|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-240 |
3.96e-156 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 432.88 E-value: 3.96e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISldvekgevvviigpsgsgKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-215 |
2.94e-126 |
|
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: 356.07 E-value: 2.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIGM 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-240 |
1.02e-109 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 315.49 E-value: 1.02e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIG 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-241 |
1.73e-108 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 312.89 E-value: 1.73e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKT--------DMN 74
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelvpaDRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 75 ELRR---NIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARG 151
Cdd:COG4598 89 QLQRirtRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:COG4598 169 LAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
250
....*....|
gi 489402728 232 RARLFLSRVL 241
Cdd:COG4598 249 RLRQFLSSSL 258
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
3-241 |
7.73e-87 |
|
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: 257.84 E-value: 7.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKT----------- 71
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGrngplvpadek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMNELRRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARG 151
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQ 230
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 489402728 231 ERARLFLSRVL 241
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-243 |
6.29e-86 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 255.45 E-value: 6.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEV------HNKKTDMNEL 76
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslSQQKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLF 236
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
....*..
gi 489402728 237 LSRVLNH 243
Cdd:PRK11264 244 LEKFLLQ 250
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-243 |
7.48e-84 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 253.46 E-value: 7.48e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYY----GNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELR 77
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSltiekgeifgiigysgagKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPE 157
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 158 IMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLF 236
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
....*..
gi 489402728 237 LSRVLNH 243
Cdd:COG1135 241 LPTVLND 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-238 |
4.57e-82 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 245.31 E-value: 4.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEV----HNKKTDMNEL 76
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTpAQFFANPEQERARLF 236
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHY 239
|
..
gi 489402728 237 LS 238
Cdd:COG4161 240 LS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-238 |
1.82e-79 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 238.76 E-value: 1.82e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKT----DMNEL 76
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTpAQFFANPEQERARLF 236
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNY 239
|
..
gi 489402728 237 LS 238
Cdd:PRK11124 240 LS 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-241 |
1.36e-78 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 237.17 E-value: 1.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 7 NVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVH-----------NKKTDMNE 75
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANV-YPHQLSGGQQQRVAIARGLAM 154
Cdd:PRK10619 90 LRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERAR 234
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*..
gi 489402728 235 LFLSRVL 241
Cdd:PRK10619 250 QFLKGSL 256
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-238 |
2.23e-73 |
|
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: 223.33 E-value: 2.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITD-----GGLIVQNTEVHNKKTDMNEL 76
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPgvrieGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPhKTVLQNITLAPiKVNKV-SKEEAEKTAMFYLEKVGIPE----KANVYPHQLSGGQQQRVAIARG 151
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIkDKKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEK 237
|
....*..
gi 489402728 232 RARLFLS 238
Cdd:TIGR00972 238 RTEDYIS 244
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-229 |
5.11e-72 |
|
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: 219.37 E-value: 5.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN----FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNEL 76
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-242 |
2.64e-67 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 211.20 E-value: 2.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYY----GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELR 77
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPE 157
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 158 IMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLF 236
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*.
gi 489402728 237 LSRVLN 242
Cdd:PRK11153 241 IQSTLH 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-219 |
3.72e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 206.82 E-value: 3.72e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN----FQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNEL 76
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSlsieagefvaivgpsgsgKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RR-NIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFArEVADRILFMDDGQIIEDT 219
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSDE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
41-240 |
5.09e-67 |
|
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: 215.15 E-value: 5.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFY--LYPHKTVLQNITLAPIKVNKVSKEEAEKT 117
Cdd:COG1123 304 KSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRELRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRER 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:COG1123 384 VAELLERVGLPPDlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 196 EMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:COG1123 464 DLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-215 |
6.07e-65 |
|
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: 200.79 E-value: 6.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN----FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKK-TDMNELR 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 R-NIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREvADRILFMDDGQI 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
41-229 |
1.63e-64 |
|
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: 200.25 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQhfylYP-----HKTVLQNITLAPIkvN-KVSKEEA 114
Cdd:COG1122 40 KSTLLRLLNGLLKPTSGEVLVDGKDI--TKKNLRELRRKVGLVFQ----NPddqlfAPTVEEDVAFGPE--NlGLPREEI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVT 194
Cdd:COG1122 112 RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVT 191
|
170 180 190
....*....|....*....|....*....|....*
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:COG1122 192 HDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-237 |
2.26e-64 |
|
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: 200.21 E-value: 2.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNI 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSldvprgeilaiiggsgsgKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEqERARLFL 237
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQFL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-224 |
7.96e-64 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 199.13 E-value: 7.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNK-YYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEV-HNKKTDMNELRR 78
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSleiergefvaligpsgagKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPHKTVLQNI---------TLAPIkVNKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIA 149
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSL-LGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-228 |
1.64e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 201.87 E-value: 1.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTevhnkktDMNEL---RR 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSlsiepgefvallgpsgcgKTTLLRMIAGFETPDSGRILLDGR-------DVTGLppeKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEI 158
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAF-GLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 159 MLFDEPTSALDP----EMIGEVLDVMKTLakeGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG3842 157 LLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-223 |
1.18e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 195.27 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN-FQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNI 80
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSleiekgefvfltgpsgagKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-217 |
6.25e-62 |
|
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: 193.12 E-value: 6.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGM 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV----TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIE 217
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-226 |
8.21e-61 |
|
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: 191.18 E-value: 8.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVH-NKKTDMNELRRNIG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISgLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLaPIKVN-KVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFA 226
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
41-218 |
1.43e-60 |
|
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: 190.02 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRN-IGMVFQHFY--LYPHKTVLQNITLAPIKVNKVSKEEAEKT 117
Cdd:cd03257 44 KSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKeIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFY-LEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:cd03257 124 AVLLlLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFIT 203
|
170 180
....*....|....*....|....
gi 489402728 195 HEMGFAREVADRILFMDDGQIIED 218
Cdd:cd03257 204 HDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-224 |
1.78e-60 |
|
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: 190.08 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAI-----TDGGLIVQNTEVHNKKTDMNELR 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPhKTVLQNITLAP----IKVNKVSKEEAEKTamfyLEKVGIPE--KANVYPHQLSGGQQQRVAIARG 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLrlhgIKLKEELDERVEEA----LRKAALWDevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEgMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-224 |
2.17e-60 |
|
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: 190.09 E-value: 2.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNI 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNI------TLAPIKV--NKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGL 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgRRSTWRSlfGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 153 AMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
2.19e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 190.69 E-value: 2.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYY----GNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHnkktdmnEL 76
Cdd:COG1116 6 PALELRGVSKRFptggGGVTALDDVSltvaagefvalvgpsgcgKSTLLRLIAGLEKPTSGEVLVDGKPVT-------GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 157 EIMLFDEPTSALDP----EMIGEVLDVmktLAKEGMTMVVVTHEMgfaRE---VADRILFMDD--GQIIED 218
Cdd:COG1116 158 EVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDV---DEavfLADRVVVLSArpGRIVEE 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-214 |
1.28e-59 |
|
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: 185.85 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIGM 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLApikvnkvskeeaektamfylekvgipekanvyphqLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQ 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-224 |
5.01e-59 |
|
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: 186.74 E-value: 5.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN 79
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNI---------TLAPIkVNKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIAR 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSL-LGRFSEEDKER-ALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 151 GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
41-228 |
5.29e-59 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 191.08 E-value: 5.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN-IGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTA 118
Cdd:COG4175 66 KSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRRKkMSMVFQHFALLPHRTVLENVAF-GLEIQGVPKAERRERA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP----EMIGEVLDVMKTLAKegmTMVVVT 194
Cdd:COG4175 145 REALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKLKK---TIVFIT 221
|
170 180 190
....*....|....*....|....*....|....
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG4175 222 HDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
41-237 |
7.08e-59 |
|
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: 186.55 E-value: 7.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKktDMNELRRNIGMVFQHFY--LYPHKTVLQniTLA-PIKVNKVSKEEAEKT 117
Cdd:COG1124 44 KSTLLRALAGLERPWSGEVTFDGRPVTRR--RRKAFRRRVQMVFQDPYasLHPRHTVDR--ILAePLRIHGLPDREERIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMfyLEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:COG1124 120 EL--LEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSH 197
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 196 EMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFL 237
Cdd:COG1124 198 DLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELL 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
41-236 |
1.78e-58 |
|
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: 186.31 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN-IGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTA 118
Cdd:cd03294 63 KSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMVFQSFALLPHRTVLENVAF-GLEVQGVPRAEREERA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP----EMIGEVLDVMktlAKEGMTMVVVT 194
Cdd:cd03294 142 AEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrEMQDELLRLQ---AELQKTIVFIT 218
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLF 236
Cdd:cd03294 219 HDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-229 |
6.37e-58 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 187.28 E-value: 6.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAItDGGLIVQNTEVHNkkTDMNELRRNI 80
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSleiasgelvallgpsgsgKTTLLRIIAGLETP-DSGRIVLNGRDLF--TNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGL-RVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 161 FDEPTSALD----PEMIGEvldVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:COG1118 157 LDEPFGALDakvrKELRRW---LRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-237 |
7.47e-58 |
|
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: 183.66 E-value: 7.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIG 81
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI--REQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEK--ANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVP-KLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 160 LFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFL 237
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-228 |
1.55e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 186.43 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGM 82
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDldiedgeflvllgpsgcgKSTLLRMIAGLEDPTSGEILIGGRDV----TDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:COG3839 80 VFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 163 EPTSALDP----EMIGEVLDVMKTLakeGMTMVVVTHE----MGFarevADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG3839 159 EPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-238 |
1.26e-56 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 181.00 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQL-----EAITDGGLIVQNTEVHNKKTDMNELR 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINldipenkvtaligpsgcgKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPhKTVLQNITLAPiKVNKV-SKEEAEKTAMFYLEKVGIPE------KANVYphQLSGGQQQRVAIAR 150
Cdd:COG1117 92 RRVGMVFQKPNPFP-KSIYDNVAYGL-RLHGIkSKSELDEIVEESLRKAALWDevkdrlKKSAL--GLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 151 GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEgMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQ 230
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKD 246
|
....*...
gi 489402728 231 ERARLFLS 238
Cdd:COG1117 247 KRTEDYIT 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-224 |
3.81e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 3.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHnkkTDMNELRRNIGM 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSltvepgeifgllgpngagKTTTIRMLLGLLRPTSGEVRVLGEDVA---RDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-228 |
8.76e-56 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 180.29 E-value: 8.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQV-LKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIG 81
Cdd:COG1125 2 IEFENVTKRYPDGTVaVDDLSltipageftvlvgpsgcgKTTTLRMINRLIEPTSGRILIDGEDI--RDLDPVELRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEK--ANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVP-RLLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 160 LFDEPTSALDP----EMIGEVLDVMKTLAKegmTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG1125 159 LMDEPFGALDPitreQLQDELLRLQRELGK---TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANP 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
41-214 |
1.67e-55 |
|
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: 176.50 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHfylyP-----HKTVLQNITLAPiKVNKVSKEEAE 115
Cdd:cd03225 40 KSTLLRLLNGLLGPTSGEVLVDGKDL--TKLSLKELRRKVGLVFQN----PddqffGPTVEEEVAFGL-ENLGLPEEEIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH 195
Cdd:cd03225 113 ERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTH 192
|
170
....*....|....*....
