAMLFDEPTSALDPEMVKEVLDTMIGLARD-GMTMICVTHEMGFARQVADRVIFM 218
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-177 |
4.68e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 32 TVRKGEKIVLCGPSGSGKSTLIRCI------------------------------NHLEEIQEGKITVegttlSDSSRAI 81
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlkrfrgtelqNYFKKLYNGEIKV-----VHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DavrrevgmvfqsfnlfphktimenctLAPMRVKG-----LSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAI 156
Cdd:PRK13409 170 D--------------------------LIPKVFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAI 223
|
170 180
....*....|....*....|.
gi 1150860720 157 ARALCMEPKAMLFDEPTSALD 177
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLD 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-205 |
1.01e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 21 GAFH-ALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdsSRAIDAVrrevgmvfqSFNLFP 99
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAI---------SSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 100 HKTIMENCTLAPMrVKGLSKADAEATARKYLERVRI---LNQADKypaQLSGGQQQRAAIARALCMEPKAMLFDEPTSAL 176
Cdd:PRK13545 99 QLTGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIgkfIYQPVK---TYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180
....*....|....*....|....*....
gi 1150860720 177 DPEMVKEVLDTMIGLARDGMTMICVTHEM 205
Cdd:PRK13545 175 DQTFTKKCLDKMNEFKEQGKTIFFISHSL 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-205 |
1.23e-08 |
|
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: 54.29 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 32 TVRKGEKIVLCGPSGSGKSTLIRcinhleeIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQsfNLFPH------KTIM- 104
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALK-------ILAGKLKPNLGKFDDPPDWDEILDEFRGSELQ--NYFTKllegdvKVIVk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 105 -ENCTLAPMRVKG-----LSKADAEATARKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:cd03236 93 pQYVDLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEM 205
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-217 |
1.26e-08 |
|
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: 52.38 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 35 KGEKIVLCGPSGSGKSTLIRCI-NHLEEIQEGKITVEGTTLsdssraidavrrevgmvfqsfnlfphktimenctlapmr 113
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI--------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 114 vkglskadaeataRKYLERVRILNQADKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLAR 193
Cdd:smart00382 42 -------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|
gi 1150860720 194 DGM------TMICVTHEMGFARQVADRVIF 217
Cdd:smart00382 109 LLLkseknlTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-216 |
1.75e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.42 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLI---------------------RCINHLEEIQEGKITVEGTTLS-DSSRAI 81
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAiDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 DAVRREVGMVFQSFN----LFPHKTIMEncTLAPMRVKGLSkadaeatarkYLERVRILNQadkypaqLSGGQQQRAAIA 157
Cdd:cd03270 89 RNPRSTVGTVTEIYDylrlLFARVGIRE--RLGFLVDVGLG----------YLTLSRSAPT-------LSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 158 RALCMEPKAML--FDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVI 216
Cdd:cd03270 150 TQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-212 |
1.82e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 15 GVGKWYGA-FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITV-EGTTlsdssraidavrreVGMVF 92
Cdd:PRK11819 11 RVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIK--------------VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 93 QSFNLFPHKTIMENCTLAPMRVKGLSK-------------ADAEATARKY--LERV----------RILNQA-------- 139
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEGVAEVKAALDrfneiyaayaepdADFDALAAEQgeLQEIidaadawdldSQLEIAmdalrcpp 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 140 -DKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVkEVLDTMigLARDGMTMICVTHEMGFARQVA 212
Cdd:PRK11819 157 wDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQF--LHDYPGTVVAVTHDRYFLDNVA 227
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
26-203 |
1.95e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLE--EIQEGKITVEG---TTLSDSSRAIDAVRrevgMVFQSfnlfph 100
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGkdlLELSPEDRAGEGIF----MAFQY------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 101 ktimenctlaPMRVKGLSKADAEATA----RKYL---------------ERVRILnqadKYPAQL---------SGGQQQ 152
Cdd:PRK09580 87 ----------PVEIPGVSNQFFLQTAlnavRSYRgqepldrfdfqdlmeEKIALL----KMPEDLltrsvnvgfSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 153 RAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTH 203
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-220 |
2.27e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEgttlsdssraidavrrevgmvfQSFNLFPHKTIME 105
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------------RSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NCTlapmrVKG-LSKADAEATARkyLERVRILNQADKYPAQL---------------SGGQQQRAAIARALCMEPKAMLF 169
Cdd:PTZ00243 734 NAT-----VRGnILFFDEEDAAR--LADAVRVSQLEADLAQLgggleteigekgvnlSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150860720 170 DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVIFMSD 220
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGD 856
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-178 |
4.09e-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: 53.76 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEiQEGKITVEGttLSDSSRAIDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFS-GTFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMRvkglSKADAEATarKYLERVRILNQADKYPAQ-----------LSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:TIGR01271 1311 N--LDPYE----QWSDEEIW--KVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
....