gi 489402728 196 EMGFAREVADRILFMDDGQ 214
Cdd:cd03225 193 DLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-218 |
1.06e-53 |
|
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: 172.27 E-value: 1.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN----FQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVhnkktdmNELRR 78
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISlsveegefvalvgpsgcgKSTLLRIIAGLERPTSGEVLVDGEPV-------TGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEI 158
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 159 MLFDEPTSALDP---EMIGEVLdvMKTLAKEGMTMVVVTHEMGFAREVADRILFMD--DGQIIED 218
Cdd:cd03293 153 LLLDEPFSALDAltrEQLQEEL--LDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
41-228 |
1.43e-52 |
|
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: 172.55 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLE---AITDGGLIVQNTEVHN-KKTDMNELR-RNIGMVFQHFY--LYPHKTVLQNITLAPIKVNKVSKEE 113
Cdd:COG0444 44 KSTLARAILGLLpppGITSGEILFDGEDLLKlSEKELRKIRgREIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGLSKAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKANV---YPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMT 189
Cdd:COG0444 124 ARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLA 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 489402728 190 MVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG0444 204 ILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
41-239 |
8.49e-52 |
|
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: 175.48 E-value: 8.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQL---EAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHFY--LYPHkTVLQNITLApIKVNKVSKEEAE 115
Cdd:COG1123 45 KSTLALALMGLlphGGRISGEVLLDGRDL--LELSEALRGRRIGMVFQDPMtqLNPV-TVGDQIAEA-LENLGLSRAEAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:COG1123 121 ARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLIT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSR 239
Cdd:COG1123 201 HDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGA 245
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
41-229 |
3.40e-51 |
|
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: 167.63 E-value: 3.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEV-HNKKTDMNELRRNIGMVFQhfylYPHK-----TVLQNITLAPikVN-KVSKEE 113
Cdd:TIGR04521 44 KSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKKLKDLRKKVGLVFQ----FPEHqlfeeTVYKDIAFGP--KNlGLSEEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMV 191
Cdd:TIGR04521 118 AEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVI 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 192 VVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:TIGR04521 198 LVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-228 |
2.06e-50 |
|
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: 164.43 E-value: 2.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNI 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA----TDVPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLApIKVNKV----SKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFG-LRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-229 |
4.89e-50 |
|
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: 163.56 E-value: 4.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnelRRNIGM 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH----KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
2-214 |
1.69e-49 |
|
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: 161.26 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNK-YYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN 79
Cdd:TIGR02673 1 MIEFHNVSKaYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 160 LFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQ 214
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
41-240 |
2.65e-48 |
|
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: 162.71 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNK-KTDMNELRR-NIGMVFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTA 118
Cdd:TIGR01186 32 KSTTVRMLNRLIEPTAGQIFIDGENIMKQsPVELREVRRkKIGMVFQQFALFPHMTILQNTSLGP-ELLGWPEQERKEKA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP----EMIGEVLDVMKTLAKegmTMVVVT 194
Cdd:TIGR01186 111 LELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPlirdSMQDELKKLQATLQK---TIVFIT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:TIGR01186 188 HDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-215 |
2.75e-48 |
|
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: 158.19 E-value: 2.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGM 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
41-228 |
2.64e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 159.13 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEV-HNKKTDMNELRRNIGMVFQHFY--LYPHKTVLQnITLAPIKVNKV-SKEEAEK 116
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILFDGQDItGLSGRELRPLRRRMQMVFQDPYasLNPRMTVGD-IIAEPLRIHGLaSKAERRE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:COG4608 136 RVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFIS 215
|
170 180 190
....*....|....*....|....*....|....
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG4608 216 HDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-243 |
9.77e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 158.32 E-value: 9.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNI 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV----SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNI----TLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIafglTVLP-RRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARL 235
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235
|
....*...
gi 489402728 236 FLSRVlNH 243
Cdd:PRK10851 236 FMGEV-NR 242
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-228 |
2.39e-46 |
|
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: 157.51 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEaITDGGLIVQNTevhNKKTDMNELRRNIGM 82
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLE-RQTAGTIYQGG---RDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNIT--LAPIKVNKvsKEEAEKTAMFyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAygLKNRGMGR--AEVAERVAEL-LDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
41-229 |
7.81e-45 |
|
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: 151.04 E-value: 7.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTdMNELRRNIGMVFQHfylyPHK-----TV-------LQNItlapikvnK 108
Cdd:TIGR04520 41 KSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN-LWEIRKKVGMVFQN----PDNqfvgaTVeddvafgLENL--------G 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 109 VSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-G 187
Cdd:TIGR04520 108 VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeG 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 188 MTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:TIGR04520 188 ITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
41-239 |
6.29e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.59 E-value: 6.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA--P-IKVNKVSKEEAEKT 117
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVSMLFQENNLFPHLTVAQNIGLGlrPgLKLTAEQRAQVEQA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AmfylEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:COG3840 114 L----ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHD 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489402728 197 MGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSR 239
Cdd:COG3840 190 PEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLGI 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-231 |
1.39e-43 |
|
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: 149.57 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMF 120
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRAEIKPRVLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGF 199
Cdd:TIGR01187 84 ALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFVTHDQEE 163
|
170 180 190
....*....|....*....|....*....|..
gi 489402728 200 AREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:TIGR01187 164 AMTMSDRIAIMRKGKIAQIGTPEEIYEEPANL 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
41-222 |
4.69e-43 |
|
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: 145.27 E-value: 4.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNkktdMNE------LRRNIGMVFQHFYLYPHKTVLQNITLaPIKVnkVSKEEA 114
Cdd:COG4181 51 KSTLLGLLAGLDRPTSGTVRLAGQDLFA----LDEdararlRARHVGFVFQSFQLLPTLTALENVML-PLEL--AGRRDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVV 193
Cdd:COG4181 124 RARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLV 203
|
170 180
....*....|....*....|....*....
gi 489402728 194 THEMGFAREvADRILFMDDGQIIEDTTPA 222
Cdd:COG4181 204 THDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
41-229 |
8.42e-43 |
|
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: 144.89 E-value: 8.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKtdMNEL-RRNIGMVFQHFYLYPHKTVLQNITLA-------PIKVNKVSKE 112
Cdd:cd03219 39 KTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIaRLGIGRTFQIPRLFPELTVLENVMVAaqartgsGLLLARARRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 113 EAE--KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTM 190
Cdd:cd03219 117 EREarERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITV 196
|
170 180 190
....*....|....*....|....*....|....*....
gi 489402728 191 VVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:cd03219 197 LLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
41-223 |
1.20e-42 |
|
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: 145.19 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTdmNELRRNIGMVFQH----FYL----------YPHKTVLQnitlapikv 106
Cdd:COG1120 40 KSTLLRALAGLLKPSSGEVLLDGRDLASLSR--RELARRIAYVPQEppapFGLtvrelvalgrYPHLGLFG--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 107 nKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE 186
Cdd:COG1120 109 -RPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARE 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 187 -GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG1120 187 rGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-215 |
1.69e-42 |
|
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: 142.15 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNtevHNKKTDMNELRRNIGM 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISltvekgeiygllgpngagKTTLIKIILGLLKPDSGEIKVLG---KDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNItlapikvnkvskeeaektamfylekvgipekanvyphQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
41-215 |
2.09e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNkkTDMNELRRNIGMVFQHFYLYPhKTVLQNITLAP-IKVNKVSKEEAEKtam 119
Cdd:COG4619 39 KSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAYVPQEPALWG-GTVRDNLPFPFqLRERKFDRERALE--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 fYLEKVGIPE---KANVypHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:COG4619 113 -LLERLGLPPdilDKPV--ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSH 189
|
170 180
....*....|....*....|
gi 489402728 196 EMGFAREVADRILFMDDGQI 215
Cdd:COG4619 190 DPEQIERVADRVLTLEAGRL 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-215 |
2.85e-42 |
|
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: 142.93 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNI 80
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHemgfAREVAD----RILFMDDGQI 215
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH----AKELVDttrhRVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-241 |
3.89e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 143.83 E-value: 3.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQL-----EAITDGGLIVQNTEVHNKKTDMNELR 77
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPHKTVLQNITLApIKVNKV--SKEEAEKTAMFYLEKVG----IPEKANVYPHQLSGGQQQRVAIARG 151
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLvkSKKELDERVEWALKKAAlwdeVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEgMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHE 242
|
250
....*....|
gi 489402728 232 RARLFLSRVL 241
Cdd:PRK14267 243 LTEKYVTGAL 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-238 |
4.77e-42 |
|
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: 142.86 E-value: 4.77e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQvLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGM 82
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI----TNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLS 238
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
1.56e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.91 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVN-KYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNI 80
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHfylyPHK-----TVLQNITLAPIKVnKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK13639 81 GIVFQN----PDDqlfapTVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQ-ERAR 234
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETiRKAN 235
|
....*.
gi 489402728 235 LFLSRV 240
Cdd:PRK13639 236 LRLPRV 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
41-229 |
1.79e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 143.24 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKK--TDMNELRRNIGMVFQhfylYPH-----KTVLQNITLAPIKVNkVSKEE 113
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGTVTIGERVITAGKknKKLKPLRKKVGIVFQ----FPEhqlfeETVEKDICFGPMNFG-VSEED 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKA-NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMV 191
Cdd:PRK13634 121 AKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTV 200
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 192 VVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13634 201 LVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-243 |
3.30e-41 |
|
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: 141.15 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKtdmNELRRNIG 81
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP---REARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFAN-PEQERARLFLSRV 240
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEiGEENLEDAFVALI 236
|
...
gi 489402728 241 LNH 243
Cdd:COG4555 237 GSE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-239 |
3.80e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 144.32 E-value: 3.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIG 81
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI----THVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPeqerARLFLSR 239
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP----KNLFVAR 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
69-229 |
4.66e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 142.68 E-value: 4.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 69 KKTDMNELRRNIGMVFQ--HFYLYpHKTVLQNITLAPIKVnKVSKEEAEKTAMFYLEKVGIPEK-ANVYPHQLSGGQQQR 145
Cdd:PRK13631 107 KIKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 146 VAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFF 225
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
....
gi 489402728 226 ANPE 229
Cdd:PRK13631 265 TDQH 268
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-216 |
7.64e-41 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 139.35 E-value: 7.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAItDGGLIVQNTEV---HNKKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA-PIKVNKVSKEEAEK 116
Cdd:cd03297 36 KSTLLRCIAGLEKP-DGGTIVLNGTVlfdSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGlKRKRNREDRISVDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:cd03297 115 L----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTH 190
|
170 180
....*....|....*....|.
gi 489402728 196 EMGFAREVADRILFMDDGQII 216
Cdd:cd03297 191 DLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_arch_GlcV |
NF040933 |
glucose ABC transporter ATP-binding protein GlcV; |
41-236 |
1.02e-40 |
|
glucose ABC transporter ATP-binding protein GlcV;
Pssm-ID: 468866 [Multi-domain] Cd Length: 357 Bit Score: 142.83 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEV-HNKKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAM 119
Cdd:NF040933 45 KTTFLRIIAGLEVPTDGEIYFDDKLVaSPGKIIVPPEDRNIGMVFQNWALYPNMTVFDNIAF-PLKIKKVPKDEIEKKVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemiGEVLDVMKTLAKE-----GMTMVVVT 194
Cdd:NF040933 124 EVAEILGISEVLDRYPRELSGGQQQRVALARALVKNPQVLLLDEPFSNLD----ARIRDSARALVKKiqrelKITTIIVS 199
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQER-ARLF 236
Cdd:NF040933 200 HDPADIFSLADRAGVINNGKFQQVGKPEEIYDNPANIFvARLI 242
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-210 |
2.02e-40 |
|
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: 137.75 E-value: 2.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 7 NVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTE---VHNKKTdmNELRRN-IGM 82
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKA--SKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFArEVADRILFM 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-238 |
3.06e-40 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 138.76 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQL-----EAITDGGLIVQNTEVHNKKTDMNEL 76
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYP---HKTVLQNITLAPIKVNKVSKEEAEKTamfyLEKVGIPEKANVYPHQ----LSGGQQQRVAIA 149
Cdd:PRK14239 85 RKEIGMVFQQPNPFPmsiYENVVYGLRLKGIKDKQVLDEAVEKS----LKGASIWDEVKDRLHDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*....
gi 489402728 230 QERARLFLS 238
Cdd:PRK14239 240 HKETEDYIS 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
72-230 |
4.95e-40 |
|
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: 144.44 E-value: 4.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMNELR-RNIGMVFQH--FYLYPHKTVLQNITlAPIKVNK-VSKEEAEKTAMFYLEKVGIPE---KANVYPHQLSGGQQQ 144
Cdd:COG4172 85 ELRRIRgNRIAMIFQEpmTSLNPLHTIGKQIA-EVLRLHRgLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTL-AKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
....*..
gi 489402728 224 FFANPEQ 230
Cdd:COG4172 244 LFAAPQH 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
41-231 |
1.10e-39 |
|
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: 143.29 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAiTDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFY--LYPHKTVLQNITlAPIKVNKV--SKEEAE 115
Cdd:COG4172 325 KSTLGLALLRLIP-SEGEIRFDGQDLDGlSRRALRPLRRRMQVVFQDPFgsLSPRMTVGQIIA-EGLRVHGPglSAAERR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVV 193
Cdd:COG4172 403 ARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFI 482
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 194 THEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:COG4172 483 SHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHP 520
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-238 |
3.06e-39 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 136.45 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLE-----AITDGGLIVQNTEVHNKKTDMNEL 76
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPhKTVLQNITLAPiKVNKVSK------EEAEKTAMFYLEkvgIPEKANVYPHQLSGGQQQRVAIAR 150
Cdd:PRK14243 90 RRRIGMVFQKPNPFP-KSIYDNIAYGA-RINGYKGdmdelvERSLRQAALWDE---VKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 151 GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGFAREVADRILFMD---------DGQIIEDTTP 221
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRT 243
|
250
....*....|....*..
gi 489402728 222 AQFFANPEQERARLFLS 238
Cdd:PRK14243 244 EKIFNSPQQQATRDYVS 260
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
41-238 |
3.57e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.17 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEV-HNKKTDMNELRRNIGMVFQHFY--LYPHKTVLQnITLAPIKVN-KVSKEE-AE 115
Cdd:PRK11308 54 KSTLARLLTMIETPTGGELYYQGQDLlKADPEAQKLLRQKIQIVFQNPYgsLNPRKKVGQ-ILEEPLLINtSLSAAErRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KT-AMfyLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVV 192
Cdd:PRK11308 133 KAlAM--MAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVF 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489402728 193 VTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLS 238
Cdd:PRK11308 211 ISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
41-239 |
8.31e-39 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 138.20 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCIN---QLEAITdGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKT 117
Cdd:TIGR03258 44 KTTLLRAIAgfvKAAGLT-GRIAIADRDL----THAPPHKRGLALLFQNYALFPHLKVEDNVAFG-LRAQKMPKADIAER 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE--GMTMVVVTH 195
Cdd:TIGR03258 118 VADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElpELTILCVTH 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489402728 196 EMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSR 239
Cdd:TIGR03258 198 DQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGA 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-231 |
1.09e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 134.66 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQL-----EAITDGGLIVQNTEVHnkKTDMNELR 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPHKTVLQNITLAPiKVNKV--SKEEAEKTAMFYLEKVG----IPEKANVYPHQLSGGQQQRVAIARG 151
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALGL-KLNRLvkSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEgMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
41-225 |
2.89e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 134.49 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEV--HNKKTDMNELRRNIGMVFQhfylYPH-----KTVLQNITLAPIKVNkVSKEE 113
Cdd:PRK13649 46 KSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQ----FPEsqlfeETVLKDVAFGPQNFG-VSQEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKA-NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVV 192
Cdd:PRK13649 121 AEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL 200
|
170 180 190
....*....|....*....|....*....|...
gi 489402728 193 VTHEMGFAREVADRILFMDDGQIIEDTTPAQFF 225
Cdd:PRK13649 201 VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
41-229 |
1.03e-37 |
|
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: 132.47 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnEL-RRNIGMVFQHFYLYPHKTVLQNITLA------------PIKVN 107
Cdd:COG0411 43 KTTLFNLITGFYRPTSGRILFDGRDITGLPPH--RIaRLGIARTFQNPRLFPELTVLENVLVAaharlgrgllaaLLRLP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 108 KVSKEEAE--KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAK 185
Cdd:COG0411 121 RARREEREarERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRD 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 186 E-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:COG0411 201 ErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
59-218 |
1.46e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 133.29 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 59 LIVQNTEVHNKKtDMNELRRNIGMVFQhFYLYP--HKTVLQNITLAPIKVNkVSKEEAEKTAMFYLEKVGIPEKanvY-- 134
Cdd:PRK13651 87 LVIQKTRFKKIK-KIKEIRRRVGVVFQ-FAEYQlfEQTIEKDIIFGPVSMG-VSKEEAKKRAAKYIELVGLDES---Ylq 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 135 --PHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDD 212
Cdd:PRK13651 161 rsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*.
gi 489402728 213 GQIIED 218
Cdd:PRK13651 241 GKIIKD 246
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
2.48e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGglivqntEVHNKKTDMNELRRNI 80
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSltippgefvaivgpngagKSTLLKAILGLLPPTSG-------TVRLFGKPPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHF----------------YLYPHKTVLQNITlapikvnKVSKEEAEKTamfyLEKVGIPEKANVYPHQLSGGQQQ 144
Cdd:COG1121 78 GYVPQRAevdwdfpitvrdvvlmGRYGRRGLFRRPS-------RADREAVDEA----LERVGLEDLADRPIGELSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDtTPAQF 224
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG-PPEEV 225
|
250
....*....|....*....
gi 489402728 225 FANPEQERARLFLSRVLNH 243
Cdd:COG1121 226 LTPENLSRAYGGPVALLAH 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-243 |
6.18e-37 |
|
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: 132.92 E-value: 6.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAiTDGGLIVQNTEV---HNKKTDMNELRRNIGMVFQHFYLYPHKTVLQNITL----APIKVNKVSKEE 113
Cdd:COG4148 38 KTTLLRAIAGLER-PDSGRIRLGGEVlqdSARGIFLPPHRRRIGYVFQEARLFPHLSVRGNLLYgrkrAPRAERRISFDE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AektamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVV 192
Cdd:COG4148 117 V-------VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDElDIPILY 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 193 VTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP-------EQERARLFLSRVLNH 243
Cdd:COG4148 190 VSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPdllplagGEEAGSVLEATVAAH 247
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-215 |
7.72e-37 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 132.85 E-value: 7.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 5 FRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEvhnkktdMNEL---RRNIG 81
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-------MNDVppaERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 162 DEPTSALDP----EMIGEVLDVMKTLakeGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK11000 158 DEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-240 |
1.26e-36 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 132.65 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIG 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL----SHVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 162 DEPTSALDPE----MIGEVLDVmktLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFL 237
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
...
gi 489402728 238 SRV 240
Cdd:PRK11607 251 GSV 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-229 |
1.81e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYG-----NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQ----NTEVHNKkt 71
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMNELRRNIGMVFQhfylYPH-----KTVLQNITLAPIKVNkVSKEEAEKTAMFYLEKVGIPEK-ANVYPHQLSGGQQQR 145
Cdd:PRK13641 79 NLKKLRKKVSLVFQ----FPEaqlfeNTVLKDVEFGPKNFG-FSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 146 VAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFF 225
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
....
gi 489402728 226 ANPE 229
Cdd:PRK13641 234 SDKE 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
40-229 |
5.59e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.63 E-value: 5.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 40 GKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIGMVFQhfylYP-----HKTVLQNITLAPIKVNkVSKEEA 114
Cdd:PRK13637 45 GKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQ----YPeyqlfEETIEKDIAFGPINLG-LSEEEI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVGIP--EKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMV 191
Cdd:PRK13637 120 ENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTII 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 192 VVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13637 200 LVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
41-223 |
6.54e-36 |
|
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: 134.19 E-value: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHFYLYpHKTVLQNITLApikVNKVSKEEAEKTAmf 120
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDL--RQIDPASLRRQIGVVLQDVFLF-SGTIRENITLG---DPDATDEEIIEAA-- 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 ylEKVGIPEKANVYPH-----------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMT 189
Cdd:COG2274 586 --RLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRT 662
|
170 180 190
....*....|....*....|....*....|....
gi 489402728 190 MVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQ 223
Cdd:COG2274 663 VIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
41-214 |
6.96e-36 |
|
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: 124.66 E-value: 6.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRNIGMVFQhfylyphktvlqnitlapikvnkvskeeaektamf 120
Cdd:cd00267 38 KSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE--ELRRRIGYVPQ----------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 ylekvgipekanvyphqLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFA 200
Cdd:cd00267 81 -----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELA 143
|
170
....*....|....
gi 489402728 201 REVADRILFMDDGQ 214
Cdd:cd00267 144 ELAADRVIVLKDGK 157
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
41-215 |
9.02e-36 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 126.37 E-value: 9.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN-IGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTA 118
Cdd:NF038007 44 KSTLLNIIGMFDSLDSGSLTLAGKEVTNlSYSQKIILRRElIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMG 198
Cdd:NF038007 123 NQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDE 202
|
170
....*....|....*..
gi 489402728 199 fAREVADRILFMDDGQI 215
Cdd:NF038007 203 -ASTYGNRIINMKDGKL 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-218 |
1.10e-35 |
|
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: 125.68 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA--P-IKVNKVSKEEAEKT 117
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLINGVDV----TAAPPADRPVSMLFQENNLFAHLTVEQNVGLGlsPgLKLTAEDRQAIEVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 amfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:cd03298 113 ----LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQ 188
|
170 180
....*....|....*....|..
gi 489402728 197 MGFAREVADRILFMDDGQIIED 218
Cdd:cd03298 189 PEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-227 |
1.36e-35 |
|
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: 126.01 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMnELRRNIGM 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTAMF-YLEkvgipEKANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGayARRRAKRKARLERVYELFpRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 160 LFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFAN 227
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
41-240 |
1.57e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.15 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN-IGMVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTA 118
Cdd:PRK10070 67 KSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFALMPHMTVLDNTAFG-MELAGINAEERREKA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD-VMKTLAKEGMTMVVVTHEM 197
Cdd:PRK10070 146 LDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDeLVKLQAKHQRTIVFISHDL 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489402728 198 GFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:PRK10070 226 DEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
41-216 |
3.32e-35 |
|
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: 124.29 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVqntevHNKKTDMNELRRNIGMVFQH--FYLYpHKTVLQNITLApikvNKVSKEEAEKTA 118
Cdd:cd03226 39 KTTLAKILAGLIKESSGSILL-----NGKPIKAKERRKSIGYVMQDvdYQLF-TDSVREELLLG----LKELDAGNEQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MfYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMG 198
Cdd:cd03226 109 T-VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYE 187
|
170
....*....|....*...