gi 1150860720 175 ALDP 178
Cdd:TIGR01271 1383 HLDP 1386
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
18-216 |
4.47e-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: 51.42 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 18 KWYGAFHALKNVNmTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLSDSSRAIDavrrevgmvfqsfnl 97
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 98 fphktimenctlapmrvkglskadaeatarkylervrilnqadkypaqLSGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:cd03222 72 ------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150860720 178 PEMVKEVLDTMIGLARDGM-TMICVTHEMGFARQVADRVI 216
Cdd:cd03222 104 IEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-177 |
1.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsdSSRAIDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFS-GTVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMrvkglsKADAEATARKYLERVRILNQADKYPAQL-----------SGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PLN03232 1329 N--IDPF------SEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
...
gi 1150860720 175 ALD 177
Cdd:PLN03232 1401 SVD 1403
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
7-218 |
1.29e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 7 QAPLIALEGVGKWY--GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsdSSRAIDAV 84
Cdd:PTZ00243 1305 QAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 85 RREVGMVFQSFNLFpHKTIMENctLAPMrvkgLSKADAEATARKYL----ERV---------RILNQADKYpaqlSGGQQ 151
Cdd:PTZ00243 1383 RRQFSMIPQDPVLF-DGTVRQN--VDPF----LEASSAEVWAALELvglrERVasesegidsRVLEGGSNY----SVGQR 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150860720 152 QRAAIARALCMEPKA-MLFDEPTSALDPEMVKEVLDTMIGlARDGMTMICVTHEMGFARQVaDRVIFM 218
Cdd:PTZ00243 1452 QLMCMARALLKKGSGfILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVM 1517
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-216 |
1.83e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 4 SAEQAPLIALEGVGKWYGAFHaLKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEgTTLSdssraida 83
Cdd:PRK13409 334 ESERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 84 vrrevgmvfqsfnlfpHKtimenctlaPMRVKglskADAEATARKYLERV--------------------RILnqaDKYP 143
Cdd:PRK13409 404 ----------------YK---------PQYIK----PDYDGTVEDLLRSItddlgssyykseiikplqleRLL---DKNV 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 144 AQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPE---MVKEVLDTMIglARDGMTMICVTHEMGFARQVADRVI 216
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIA--EEREATALVVDHDIYMIDYISDRLM 525
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-177 |
2.32e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI-------NHleeiqEGKITVEGT--TLSDSSRAIDA----V---RREVG 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrNI-----SGTVFKDGKevDVSTVSDAIDAglayVtedRKGYG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 90 MVFqsfnlfpHKTIMENCTLApmRVKGLSKA-----DAE-ATARKYLERVRIlnqadKYP------AQLSGGQQQRAAIA 157
Cdd:NF040905 351 LNL-------IDDIKRNITLA--NLGKVSRRgvideNEEiKVAEEYRKKMNI-----KTPsvfqkvGNLSGGNQQKVVLS 416
|
170 180
....*....|....*....|
gi 1150860720 158 RALCMEPKAMLFDEPTSALD 177
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID 436
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-216 |
3.39e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCI--------NHLEEIQEGKIT-VEGTTLSDSSRAIDavRREVGM---- 90
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalarrLHLKKEQPGNHDrIEGLEHIDKVIVID--QSPIGRtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 91 -------VFQSF-NLFphktiMENC--------TLApMRVKGLSKADA-EAT---ARKYLERV-RILNQAD-------KY 142
Cdd:cd03271 87 npatytgVFDEIrELF-----CEVCkgkrynreTLE-VRYKGKSIADVlDMTveeALEFFENIpKIARKLQtlcdvglGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 143 -----PA-QLSGGQQQRAAIARALCMEPKA---MLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARqVAD 213
Cdd:cd03271 161 iklgqPAtTLSGGEAQRIKLAKELSKRSTGktlYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CAD 239
|
...