gi 489402728 199 FAREVADRILFMDDGQII 216
Cdd:cd03226 188 FLAKVCDRVLLLANGAIV 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
41-229 |
9.04e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.59 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKtDMNELRRNIGMVFQHfylyPHKT-----VLQNITLAPIKVNkVSKEEAE 115
Cdd:PRK13633 49 KSTIAKHMNALLIPSEGKVYVDGLDTSDEE-NLWDIRNKAGMVFQN----PDNQivatiVEEDVAFGPENLG-IPPEEIR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:PRK13633 123 ERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILIT 202
|
170 180 190
....*....|....*....|....*....|....*
gi 489402728 195 HEMGFAREvADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13633 203 HYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-214 |
1.27e-34 |
|
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: 121.72 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNF--QVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSltikpgekvaivgpsgsgKSTLLKLLLRLYDPTSGEILIDGVDL--RDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNItlapikvnkvskeeaektamfylekvgipekanvyphqLSGGQQQRVAIARGLAMQPEIML 160
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQ 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
41-230 |
1.63e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhNKKTdMNELRRNIGMVFQHfylyPHK-----TVLQNITLApIKVNKVSKEEAE 115
Cdd:PRK13635 46 KSTLAKLLNGLLLPEAGTITVGGMVL-SEET-VWDVRRQVGMVFQN----PDNqfvgaTVQDDVAFG-LENIGVPREEMV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM-TMVVVT 194
Cdd:PRK13635 119 ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSIT 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 489402728 195 HEMGFAREvADRILFMDDGQIIEDTTPAQFFANPEQ 230
Cdd:PRK13635 199 HDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHM 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-213 |
4.30e-34 |
|
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: 122.19 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTD-MnelrrnigMVFQHFYLYPHKTVLQNITLAPIKVNK-VSKEEAEKTA 118
Cdd:TIGR01184 24 KSTLLNLISGLAQPTSGGVILEGKQITEPGPDrM--------VVFQNYSLLPWLTVRENIALAVDRVLPdLSKSERRAIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD-VMKTLAKEGMTMVVVTHEM 197
Cdd:TIGR01184 96 EEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQIWEEHRVTVLMVTHDV 175
|
170
....*....|....*.
gi 489402728 198 GFAREVADRILFMDDG 213
Cdd:TIGR01184 176 DEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
7.07e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 122.99 E-value: 7.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNV-NKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:PRK13652 3 LIETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI--TKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQH-----FylypHKTVLQNITLAPIKVNkVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK13652 81 GLVFQNpddqiF----SPTVEQDIAFGPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE-QERA 233
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDlLARV 235
|
..
gi 489402728 234 RL 235
Cdd:PRK13652 236 HL 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
41-231 |
8.38e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 122.25 E-value: 8.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKktDMNELRRNIGMVFQHFY--LYPHKTVLQnITLAPIKVN-KVSKEEAEKT 117
Cdd:COG4167 52 KSTLAKMLAGIIEPTSGEILINGHKLEYG--DYKYRCKHIRMIFQDPNtsLNPRLNIGQ-ILEEPLRLNtDLTAEEREER 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:COG4167 129 IFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQ 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 489402728 196 EMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:COG4167 209 HLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-215 |
9.18e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.09 E-value: 9.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 6 RNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHnkktdmnELRRNIGMVFQ 85
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA-------EAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 86 HFYLYPHKTVLQNITLApIKVNkvSKEEAEKTamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPT 165
Cdd:PRK11247 89 DARLLPWKKVIDNVGLG-LKGQ--WRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489402728 166 SALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-216 |
1.02e-33 |
|
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: 119.85 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRNIGMVFQhfylyphktvlqnitlapikvnkvskeeaektamf 120
Cdd:cd03214 38 KSTLLKTLAGLLKPSSGEILLDGKDLASLSPK--ELARKIAYVPQ----------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGF 199
Cdd:cd03214 81 ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNL 160
|
170
....*....|....*..
gi 489402728 200 AREVADRILFMDDGQII 216
Cdd:cd03214 161 AARYADRVILLKDGRIV 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
41-235 |
2.30e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 120.46 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVqNTEVHnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITL--AP-IKVNKVSKEEAEKT 117
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTL-NGQDH---TTTPPSRRPVSMLFQENNLFSHLTVAQNIGLglNPgLKLNAAQREKLHAI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AmfylEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:PRK10771 114 A----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQErQLTLLMVSHS 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 489402728 197 MGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARL 235
Cdd:PRK10771 190 LEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-238 |
2.31e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 123.29 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGM 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV----THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPeqerARLFLS 238
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP----ASRFMA 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-166 |
4.39e-33 |
|
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: 117.36 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLAPIkVNKVSKEEAEKTAMF 120
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGQDLT--DDERKSLRKEIGYVFQDPQLFPRLTVRENLRLGLL-LKGLSKREKDARAEE 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKAN----VYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTS 166
Cdd:pfam00005 101 ALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
4.51e-33 |
|
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: 119.70 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnEL-RRN 79
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSleveegeivallgrngagKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--RIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLekvgIP---EKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYEL----FPrlkERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARL 235
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-215 |
4.92e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.21 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNK-YYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRN 79
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 160 LFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
41-200 |
5.30e-33 |
|
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: 118.29 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIGMVFQH-----FYlyphKTVLQNITLAPIKVNkVSKEEAE 115
Cdd:TIGR01166 31 KSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDpddqlFA----ADVDQDVAFGPLNLG-LSEAEVE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH 195
Cdd:TIGR01166 106 RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
....*
gi 489402728 196 EMGFA 200
Cdd:TIGR01166 186 DVDLA 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
41-215 |
1.38e-32 |
|
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: 118.04 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA---PIKVNKVSKEEAEKT 117
Cdd:TIGR01277 37 KSTLLNLIAGFIEPASGSIKVNDQSH----TGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGlhpGLKLNAEQQEKVVDA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AmfylEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:TIGR01277 113 A----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSErQRTLLMVTHH 188
|
170
....*....|....*....
gi 489402728 197 MGFAREVADRILFMDDGQI 215
Cdd:TIGR01277 189 LSDARAIASQIAVVSQGKI 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-223 |
4.99e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.58 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVN-KYYGNFQVLKNINvqvkkgevvvvvgpsgsGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIG 81
Cdd:COG1132 340 IEFENVSfSYPGDRPVLKDISltippgetvalvgpsgsGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYpHKTVLQNITLAPIkvnKVSKEEAEKTAmfylekvgipEKANVY------PH-----------QLSGGQQQ 144
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGRP---DATDEEVEEAA----------KAAQAHefiealPDgydtvvgergvNLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQ 223
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
41-227 |
6.10e-32 |
|
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: 122.56 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNkkTDMNELRRNIGMVFQHFYLyPHKTVLQNITLApikvnkvsKEEAEKTAMF 120
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDLSD--LDPASWRRQIAWVPQNPYL-FAGTIRENLRLG--------RPDASDEELE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 Y-LEKVGIPEKANVYPH-----------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGM 188
Cdd:COG4988 445 AaLEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GR 523
|
170 180 190
....*....|....*....|....*....|....*....
gi 489402728 189 TMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFAN 227
Cdd:COG4988 524 TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-225 |
8.05e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 117.91 E-value: 8.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN--KKTDMNELRRNIGMVFQhfylYPH-----KTVLQNITLAPIKVNkVSKEE 113
Cdd:PRK13643 45 KSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQ----FPEsqlfeETVLKDVAFGPQNFG-IPKEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKA-NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVV 192
Cdd:PRK13643 120 AEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL 199
|
170 180 190
....*....|....*....|....*....|...
gi 489402728 193 VTHEMGFAREVADRILFMDDGQIIEDTTPAQFF 225
Cdd:PRK13643 200 VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
10-221 |
9.06e-32 |
|
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: 117.88 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 10 KYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnkKTDMNELRRNIGMVFQHFYL 89
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV---VREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 90 YPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALD 169
Cdd:TIGR01188 78 DEDLTGRENLEMMG-RLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489402728 170 PEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTP 221
Cdd:TIGR01188 157 PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-226 |
1.05e-31 |
|
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: 116.18 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVN-KYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIG 81
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI--REVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKanvYPHQ-------LSGGQQQRVAIARGLAM 154
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDG---YDTIvgerglkLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMgfaREV--ADRILFMDDGQIIEDTTPAQFFA 226
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
1.19e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 117.26 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNI 80
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQH--FYLYPhKTVLQNITLAPIKVnKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEI 158
Cdd:PRK13636 85 GMVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 159 MLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQER-ARLF 236
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRkVNLR 242
|
....
gi 489402728 237 LSRV 240
Cdd:PRK13636 243 LPRI 246
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-221 |
1.57e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 121.75 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYY----GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTD-MNEL 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADaLAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RR-NIGMVFQHFYLYPHKTVLQNITLAPIKVNkVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK10535 84 RReHFGFIFQRYHLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTP 221
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-218 |
1.96e-31 |
|
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: 114.99 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQ--VLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI--RQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITL-APIkvnkVSKEEAEKTAMFylekVGIPEKANVYPH-----------QLSGGQQQRVAI 148
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLgAPL----ADDERILRAAEL----AGVTDFVNKHPNgldlqigergrGLSGGQRQAVAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 149 ARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAkEGMTMVVVTHEMGFArEVADRILFMDDGQIIED 218
Cdd:cd03245 152 ARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
2.10e-31 |
|
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: 113.29 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKkTDMNELRRNIGM 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFA-SPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VfqhfylyphktvlqnitlapikvnkvskeeaektamfylekvgipekanvypHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03216 80 V----------------------------------------------------YQLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
41-216 |
2.47e-31 |
|
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: 114.91 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITL-APIKvnKVSKEEAEKTAM 119
Cdd:cd03263 41 KTTTLKMLTGELRPTSGTAYINGYSIR---TDRKAARQSLGYCPQFDALFDELTVREHLRFyARLK--GLPKSEIKEEVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGF 199
Cdd:cd03263 116 LLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDE 194
|
170
....*....|....*..
gi 489402728 200 AREVADRILFMDDGQII 216
Cdd:cd03263 195 AEALCDRIAIMSDGKLR 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-243 |
2.90e-31 |
|
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: 117.91 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAiTDGGLIVQNTEVHN---KKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLApikVNKVSKEEAEKT 117
Cdd:TIGR02142 36 KTTLIRLIAGLTR-PDEGEIVLNGRTLFdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYG---MKRARPSERRIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:TIGR02142 112 FERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHS 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489402728 197 MGFAREVADRILFMDDGQIIEDTTPAQFFANPE------QERARLFLSRVLNH 243
Cdd:TIGR02142 192 LQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlpwlarEDQGSLIEGVVAEH 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
41-211 |
6.98e-31 |
|
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: 113.40 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINqleaitdgGLIVQNT-EVHNKKTDMNELRRNIGMVFQHFY----------------LYPHKTVLQnitlap 103
Cdd:cd03235 38 KSTLLKAIL--------GLLKPTSgSIRVFGKPLEKERKRIGYVPQRRSidrdfpisvrdvvlmgLYGHKGLFR------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 104 ikvnKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTL 183
Cdd:cd03235 104 ----RLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL 178
|
170 180
....*....|....*....|....*...
gi 489402728 184 AKEGMTMVVVTHEMGFAREVADRILFMD 211
Cdd:cd03235 179 RREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
1.32e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHNKkTDMNELRRNI 80
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSlelrpgevhallgengagKSTLMKILSGVYQPDSGEILLDGEPVRFR-SPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEI 158
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 159 MLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII-----EDTTPAQ 223
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVgtgpvAELTEDE 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
1.39e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHNKKTdmNE-LRRN 79
Cdd:COG3845 4 PALELRGITKRFGGVVANDDVSltvrpgeihallgengagKSTLMKILYGLYQPDSGEILIDGKPVRIRSP--RDaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPE 157
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 158 IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII-----EDTTPAQ 223
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVgtvdtAETSEEE 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
41-223 |
2.32e-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: 118.43 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAektamf 120
Cdd:TIGR03375 504 KSTLLKLLLGLYQPTEGSVLLDGVDIR--QIDPADLRRNIGYVPQDPRLF-YGTLRDNIALGAPYADDEEILRA------ 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 yLEKVGIPEKANVYPH-----------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAkEGMT 189
Cdd:TIGR03375 575 -AELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKT 652
|
170 180 190
....*....|....*....|....*....|....
gi 489402728 190 MVVVTHEMGFArEVADRILFMDDGQIIEDTTPAQ 223
Cdd:TIGR03375 653 LVLVTHRTSLL-DLVDRIIVMDNGRIVADGPKDQ 685
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
41-230 |
2.93e-30 |
|
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: 117.56 E-value: 2.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkktDMNE--LRRNIGMVFQHFYLYpHKTVLQNITLA-PikvnKVSKEEAEKT 117
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLR----DLDEddLRRRIAVVPQRPHLF-DTTLRENLRLArP----DATDEELWAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 amfyLEKVGI-------PEK--ANVYPH--QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKe 186
Cdd:COG4987 445 ----LERVGLgdwlaalPDGldTWLGEGgrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA- 519
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489402728 187 GMTMVVVTHEMGfAREVADRILFMDDGQIIEDTTPAQFFANPEQ 230
Cdd:COG4987 520 GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
41-240 |
3.53e-30 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 114.42 E-value: 3.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQH--FYLYPHKTVlQNITLAPIKVN--KVSKEEAE 115
Cdd:PRK15079 60 KSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDplASLNPRMTI-GEIIAEPLRTYhpKLSRQEVK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVV 193
Cdd:PRK15079 139 DRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREmGLSLIFI 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489402728 194 THEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:PRK15079 219 AHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-234 |
7.91e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 112.50 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDG-----GLIVQNTEVHNKKtDMNELRRNIGMVFQHFYLYPhKTVLQNItLAPIKVNK-VSKEEA 114
Cdd:PRK14271 60 KTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYR-DVLEFRRRVGMLFQRPNPFP-MSIMDNV-LAGVRAHKlVPRKEF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVG----IPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAkEGMTM 190
Cdd:PRK14271 137 RGVAQARLTEVGlwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTV 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 191 VVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQ-ERAR 234
Cdd:PRK14271 216 IIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHaETAR 260
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
1.33e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVN-KYYGNFQ-VLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:PRK13632 8 IKVENVSfSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI--SKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHfylyPHK-----TV-------LQNITLAPIKVNKVSKEEAEKTAMF-YLEKvgipekanvYPHQLSGGQQQRVA 147
Cdd:PRK13632 86 GIIFQN----PDNqfigaTVeddiafgLENKKVPPKKMKDIIDDLAKKVGMEdYLDK---------EPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 148 IARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM-TMVVVTHEMgfaREV--ADRILFMDDGQIIEDTTPAQF 224
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEI 229
|
....*
gi 489402728 225 FANPE 229
Cdd:PRK13632 230 LNNKE 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-230 |
2.25e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.41 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGN-----FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTD--M 73
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 74 NELRRNIGMVFQhfylYPHK-----TVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKA-NVYPHQLSGGQQQRVA 147
Cdd:PRK13646 81 RPVRKRIGMVFQ----FPESqlfedTVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 148 IARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTL-AKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFA 226
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
....
gi 489402728 227 NPEQ 230
Cdd:PRK13646 236 DKKK 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-241 |
3.45e-29 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 110.28 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYY---------GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHN-KKT 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMNELRRNIGMVFQHFY--LYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAI 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPsaVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 149 ARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF--F 225
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLlsF 241
|
250
....*....|....*.
gi 489402728 226 ANPEqerARLFLSRVL 241
Cdd:TIGR02769 242 KHPA---GRNLQSAVL 254
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-238 |
3.89e-29 |
|
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: 109.15 E-value: 3.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 4 EFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMnELRRNIGMV 83
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 84 FQHFYLYPHKTVLQNITLAPIKVNKVSKE-EAEKTAMF-YLEKVgIPEKANVyphqLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKiPDEIYELFpVLKEM-LGRRGGD----LSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFfanpEQERARLFLS 238
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-231 |
5.03e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.75 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKK----TDMNELRRNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVS-KEEAE 115
Cdd:PRK14246 49 KSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAY-PLKSHGIKeKREIK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVG----IPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEgMTMV 191
Cdd:PRK14246 128 KIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489402728 192 VVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:PRK14246 207 IVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-229 |
5.44e-29 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 111.86 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNK-YYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGglivqntEVHNKKTDMNELR---R 78
Cdd:PRK11650 4 LKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSG-------EIWIGGRVVNELEpadR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPHKTVLQNITLApIKVNKVSKEE-----AEKTAMFYLEKVgIPEKanvyPHQLSGGQQQRVAIARGLA 153
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEieervAEAARILELEPL-LDRK----PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 154 MQPEIMLFDEPTSALDP----EMIGEVLDVMKTLakeGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPA 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-218 |
1.16e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.81 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHNKKtdmnelRRNIGm 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSftvpkgeifgllgpngagKTTTIRIILGILAPDSGEVLWDGEPLDPED------RRRIG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 vfqhfY------LYPHKTVLQNIT-LAPIKvnKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:COG4152 75 -----YlpeergLYPKMKVGEQLVyLARLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-216 |
1.24e-28 |
|
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: 107.37 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNtevhNKKTDmnELRRNIGM 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDI--AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVL-QNITLAPIKvnKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:cd03269 75 LPEERGLYPKMKVIdQLVYLAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
2.43e-28 |
|
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: 112.20 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYY-----GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQnteVHNKKTDMNEL 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 R--------RNIGMVFQHFYLYPHKTVLQNITLApIKVnKVSKEEAEKTAMFYLEKVGIPEKA-----NVYPHQLSGGQQ 143
Cdd:TIGR03269 356 GpdgrgrakRYIGILHQEYDLYPHRTVLDNLTEA-IGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 144 QRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD-VMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPA 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
.
gi 489402728 223 Q 223
Cdd:TIGR03269 514 E 514
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
41-214 |
7.50e-28 |
|
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: 105.98 E-value: 7.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCI--NQLeaiTDGGLIVQNTEvhNKKTDMN--------ELRRN-IGMVFQHFYLYPHKTVLQnITLAPIKVNKV 109
Cdd:COG4778 50 KSTLLKCIygNYL---PDSGSILVRHD--GGWVDLAqaspreilALRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERGV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 110 SKEEAEKTAMFYLEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM 188
Cdd:COG4778 124 DREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGT 203
|
170 180
....*....|....*....|....*.
gi 489402728 189 TMVVVTHEMGFAREVADRILFMDDGQ 214
Cdd:COG4778 204 AIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
41-240 |
1.11e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.72 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFY--LYPHKTVLQNItLAPIKVNKV-SKEEAEK 116
Cdd:PRK10261 363 KSTTGRALLRLVESQGGEIIFNGQRIDTlSPGKLQALRRDIQFIFQDPYasLDPRQTVGDSI-MEPLRVHGLlPGKAAAA 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:PRK10261 442 RVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFIS 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRV 240
Cdd:PRK10261 522 HDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-241 |
1.35e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 106.31 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFY--LYPHKTVlQNITLAPIK-VNKVSKEEAEK 116
Cdd:PRK10419 51 KSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDSIsaVNPRKTV-REIIREPLRhLLSLDKAERLA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:PRK10419 130 RASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFIT 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489402728 195 HEMGFAREVADRILFMDDGQIIED--TTPAQFFANPEqerARLFLSRVL 241
Cdd:PRK10419 210 HDLRLVERFCQRVMVMDNGQIVETqpVGDKLTFSSPA---GRVLQNAVL 255
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
41-212 |
1.69e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCIN-QLEAI--TDGGLIVQNTEVhnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA-PikvNKVSKEEAEK 116
Cdd:COG4136 40 KSTLLAAIAgTLSPAfsASGEVLLNGRRL----TALPAEQRRIGILFQDDLLFPHLSVGENLAFAlP---PTIGRAQRRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD-VMKTLAKEGMTMVVVTH 195
Cdd:COG4136 113 RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
170
....*....|....*..
gi 489402728 196 EMGfAREVADRILFMDD 212
Cdd:COG4136 193 DEE-DAPAAGRVLDLGN 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-220 |
1.79e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.28 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYY--GNFQ--VLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhNKKTDMN--E 75
Cdd:PRK11629 5 LLQCDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPM-SKLSSAAkaE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LR-RNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAM 154
Cdd:PRK11629 84 LRnQKLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTL-AKEGMTMVVVTHEMGFAREVaDRILFMDDGQIIEDTT 220
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-240 |
2.10e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQL-----EAITDGGLIVQNTEVHNKKTDMNELR 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMVFQHFYLYPhKTVLQNITLAPIKVNKVSK-------EEAEKTAMFYLEkvgIPEKANVYPHQLSGGQQQRVAIAR 150
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDE---IKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 151 GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLA-KEGMTMVVVTHEMGFAREVADRILFMDD-----GQIIEDTTPAQF 224
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|....*..
gi 489402728 225 FANPEQERARLF-LSRV 240
Cdd:PRK14258 244 FNSPHDSRTREYvLSRL 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
41-229 |
2.48e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.25 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVH---NKKTDMNELRRNIGMVFQ--HFYLYpHKTVLQNITLAPIKVNKvSKEEAE 115
Cdd:PRK13645 50 KSTMIQLTNGLIISETGQTIVGDYAIPanlKKIKEVKRLRKEIGLVFQfpEYQLF-QETIEKDIAFGPVNLGE-NKQEAY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEK-ANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVV 193
Cdd:PRK13645 128 KKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMV 207
|
170 180 190
....*....|....*....|....*....|....*.
gi 489402728 194 THEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13645 208 THNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
41-229 |
4.94e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQL---EAITDGGLIVQNTEVhNKKTdMNELRRNIGMVFQHfylyPHK-----TVLQNITLApIKVNKVSKE 112
Cdd:PRK13640 46 KSTISKLINGLllpDDNPNSKITVDGITL-TAKT-VWDIREKVGIVFQN----PDNqfvgaTVGDDVAFG-LENRAVPRP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 113 EAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMV 191
Cdd:PRK13640 119 EMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVI 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 192 VVTHEMGFArEVADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13640 199 SITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
5.72e-27 |
|
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: 103.22 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNtevHNKKTDMNELRRNIGM 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHA-RLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 163 EPTSALDPEMIGEVLDVMKTL-AKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTP 221
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
79-240 |
8.89e-27 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 108.02 E-value: 8.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQH--FYLYPHKTVLQNITlAPIKVNK-VSKEEAEKTAMFYLEKVGIPEKANV---YPHQLSGGQQQRVAIARGL 152
Cdd:PRK10261 105 DMAMIFQEpmTSLNPVFTVGEQIA-ESIRLHQgASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMAL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 153 AMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQE 231
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHP 263
|
....*....