gi 1150860720 214 RVI 216
Cdd:cd03271 240 WII 242
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
40-203 |
4.70e-07 |
|
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: 48.51 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 40 VLCGPSGSGKSTLIRCInhleeiqegkitvegttlsdssraidavrrEVGMVFQSFNLFPHKTIMENCTlapmrvkglsK 119
Cdd:cd03227 25 IITGPNGSGKSTILDAI------------------------------GLALGGAQSATRRRSGVKAGCI----------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 120 ADAEATArkYLERVrilnqadkypaQLSGGQQQRAAIARAL----CMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDG 195
Cdd:cd03227 65 AAVSAEL--IFTRL-----------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
....*...
gi 1150860720 196 MTMICVTH 203
Cdd:cd03227 132 AQVIVITH 139
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
26-205 |
5.40e-07 |
|
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: 49.47 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIqEGKITVEGttLSDSSRAIDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDG--VSWNSVPLQKWRKAFGVIPQKVFIFS-GTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMRvkglSKADAEATarKYLERVRILNQADKYPAQL-----------SGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:cd03289 96 N--LDPYG----KWSDEEIW--KVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190
....*....|....*....|....*....|.
gi 1150860720 175 ALDPeMVKEVLDTMIGLARDGMTMICVTHEM 205
Cdd:cd03289 168 HLDP-ITYQVIRKTLKQAFADCTVILSEHRI 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-216 |
1.39e-06 |
|
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: 48.63 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 32 TVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITvEGTTLS--------DSSRAIDAVRREVgmVFQSFNLFPHKT- 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISykpqyispDYDGTVEEFLRSA--NTDDFGSSYYKTe 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMEnctlaPMRVKglskadaeatarkylervRILnqaDKYPAQLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVK 182
Cdd:COG1245 439 IIK-----PLGLE------------------KLL---DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
170 180 190
....*....|....*....|....*....|....*
gi 1150860720 183 EVLDTMIGLARD-GMTMICVTHEMGFARQVADRVI 216
Cdd:COG1245 493 AVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-220 |
1.69e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 9 PLIALEGVGKWYGAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVegttlsdsSRAIdavrrEV 88
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------AKGI-----KL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 GMVFQsfnlfpHKTIMENCTLAPMR-VKGLSKADAEATARKYLERVRIlnQADKYP---AQLSGGQQQRAAIARALCMEP 164
Cdd:PRK10636 378 GYFAQ------HQLEFLRADESPLQhLARLAPQELEQKLRDYLGGFGF--QGDKVTeetRRFSGGEKARLVLALIVWQRP 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 165 KAMLFDEPTSALDPEMVKEVLDTMIGLarDGmTMICVTHEMGFARQVADRVIFMSD 220
Cdd:PRK10636 450 NLLLLDEPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHD 502
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-192 |
2.06e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.93 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 39 IVLCGPSGSGKSTLIRCI---------------NHLEEIQEGKITVEGT---------------TLSDSSRAIDAVRREv 88
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIryalygkarsrsklrSDLINVGSEEASVELEfehggkryrierrqgEFAEFLEAKPSERKE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 89 gMVFQSFNLFPHKTIMENctlAPMRVKGLSKADAEATARKYLERvRILNQADKY--PAQLSGGQQQRAAIARALcmepkA 166
Cdd:COG0419 105 -ALKRLLGLEIYEELKER---LKELEEALESALEELAELQKLKQ-EILAQLSGLdpIETLSGGERLRLALADLL-----S 174
|
170 180
....*....|....*....|....*.
gi 1150860720 167 MLFDepTSALDPEMVKEVLDTMIGLA 192
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEELA 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-177 |
3.02e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGTTLsdSSRAIDAVRREVGMVFQSFNLFPhKTIME 105
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFS-GTVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 106 NctLAPMRVKglSKADA-EATARKYLERVrILNQADKYPAQL-------SGGQQQRAAIARALCMEPKAMLFDEPTSALD 177
Cdd:PLN03130 1332 N--LDPFNEH--NDADLwESLERAHLKDV-IRRNSLGLDAEVseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-179 |
3.09e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 11 IALEGVGKWYGAFHALKNVNMTVRKGeKIV-LCGPSGSGKSTLIRCINHLEEIQEGKITVeGTT--LS--DSSRAidavr 85
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPG-GIVgIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETvkLAyvDQSRD----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 86 revgmvfqsfNLFPHKTIMENCT--LAPMRVkglskADAEATARKYLERVRiLNQAD--KYPAQLSGGQQQRAAIARALC 161
Cdd:PRK11819 398 ----------ALDPNKTVWEEISggLDIIKV-----GNREIPSRAYVGRFN-FKGGDqqKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 1150860720 162 MEPKAMLFDEPTSALDPE 179
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-52 |
4.26e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 4.26e-06
10 20
....*....|....*....|....*....
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTL 52
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-215 |
4.90e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 23 FHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGttlsdssraidavrrEVGMVFQSFNLFPHKT 102
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 103 IMENCTLApMRVKGLSKADAEATARKYLERVR----ILNQADKYpaqlSGGQQQRAAIARALCMEPKAMLFDEPTSALDP 178
Cdd:PRK13546 102 GIENIEFK-MLCMGFKRKEIKAMTPKIIEFSElgefIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150860720 179 EMVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRV 215
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKI 213
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-204 |
5.57e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIrcinhleEIQEGKIT---VEGTT-LSDSSRAIDAVRREVGMVFQSFNLFPHK 101
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLM-------DVLAGRKTggyIEGDIrISGFPKKQETFARISGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 102 TIMENCTL-APMRV-KGLSKADAEATARKYLERVRILNQADK---YPA--QLSGGQQQRAAIARALCMEPKAMLFDEPTS 174
Cdd:PLN03140 969 TVRESLIYsAFLRLpKEVSKEEKMMFVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|
gi 1150860720 175 ALDPEMVKEVLDTMIGLARDGMTMICVTHE 204
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-216 |
1.42e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINH--LEEIQEGKITVEGTTLS-------------------DSSRAID 82
Cdd:TIGR00630 622 NNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYpaLANRLNGAKTVPGRYTSieglehldkvihidqspigRTPRSNP 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 83 A----VRREVGMVFQ---------------SFNLfPH------------KTIM----------ENC--------TLApMR 113
Cdd:TIGR00630 702 AtytgVFDEIRELFAetpeakvrgytpgrfSFNV-KGgrceacqgdgviKIEMhflpdvyvpcEVCkgkrynreTLE-VK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 114 VKGLSKAD--------------AEATARKYLER--------VRiLNQadkyPA-QLSGGQQQRAAIARALCME---PKAM 167
Cdd:TIGR00630 780 YKGKNIADvldmtveeayeffeAVPSISRKLQTlcdvglgyIR-LGQ----PAtTLSGGEAQRIKLAKELSKRstgRTLY 854
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1150860720 168 LFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFARQvADRVI 216
Cdd:TIGR00630 855 ILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYII 902
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-218 |
2.65e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 31 MTVRKGEKIVLCGPSGSGKSTLIR-------------C-INHLE-EIQEGKITVEGTTLSDSSRAIDAVRREVGMVFQsf 95
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipknCqILHVEqEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQ-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 96 nlfpHKTIMENCTLAPMRVKGLSKADAEATARKYLERVRILNQADKYPA-----------------------QLSGGQQQ 152
Cdd:PLN03073 276 ----QRELEFETETGKGKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAearaasilaglsftpemqvkatkTFSGGWRM 351
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150860720 153 RAAIARALCMEPKAMLFDEPTSALDpemVKEVLDTMIGLARDGMTMICVTHEMGFARQVADRVIFM 218
Cdd:PLN03073 352 RIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
40-189 |
4.70e-05 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 42.44 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 40 VLCGPSGSGKSTLIRCInhLEEIQEGKITVEGTTlsdssRAIDAVRREVGMVFQSFNL--------FPHKTIMENCTLAP 111
Cdd:cd00882 1 VVVGRGGVGKSSLLNAL--LGGEVGEVSDVPGTT-----RDPDVYVKELDKGKVKLVLvdtpgldeFGGLGREELARLLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 112 MRVKGL----------SKADAEATARKYLERVRI-----LNQADKYPAQlsggQQQRAAIARALCMEPKAMLFdePTSAL 176
Cdd:cd00882 74 RGADLIllvvdstdreSEEDAKLLILRRLRKEGIpiilvGNKIDLLEER----EVEELLRLEELAKILGVPVF--EVSAK 147
|
170
....*....|...