gi 489402728 232 RARLFLSRV 240
Cdd:PRK10261 264 YTRALLAAV 272
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
80-228 |
1.67e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 104.44 E-value: 1.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQH--FYLYPHKTVLQNITLApIKVNKV-SKEEAEKTAMFYLEKVGIPEKA---NVYPHQLSGGQQQRVAIARGLA 153
Cdd:PRK11022 91 VAMIFQDpmTSLNPCYTVGFQIMEA-IKVHQGgNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIA 169
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 154 MQPEIMLFDEPTSALDPEMIGEVLDVMKTLA-KEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:PRK11022 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
41-203 |
1.81e-26 |
|
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: 101.79 E-value: 1.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITL-APIKVNKVSKEEAEKTam 119
Cdd:COG4133 41 KTTLLRILAGLLPPSAGEVLWNGEPIR---DAREDYRRRLAYLGHADGLKPELTVRENLRFwAALYGLRADREAIDEA-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 fyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH---E 196
Cdd:COG4133 116 --LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHqplE 193
|
....*..
gi 489402728 197 MGFAREV 203
Cdd:COG4133 194 LAAARVL 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-233 |
3.55e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 102.25 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnelrRniGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEAEKTAMF 120
Cdd:COG4525 46 KTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-----R--GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP---EMIGE-VLDVMktlAKEGMTMVVVTHE 196
Cdd:COG4525 118 LLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMQElLLDVW---QRTGKGVFLITHS 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489402728 197 MGFAREVADRILFMDD--GQIIEDTTP--AQFFANPEQERA 233
Cdd:COG4525 195 VEEALFLATRLVVMSPgpGRIVERLELdfSRRFLAGEDARA 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
41-234 |
4.61e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 102.18 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQ--HFYLYPHKTVLQnITLAPIKVN-KVSKEEAEKT 117
Cdd:PRK15112 52 KSTLAKMLAGMIEPTSGELLIDDHPLH--FGDYSYRSQRIRMIFQdpSTSLNPRQRISQ-ILDFPLRLNtDLEPEQREKQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTL-AKEGMTMVVVTH 195
Cdd:PRK15112 129 IIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQ 208
|
170 180 190
....*....|....*....|....*....|....*....
gi 489402728 196 EMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERAR 234
Cdd:PRK15112 209 HLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-218 |
4.83e-26 |
|
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: 101.70 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINvqvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIvqntEVHNKK---TDMNELR 77
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISwtvkpgehwailgpngagKSTLLSLITGDLPPTYGNDV----RLFGERrggEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 78 RNIGMV--FQHFYLYPHKTVLQ--------NITLapikVNKVSKEEAEKtAMFYLEKVGIPEKANVYPHQLSGGQQQRVA 147
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDvvlsgffdSIGL----YREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 148 IARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEG-MTMVVVTH---EM--GFarevaDRILFMDDGQIIED 218
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
41-230 |
4.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMN--ELRRNIGMVFQHfylyPHK-----TVLQNITLApIKVNKVSKEE 113
Cdd:PRK13650 46 KSTTVRLIDGLLEAESGQIIIDGDLL----TEENvwDIRHKIGMVFQN----PDNqfvgaTVEDDVAFG-LENKGIPHEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVV 192
Cdd:PRK13650 117 MKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVIS 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489402728 193 VTHEMGfarEVA--DRILFMDDGQIIEDTTPAQFFANPEQ 230
Cdd:PRK13650 197 ITHDLD---EVAlsDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
41-216 |
4.99e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 102.12 E-value: 4.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQHfylyPH-----KTVLQNITLAPIKVnKVSKEEAE 115
Cdd:PRK13647 44 KSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVRSKVGLVFQD----PDdqvfsSTVWDDVAFGPVNM-GLDKDEVE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH 195
Cdd:PRK13647 117 RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
170 180
....*....|....*....|.
gi 489402728 196 EMGFAREVADRILFMDDGQII 216
Cdd:PRK13647 197 DVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-237 |
8.56e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 101.38 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCIN-QLEAitDGGLIVQNTEvhN----KKTDMNEL 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGgQIAP--DHGEILFDGE--NipamSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQP 156
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQeRARL 235
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQ 241
|
..
gi 489402728 236 FL 237
Cdd:PRK11831 242 FL 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-226 |
8.86e-26 |
|
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: 100.38 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVN-KYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIG 81
Cdd:cd03254 3 IEFENVNfSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI--RDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPhKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYP----HQLSGGQQQRVAIARGLAMQPE 157
Cdd:cd03254 81 VVLQDTFLFS-GTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 158 IMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFA 226
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
41-229 |
9.08e-26 |
|
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: 100.69 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNteVHNKKTDMNELRRNIGMVFQHFYLYPhKTVLQNITLAPIKVNKVSKEEAEKTAMF 120
Cdd:cd03249 42 KSTVVSLLERFYDPTSGEILLDG--VDIRDLNLRWLRSQIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKAN--VYPH--QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPE---MIGEVLDvmktLAKEGMTMVVV 193
Cdd:cd03249 119 HDFIMSLPDGYDtlVGERgsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAEsekLVQEALD----RAMKGRTTIVI 194
|
170 180 190
....*....|....*....|....*....|....*.
gi 489402728 194 THEMGFAREvADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:cd03249 195 AHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-219 |
1.08e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 100.24 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNkktdMNE-----LR-RNIGMVFQHFYLYPHKTVLQNITLaPIKVNKVSKEEA 114
Cdd:PRK10584 49 KSTLLAILAGLDDGSSGEVSLVGQPLHQ----MDEearakLRaKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVV 193
Cdd:PRK10584 124 RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILV 203
|
170 180
....*....|....*....|....*.
gi 489402728 194 THEMGFAREvADRILFMDDGQIIEDT 219
Cdd:PRK10584 204 THDLQLAAR-CDRRLRLVNGQLQEEA 228
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
117-241 |
1.80e-25 |
|
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: 100.29 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGIPE-KANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:TIGR02323 127 TAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVT 206
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRVL 241
Cdd:TIGR02323 207 HDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSIL 253
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-226 |
6.05e-25 |
|
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: 98.46 E-value: 6.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGN--FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV--RDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAEKTAmfYLEKVgIPEKANVYPH-------QLSGGQQQRVAIARGLA 153
Cdd:cd03251 79 GLVSQDVFLF-NDTVAENIAYGRPGATREEVEEAARAA--NAHEF-IMELPEGYDTvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 154 MQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFA 226
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
41-216 |
6.66e-25 |
|
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: 97.24 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCI-NQLEAITDGGLIVQNtevhNKKTDMNELRRNIGMVFQHFYLYPHKTVlqnitlapikvnkvskeeaEKTAM 119
Cdd:cd03213 48 KSTLLNALaGRRTGLGVSGEVLIN----GRPLDKRSFRKIIGYVPQDDILHPTLTV-------------------RETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 FYLEKVGIpekanvyphqlSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH---- 195
Cdd:cd03213 105 FAAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpss 173
|
170 180
....*....|....*....|.
gi 489402728 196 EMgFarEVADRILFMDDGQII 216
Cdd:cd03213 174 EI-F--ELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-228 |
1.50e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN-FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKkTDMNELRRNI 80
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF-SKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYL-YPHKTVLQ-------NITLAPIKVNK-VSKEEAEktamfylekVGIPEKANVYPHQLSGGQQQRVAIARG 151
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEdlafgpeNLCLPPIEIRKrVDRALAE---------IGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGfAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
111-237 |
1.89e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.94 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 111 KEEAEKTAMFYLEKVGIPEKA---NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE- 186
Cdd:PRK15134 127 REAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEl 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489402728 187 GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFL 237
Cdd:PRK15134 207 NMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-218 |
2.62e-24 |
|
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: 96.13 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNtevhNKKTDMNELRRNIGM 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG----KSYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNITLAPiKVNKVSKEEAEKTamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLA-RLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
41-225 |
3.86e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.13 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKktDMNELRRNIGMVFQHfylyPHKTVLQNITLAPIKV----NKVSKEEAEK 116
Cdd:PRK13648 48 KSTIAKLMIGIEKVKSGEIFYNNQAITDD--NFEKLRKHIGIVFQN----PDNQFVGSIVKYDVAFglenHAVPYDEMHR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:PRK13648 122 RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITH 201
|
170 180 190
....*....|....*....|....*....|
gi 489402728 196 EMGFAREvADRILFMDDGQIIEDTTPAQFF 225
Cdd:PRK13648 202 DLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
117-241 |
5.12e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 117 TAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:PRK11701 130 TAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVT 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 489402728 195 HEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLSRVL 241
Cdd:PRK11701 210 HDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLVSSVL 256
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-218 |
6.19e-24 |
|
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: 96.02 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYG--NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL--ALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAEKTA---MFYLEkvgIPEKANVYPHQ----LSGGQQQRVAIARGLA 153
Cdd:cd03252 79 GVVLQENVLF-NRSIRDNIALADPGMSMERVIEAAKLAgahDFISE---LPEGYDTIVGEqgagLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 154 MQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIED 218
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
41-223 |
6.26e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRnigmvfqhfylypHKTVL-QNITLA-PIKVNKV--------- 109
Cdd:PRK13548 41 KSTLLRALSGELSPDSGEVRLNGRPLADWSPA--ELAR-------------RRAVLpQHSSLSfPFTVEEVvamgraphg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 110 -SKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLA------MQPEIMLFDEPTSALDPEMIGEVLDVMKT 182
Cdd:PRK13548 106 lSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 183 LAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:PRK13548 186 LAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
41-224 |
1.85e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLeaITDGGLIVQNTEVHNKKT--------DMNELRRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSK- 111
Cdd:PRK09984 43 KSTLLRHLSGL--ITGDKSAGSHIELLGRTVqregrlarDIRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 112 ------EEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAK 185
Cdd:PRK09984 121 cfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQ 200
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489402728 186 -EGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQF 224
Cdd:PRK09984 201 nDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
41-238 |
1.86e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KST----LLRCINqleaiTDGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFY--LYPHKTVLQnITLAPIKVNK--VSK 111
Cdd:PRK15134 325 KSTtglaLLRLIN-----SQGEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNssLNPRLNVLQ-IIEEGLRVHQptLSA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 112 EEAEKTAMFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTL-AKEGMT 189
Cdd:PRK15134 399 AQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqQKHQLA 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489402728 190 MVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLS 238
Cdd:PRK15134 479 YLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-216 |
2.10e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.48 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLlrcINQLEAIT--DGGLIVQNTEV---HNKKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLApikVNKVSKEEAE 115
Cdd:PRK11144 37 KTSL---INAISGLTrpQKGRIVLNGRVlfdAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLRYG---MAKSMVAQFD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 116 KTamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVT 194
Cdd:PRK11144 111 KI----VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVS 186
|
170 180
....*....|....*....|..