gi 1150860720 177 DPEMVKEVLDTMI 189
Cdd:cd00882 148 TGEGVDELFEKLI 160
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
40-219 |
5.72e-05 |
|
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: 42.98 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 40 VLCGPSGSGKSTLIRCInhleeiqegKITVEGTtLSDSSRAIDAVRrevgmvfqsfnlfphKTIMENCTLA--PMRVKGL 117
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL---------KYALTGE-LPPNSKGGAHDP---------------KLIREGEVRAqvKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 118 SKADAEATaRKY--LERVRILNQAD------KYPAQLSGGQQQ------RAAIARALCMEPKAMLFDEPTSALDPEMVKE 183
Cdd:cd03240 81 NGKKYTIT-RSLaiLENVIFCHQGEsnwpllDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1150860720 184 VLDTMIGLAR--DGMTMICVTHEMGFaRQVADRVIFMS 219
Cdd:cd03240 160 SLAEIIEERKsqKNFQLIVITHDEEL-VDAADHIYRVE 196
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-216 |
8.58e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 144 AQLSGGQQQRAAIARALCMEPKAMLF--DEPTSALDPEMVKEVLDTMIGLARDGMTMICVTHEMGFArQVADRVI 216
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRII 548
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
24-216 |
1.39e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLIR-----CINHL-EEIQEGKITVEGTTLSD-----------SSRAI----- 81
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFiEQGFCSNLSIQWGAISRlvhitrdlpgrSQRSIpltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 82 ---DAVR---------REVGMV---FqSFNL----------FPHKTIMENCTLAP---------------MRVKGLSKAD 121
Cdd:PRK00635 689 kafDDLRelfaeqprsKRLGLTkshF-SFNTplgacaecqgLGSITTTDNRTSIPcpsclgkrflpqvleVRYKGKNIAD 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 122 A-EATARK----YLERVRILNQA--------DKYP-----AQLSGGQQQRAAIARALCM---EPKAMLFDEPTSALDPEM 180
Cdd:PRK00635 768 IlEMTAYEaekfFLDEPSIHEKIhalcslglDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*.
gi 1150860720 181 VKEVLDTMIGLARDGMTMICVTHEMGFARqVADRVI 216
Cdd:PRK00635 848 IKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
24-52 |
2.53e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.53e-04
10 20
....*....|....*....|....*....
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTL 52
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSSL 42
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-216 |
3.35e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 26 LKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINHLEEIQEGKITVEGT---------TLSDSSRAIDAV---RREVGMVFQ 93
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqeTPALPQPALEYVidgDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 94 SFNLFPHKtimeNCTLAPMRVKGlsKADA------EATARKYLERVRILNQADKYPAQ-LSGGQQQRAAIARALCMEPKA 166
Cdd:PRK10636 97 QLHDANER----NDGHAIATIHG--KLDAidawtiRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150860720 167 MLFDEPTSALDpemvkevLDTMIGLAR-----DGmTMICVTHEMGFARQVADRVI 216
Cdd:PRK10636 171 LLLDEPTNHLD-------LDAVIWLEKwlksyQG-TLILISHDRDFLDPIVDKII 217
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
147-220 |
3.94e-04 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 40.66 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 147 SGGQQQRAAIARALCMEPKAMLFDEPTSA-----LDPEM------VKEVLDTMIGLARD-----GMTMICVTHEMGFARQ 210
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMqalvskDKEPITPFVDRVRSlyddlGVSTILVVGGSGDYLD 238
|
90
....*....|
gi 1150860720 211 VADRVIFMSD 220
Cdd:pfam09818 239 VADTVILMDE 248
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
39-54 |
5.71e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 39.04 E-value: 5.71e-04
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
39-56 |
6.09e-04 |
|
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: 39.05 E-value: 6.09e-04
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
24-52 |
8.68e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 8.68e-04
10 20
....*....|....*....|....*....
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTL 52
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-204 |
9.76e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 2 PQSAEQAPLIALEGVGKWY-GAFHALKNVNMTVRKGEKIVLCGPSGSGKSTLIRCINhleeiqeGKITVEGTTLSDSSRA 80
Cdd:PLN03073 500 PDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GELQPSSGTVFRSAKV 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 81 IDAV--RREVGMVFQSFNlfPHKTIMENCTLAPmrvkglskadaEATARKYLERVRIL-NQADKYPAQLSGGQQQRAAIA 157
Cdd:PLN03073 573 RMAVfsQHHVDGLDLSSN--PLLYMMRCFPGVP-----------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFA 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150860720 158 RALCMEPKAMLFDEPTSALDPEMVkEVLDTMIGLARDGMTMicVTHE 204
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDAV-EALIQGLVLFQGGVLM--VSHD 683
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
143-203 |
1.47e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150860720 143 PAQLSGGQQQ---RAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICVTH 203
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
38-195 |
2.29e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 37.65 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 38 KIVLCGPSGSGKSTLIRcinhleEIQEGKITVEGTtlsDSSRAIDAVRREVGMVFQSFNL----FPhkTIMENCTLAPMR 113
Cdd:COG1100 5 KIVVVGTGGVGKTSLVN------RLVGDIFSLEKY---LSTNGVTIDKKELKLDGLDVDLviwdTP--GQDEFRETRQFY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150860720 114 VKGLSKADA---------------EATARKYLERVR-------ILNQADKYPAQlsgGQQQRAAIARALCMEPKAMLFde 171
Cdd:COG1100 74 ARQLTGASLylfvvdgtreetlqsLYELLESLRRLGkkspiilVLNKIDLYDEE---EIEDEERLKEALSEDNIVEVV-- 148
|
170 180
....*....|....*....|....
gi 1150860720 172 PTSALDPEMVKEVLDTMIGLARDG 195
Cdd:COG1100 149 ATSAKTGEGVEELFAALAEILRGE 172
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
39-89 |
2.63e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 2.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1150860720 39 IVLCGPSGSGKSTLIRCI-NHLEEIQEGKITVEGTTLSDSSRAIDAVRREVG 89
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLlEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALG 59
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
39-54 |
2.64e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 37.74 E-value: 2.64e-03
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
34-56 |
2.94e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.76 E-value: 2.94e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
35-59 |
3.07e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.76 E-value: 3.07e-03
10 20
....*....|....*....|....*
gi 1150860720 35 KGEKIVLCGPSGSGKSTLircINHL 59
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNAL 105
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
24-53 |
3.18e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.18e-03
10 20 30
....*....|....*....|....*....|
gi 1150860720 24 HALKNVNMTVRKGEKIVLCGPSGSGKSTLI 53
Cdd:COG0178 619 NNLKNVDVEIPLGVLTCVTGVSGSGKSTLV 648
|
|
| guanyl_kin |
TIGR03263 |
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ... |
39-73 |
4.00e-03 |
|
guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 213788 Cd Length: 179 Bit Score: 37.09 E-value: 4.00e-03
10 20 30
....*....|....*....|....*....|....*
gi 1150860720 39 IVLCGPSGSGKSTLIRCInhLEEIQEGKITVEGTT 73
Cdd:TIGR03263 3 IVISGPSGAGKSTLVKAL--LEEDPNLKFSISATT 35
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
35-59 |
5.24e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 5.24e-03
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
145-201 |
5.50e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 5.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 145 QLSGGQQQRAAIARALCMEPKAMLFDEPTSALDPEMVKEVLDTMIGLARDGMTMICV 201
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
39-61 |
5.71e-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: 5.71e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
145-215 |
6.24e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.85 E-value: 6.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150860720 145 QLSGGQQQRAAIARALCM---EPKAM-LFDEPTSALDPEMVKEVLDTMIGLArDGMTMICVTH--EMgfaRQVADRV 215
Cdd:cd03272 158 QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQYRTAVANMIKELS-DGAQFITTTFrpEL---LEVADKF 230
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
28-72 |
6.53e-03 |
|
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410885 [Multi-domain] Cd Length: 168 Bit Score: 36.60 E-value: 6.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1150860720 28 NVNMTVRKGEKIVLCGPSGSGKSTLIRCInhLEEI--QEGKITVEGT 72
Cdd:cd19477 2 AIKDGIAIGKNVIVCGGTGSGKTTYIKSI--LEFIpkEERIISIEDT 46
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
23-56 |
8.35e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 36.32 E-value: 8.35e-03
10 20 30
....*....|....*....|....*....|....
gi 1150860720 23 FHALKNVNMTVRKGeKIVLCGPSGSGKSTLIRCI 56
Cdd:pfam13476 6 FRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| |