gi 489402728 195 HEMGFAREVADRILFMDDGQII 216
Cdd:PRK11144 187 HSLDEILRLADRVVVLEQGKVK 208
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
41-227 |
3.77e-23 |
|
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: 97.72 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHFYLYPhKTVLQNITLApikvNKVSKEEAEKTAmf 120
Cdd:TIGR03797 492 KSTLLRLLLGFETPESGSVFYDGQDL--AGLDVQAVRRQLGVVLQNGRLMS-GSIFENIAGG----APLTLDEAWEAA-- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 ylEKVGIPEKANVYP---H--------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEM--IgevldVMKTLAKEG 187
Cdd:TIGR03797 563 --RMAGLAEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTqaI-----VSESLERLK 635
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489402728 188 MTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQ------FFAN 227
Cdd:TIGR03797 636 VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDElmaregLFAQ 680
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
41-218 |
3.89e-23 |
|
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: 93.03 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkKTDMNELRRNIGMVFQHFYLYPHKTVLQNI-TLAPIKvnKVSKEEAEKTAM 119
Cdd:cd03264 38 KTTLMRILATLTPPSSGTIRIDGQDV---LKQPQKLRRRIGYLPQEFGVYPNFTVREFLdYIAWLK--GIPSKEVKARVD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAkEGMTMVVVTHEMGF 199
Cdd:cd03264 113 EVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVED 191
|
170
....*....|....*....
gi 489402728 200 AREVADRILFMDDGQIIED 218
Cdd:cd03264 192 VESLCNQVAVLNKGKLVFE 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
41-215 |
6.61e-23 |
|
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: 91.51 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQHFYLYPhKTVLQNItlapikvnkvskeeaektamf 120
Cdd:cd03246 41 KSTLARLILGLLRPTSGRVRLDGADIS--QWDPNELGDHVGYLPQDDELFS-GSIAENI--------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 ylekvgipekanvyphqLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmiGE--VLDVMKTLAKEGMTMVVVTHEMG 198
Cdd:cd03246 97 -----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE--GEraLNQAIAALKAAGATRIVIAHRPE 157
|
170
....*....|....*..
gi 489402728 199 FAREvADRILFMDDGQI 215
Cdd:cd03246 158 TLAS-ADRILVLEDGRV 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-223 |
7.72e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.26 E-value: 7.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTdmNELRRnigmvfqhfylypHKTVL-QNITLA-PIKVNKV--------- 109
Cdd:COG4559 40 KSTLLKLLTGELTPSSGEVRLNGRPLAAWSP--WELAR-------------RRAVLpQHSSLAfPFTVEEVvalgraphg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 110 -SKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLA-------MQPEIMLFDEPTSALDpemIGEVLDVM- 180
Cdd:COG4559 105 sSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALD---LAHQHAVLr 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 181 --KTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG4559 182 laRQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
41-210 |
4.33e-22 |
|
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: 94.28 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNE--LRRNIGMVFQHFYLYPhKTVLQNITLApikvNKVSKEEAEKTA 118
Cdd:TIGR02857 361 KSTLLNLLLGFVDPTEGSIAVNGVPL----ADADAdsWRDQIAWVPQHPFLFA-GTIAENIRLA----RPDASDAEIREA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 mfyLEKVGIPEKANVYP-----------HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAkEG 187
Cdd:TIGR02857 432 ---LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QG 507
|
170 180
....*....|....*....|...
gi 489402728 188 MTMVVVTHEMGFAREvADRILFM 210
Cdd:TIGR02857 508 RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
76-232 |
6.72e-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: 93.71 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQH-FYLYPHKTVLQNItLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAM 154
Cdd:TIGR03269 107 IRKRIAIMLQRtFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAK 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPA-------QFFA 226
Cdd:TIGR03269 186 EPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDevvavfmEGVS 265
|
....*.
gi 489402728 227 NPEQER 232
Cdd:TIGR03269 266 EVEKEC 271
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
41-218 |
9.13e-22 |
|
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: 89.73 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHnkkTDMNELRRNIGMVFQHFYLYPHKTVLQNIT-------LAPIKVNKVSKEE 113
Cdd:cd03266 44 KTTTLRMLAGLLEPDAGFATVDGFDVV---KEPAEARRRLGFVSDSTGLYDRLTARENLEyfaglygLKGDELTARLEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKtamfylekVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVV 193
Cdd:cd03266 121 ADR--------LGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFS 192
|
170 180
....*....|....*....|....*
gi 489402728 194 THEMGFAREVADRILFMDDGQIIED 218
Cdd:cd03266 193 THIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
81-233 |
1.03e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 161 FDEPTSALDP---EMIGEVLdvMKTLAKEGMTMVVVTHEMGFAREVADRILFM--DDGQIIEDTTP--AQFFANPEQERA 233
Cdd:PRK11248 152 LDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPLnfARRFVAGESSRS 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
81-235 |
2.22e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 89.28 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMV--FQHFYLYPHKTVLQNITLAP---IKVN-----------KVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQ 144
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAQhqqLKTGlfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
170
....*....|..
gi 489402728 224 FFANPEQERARL 235
Cdd:PRK11300 241 IRNNPDVIKAYL 252
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
122-208 |
2.36e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 122 LEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAR 201
Cdd:NF040873 104 LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
....*..
gi 489402728 202 EvADRIL 208
Cdd:NF040873 184 R-ADPCV 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
135-215 |
5.28e-21 |
|
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: 86.72 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 135 PHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQ 214
Cdd:cd03215 102 SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
.
gi 489402728 215 I 215
Cdd:cd03215 182 I 182
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-226 |
5.55e-21 |
|
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: 91.34 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQ--VLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL--AIADPAWLRRQM 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKAN--VYPH--QLSGGQQQRVAIARGLAMQP 156
Cdd:TIGR01846 534 GVVLQENVLF-SRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNteVGEKgaNLSGGQRQRIAIARALVGNP 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 157 EIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFA 226
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
54-228 |
5.70e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 89.78 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 54 ITDGGLIVQNTEVHN-KKTDMNELR-RNIGMVFQH--FYLYPHKTVLQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPE 129
Cdd:PRK09473 71 RIGGSATFNGREILNlPEKELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 130 ---KANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVAD 205
Cdd:PRK09473 151 arkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICD 230
|
170 180
....*....|....*....|...
gi 489402728 206 RILFMDDGQIIEDTTPAQFFANP 228
Cdd:PRK09473 231 KVLVMYAGRTMEYGNARDVFYQP 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
89-216 |
7.37e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 89 LYPHKTVLQNITLAPI-KVNK---VSKEEAEKTAMFYLEKVGIpeKANvYPHQ----LSGGQQQRVAIARGLAMQPEIML 160
Cdd:COG1129 341 LVLDLSIRENITLASLdRLSRgglLDRRRERALAEEYIKRLRI--KTP-SPEQpvgnLSGGNQQKVVLAKWLATDPKVLI 417
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 161 FDEPTSALDpemIG---EVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:COG1129 418 LDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-213 |
1.16e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEvHNKKTDMNELRRNIG 81
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLA--PIK----VNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGrhLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDG 213
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
41-216 |
2.00e-20 |
|
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: 86.17 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQL---EAITDGGLIVQNTEVHNKKTdmnelRRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKT 117
Cdd:cd03234 46 KTTLLDAISGRvegGGTTSGQILFNGQPRKPDQF-----QKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AM---FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVT 194
Cdd:cd03234 121 KRvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI 200
|
170 180
....*....|....*....|....*
gi 489402728 195 HEMG---FarEVADRILFMDDGQII 216
Cdd:cd03234 201 HQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
109-238 |
2.82e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 109 VSKEEAEKTAMFYLEKVGIPEKANV---YPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAK 185
Cdd:PRK10418 109 LGKPADDATLTAALEAVGLENAARVlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQ 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 186 E-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARLFLS 238
Cdd:PRK10418 189 KrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-226 |
2.96e-20 |
|
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: 89.01 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYG--NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRN 79
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA--SLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYpHKTVLQNITLApiKVNKVSKEEAEKTA-MFYLEKV------GIPEKANVYPHQLSGGQQQRVAIARGL 152
Cdd:TIGR02203 408 VALVSQDVVLF-NDTIANNIAYG--RTEQADRAEIERALaAAYAQDFvdklplGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 153 AMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGfAREVADRILFMDDGQIIEDTTPAQFFA 226
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
76-229 |
7.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.91 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQH-FYLYPHKTVLQNITLApIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAM 154
Cdd:PRK13642 79 LRRKIGMVFQNpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTLA-KEGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-217 |
8.29e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.77 E-value: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYY--GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKtdMNELRRNI 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT--LASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITLApiKVNKVSKEEAEKTA-----MFYLEKVG------IPEKANVyphqLSGGQQQRVAIA 149
Cdd:PRK11176 420 ALVSQNVHLF-NDTIANNIAYA--RTEQYSREQIEEAArmayaMDFINKMDngldtvIGENGVL----LSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPE---MIGEVLDvmkTLAKEgMTMVVVTHEMGfAREVADRILFMDDGQIIE 217
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTEserAIQAALD---ELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVE 558
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
94-229 |
1.22e-19 |
|
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: 84.13 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 94 TVLQNItLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMI 173
Cdd:cd03218 91 TVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 174 GEVLDVMKTLAKEGMTMVVVTHEmgfARE---VADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITDHN---VREtlsITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
57-217 |
1.60e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 57 GGLIVQNTEVHNkkTDMNELRRNIGMVFQHFYLyPHKTVLQNITLAPIKVNkvskEEAEKTAmfyLEKVGIPEKANVYPH 136
Cdd:PRK11174 404 GSLKINGIELRE--LDPESWRKHLSWVGQNPQL-PHGTLRDNVLLGNPDAS----DEQLQQA---LENAWVSEFLPLLPQ 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 137 -----------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpeMIGEVLdVMKTL--AKEGMTMVVVTHEMGFAREV 203
Cdd:PRK11174 474 gldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD--AHSEQL-VMQALnaASRRQTTLMVTHQLEDLAQW 550
|
170
....*....|....
gi 489402728 204 aDRILFMDDGQIIE 217
Cdd:PRK11174 551 -DQIWVMQDGQIVQ 563
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-217 |
4.64e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCI-NQLEAitDGGLIVQNTEVHnkktdmnelrrnIGMVFQHF-YLYPHKTVLQNITlapikvnKVSKEEAEKTA 118
Cdd:COG0488 354 KSTLLKLLaGELEP--DSGTVKLGETVK------------IGYFDQHQeELDPDKTVLDELR-------DGAPGGTEQEV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGI-PEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLakEGmTMVVVTHEM 197
Cdd:COG0488 413 RGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDR 489
|
170 180
....*....|....*....|
gi 489402728 198 GFAREVADRILFMDDGQIIE 217
Cdd:COG0488 490 YFLDRVATRILEFEDGGVRE 509
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
76-235 |
5.38e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.40 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQHFYLYpHKTVLQNITLAPIKVNKVSKEEAEKTAM---FYLEKVG-----IPEKANvyphQLSGGQQQRVA 147
Cdd:PRK13657 407 LRRNIAVVFQDAGLF-NRSIEDNIRVGRPDATDEEMRAAAERAQahdFIERKPDgydtvVGERGR----QLSGGERQRLA 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 148 IARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTT------- 220
Cdd:PRK13657 482 IARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSfdelvar 559
|
170 180
....*....|....*....|...
gi 489402728 221 --------PAQFFANPEQERARL 235
Cdd:PRK13657 560 ggrfaallRAQGMLQEDERRKQP 582
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
41-218 |
6.68e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.83 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNELRR--NIGMVFQHFYL--YPHKTVLQNITLAPIKVNK------VS 110
Cdd:COG1101 45 KSTLLNAIAGSLPPDSGSILIDGKDV----TKLPEYKRakYIGRVFQDPMMgtAPSMTIEENLALAYRRGKRrglrrgLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 111 KEEAEktamFYLEKV-----GIPEKANVYPHQLSGGQQQRVAiargLAM----QPEIMLFDEPTSALDPEMIGEVLDVMK 181
Cdd:COG1101 121 KKRRE----LFRELLatlglGLENRLDTKVGLLSGGQRQALS----LLMatltKPKLLLLDEHTAALDPKTAALVLELTE 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 489402728 182 TLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:COG1101 193 KIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-216 |
1.06e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNtevhnkktdmnELRrnIGMVFQHFYLYPHKTVLQNIT--LAPIKVNKVSKEEAEKTA 118
Cdd:COG0488 37 KSTLLKILAGELEPDSGEVSIPK-----------GLR--IGYLPQEPPLDDDLTVLDTVLdgDAELRALEAELEELEAKL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFY-----------------------------LEKVGIPEkanVYPHQ----LSGGQQQRVAIARGLAMQPEIMLFDEPT 165
Cdd:COG0488 104 AEPdedlerlaelqeefealggweaearaeeiLSGLGFPE---EDLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489402728 166 SALDPEMIG--EvldvmKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:COG0488 181 NHLDLESIEwlE-----EFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLT 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-223 |
1.23e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.05 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQvkkgevvvvvgpsgsgKSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGM 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTipkggitaligpngagKSTLLSMISRLLPPDSGEVLVDGLDVA--TTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQ--HFYL------------YPH-KTVLqnitlapikvnkvSKEEAEK--TAMFYLEKVGIpekANVYPHQLSGGQQQR 145
Cdd:COG4604 80 LRQenHINSrltvrelvafgrFPYsKGRL-------------TAEDREIidEAIAYLDLEDL---ADRYLDELSGGQRQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 146 VAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-235 |
1.39e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTdMNELRRNIG 81
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT-AKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPIKVNKvsKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAER--DQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARL 235
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-221 |
1.61e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 84.29 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkKTDMNELRRNIGMVFQHFYLYPHKTVLQNItLAPIKVNKVSKEEAEKTAMF 120
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFHHLTVAEHI-LFYAQLKGRSWEEAQLEMEA 1044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVVTHEMGFA 200
Cdd:TIGR01257 1045 MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEA 1123
|
170 180
....*....|....*....|.
gi 489402728 201 REVADRILFMDDGQIIEDTTP 221
Cdd:TIGR01257 1124 DLLGDRIAIISQGRLYCSGTP 1144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-223 |
2.96e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHFylyphktvlqnitLAP--IKVN----------- 107
Cdd:PRK11231 41 KSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSRQLARRLALLPQHH-------------LTPegITVRelvaygrspwl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 108 ----KVSKEEAEKT--AMfylEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMK 181
Cdd:PRK11231 106 slwgRLSAEDNARVnqAM---EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 182 TLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:PRK11231 183 ELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-228 |
7.13e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN---FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRR 78
Cdd:TIGR00958 478 LIEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL--VQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYpHKTVLQNITLApikVNKVSKEEAEKTAMFYLEKVGIPEKANVY-----PH--QLSGGQQQRVAIARG 151
Cdd:TIGR00958 556 QVALVGQEPVLF-SGSVRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYdtevgEKgsQLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 152 LAMQPEIMLFDEPTSALDPEMIGEVLDVMKtlaKEGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
94-229 |
9.33e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 9.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 94 TVLQNItLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMI 173
Cdd:COG1137 94 TVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 174 GEVLDVMKTLAKEGMTmVVVT-HEmgfARE---VADRILFMDDGQIIEDTTPAQFFANPE 229
Cdd:COG1137 173 ADIQKIIRHLKERGIG-VLITdHN---VREtlgICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-218 |
1.26e-17 |
|
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: 77.74 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYG--NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKtdmNELRRNI 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE---KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYpHKTVLQNITLapikvnkvskeeaektamfylekvgipekanvyphQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKEgMTMVVVTHEMGfAREVADRILFMDDGQIIED 218
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-235 |
1.64e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 12 YGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTDMNELRRNIGMVFQHfylyP 91
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 92 HKTVLQNitlapikvnkvskeEAEKTAMFYLEKVGIPEK--------------ANVYPHQ----LSGGQQQRVAIARGLA 153
Cdd:PRK13638 87 EQQIFYT--------------DIDSDIAFSLRNLGVPEAeitrrvdealtlvdAQHFRHQpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 154 MQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPE-QER 232
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEaMEQ 232
|
...
gi 489402728 233 ARL 235
Cdd:PRK13638 233 AGL 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
136-215 |
2.61e-17 |
|
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: 80.56 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 136 HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmiGE--VLDVMKTLAKEGMTMVVVTHEMGfAREVADRILFMDDG 213
Cdd:COG4618 466 ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDG 542
|
..
gi 489402728 214 QI 215
Cdd:COG4618 543 RV 544
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
2.79e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.49 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 1 MLIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKktdMNELRRNI 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR---ARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTVLQNItLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIML 160
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 161 FDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTP 221
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
41-227 |
6.87e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAitdGGLIVQNTEVHN-KKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA-----PIKVNKVSKEEA 114
Cdd:TIGR00955 64 KTTLMNALAFRSP---KGVKGSGSVLLNgMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQahlrmPRRVTKKEKRER 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EK---TAMFYLE----KVGIPEKANVyphqLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEG 187
Cdd:TIGR00955 141 VDevlQALGLRKcantRIGVPGRVKG----LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489402728 188 MTMVVVTHEMG---FarEVADRILFMDDGQIIEDTTP---AQFFAN 227
Cdd:TIGR00955 217 KTIICTIHQPSselF--ELFDKIILMAEGRVAYLGSPdqaVPFFSD 260
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
41-217 |
8.32e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkkTDMNE--LRRNIGMVFQHFYLYPHkTVLQNITLApikvnKVSKEEAEKTA 118
Cdd:PRK11160 379 KSTLLQLLTRAWDPQQGEILLNGQPI----ADYSEaaLRQAISVVSQRVHLFSA-TLRDNLLLA-----APNASDEALIE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MfyLEKVGI------PEKANVY----PHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGM 188
Cdd:PRK11160 449 V--LQQVGLeklledDKGLNAWlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NK 525
|
170 180
....*....|....*....|....*....
gi 489402728 189 TMVVVTHEMgFAREVADRILFMDDGQIIE 217
Cdd:PRK11160 526 TVLMITHRL-TGLEQFDRICVMDNGQIIE 553
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-223 |
8.72e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 12 YGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKTdmNELRRNIGMVFQHFYL-- 89
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQNATTpg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 90 ------------YPHKTVLQNItlapikvnKVSKEEAEKTAMfylEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPE 157
Cdd:PRK10253 95 ditvqelvargrYPHQPLFTRW--------RKEDEEAVTKAM---QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489402728 158 IMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
41-195 |
9.78e-17 |
|
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: 78.94 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVqnTEVHNKKTDMNELRRNIGMVFQHFYLYpHKTVLQNITLA-PikvnKVSKEEAEKTam 119
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTL--DGVPVSSLDQDEVRRRVSVCAQDAHLF-DTTVRENLRLArP----DATDEELWAA-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 fyLEKVGIPEKANVYPH-----------QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTlAKEGM 188
Cdd:TIGR02868 445 --LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGR 521
|
....*..
gi 489402728 189 TMVVVTH 195
Cdd:TIGR02868 522 TVVLITH 528
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
138-217 |
1.22e-16 |
|
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: 78.71 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMGFAREvADRILFMDDGQIIE 217
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
41-222 |
1.56e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNkkTDMNELRRNIGMVFQHFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTA 118
Cdd:PRK09536 42 KTTLLRAINGTLTPTAGTVLVAGDDVEA--LSARAASRRVASVPQDTSLSFEFDVRQVVEMGrtPHRSRFDTWTETDRAA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 M-FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEM 197
Cdd:PRK09536 120 VeRAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDL 199
|
170 180
....*....|....*....|....*
gi 489402728 198 GFAREVADRILFMDDGQIIEDTTPA 222
Cdd:PRK09536 200 DLAARYCDELVLLADGRVRAAGPPA 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
138-214 |
4.09e-16 |
|
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: 74.04 E-value: 4.09e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmIGEVL--DVMKTLAKEGMTMVVVTHEMGFAREvADRILFMDDGQ 214
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
41-217 |
8.22e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTdMNELRRNIGMVFQHFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTA 118
Cdd:PRK11288 43 KSTLLKILSGNYQPDAGSILIDGQEMRFAST-TAALAAGVAIIYQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIpekaNVYPHQ----LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVT 194
Cdd:PRK11288 122 REQLEHLGV----DIDPDTplkyLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVS 197
|
170 180
....*....|....*....|...
gi 489402728 195 HEMGFAREVADRILFMDDGQIIE 217
Cdd:PRK11288 198 HRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
134-214 |
1.80e-15 |
|
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: 70.94 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 134 YPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLakEGmTMVVVTHEMGFAREVADRILFMDDG 213
Cdd:cd03221 67 YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY--PG-TVILVSHDRYFLDQVATKIIELEDG 143
|
.
gi 489402728 214 Q 214
Cdd:cd03221 144 K 144
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-221 |
2.22e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKKtdmNELRRNIGM 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA---RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNItLAPIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:PRK13537 85 VPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTP 221
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
77-235 |
2.79e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 72.62 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNItLAPIKVNK-VSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNL-MAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANPEQERARL 235
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-216 |
4.36e-15 |
|
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: 71.66 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKktDMnelrRNIGM 82
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRK--DL----HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQHFYLYPHKTVLQNItlapiKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:TIGR03740 75 LIESPPLYENLTARENL-----KVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
138-215 |
5.54e-15 |
|
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: 73.54 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmiGE--VLDVMKTLAKEGMTMVVVTHEMGfAREVADRILFMDDGQI 215
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-215 |
5.80e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAiTDGGLIVQNTEVHNKKTDMNELRRNIG 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP-PDSGTLEIGGNPCARLTPAKAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHKTVLQNITLAPIKVNKVSKEEAEKtamfyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLF 161
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL-----LAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 162 DEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
138-215 |
1.15e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 1.15e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-229 |
2.07e-14 |
|
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: 71.78 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQL--EAITDGGLIVQNTEVHNKKTDMNElRRN 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTE-RAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHFYLYPHKTVLQNITLA---PIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYP-HQLSGGQQQRVAIARGLAMQ 155
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 156 PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIEdTTPAQFFANPE 229
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA-TKDMSTMSEDD 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
4.32e-14 |
|
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: 69.04 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGN---FQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRR 78
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI--SQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPhKTVLQNIT--LAPIKVNKVsKEEAEKT---------AMFYLEKVGipEKANvyphQLSGGQQQRVA 147
Cdd:cd03248 89 KVSLVGQEPVLFA-RSLQDNIAygLQSCSFECV-KEAAQKAhahsfiselASGYDTEVG--EKGS----QLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 148 IARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTlAKEGMTMVVVTHEMGFArEVADRILFMDDGQI 215
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-218 |
6.37e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.15 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 109 VSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM 188
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|
gi 489402728 189 TMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
77-223 |
7.42e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 77 RRNIGMVFQHFYLYPHKTVLQNITLAP-------IKVNKVSkEEAEKtamfYLEKVGIPEKANVYPHQLSGGQQQRVAIA 149
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNeitpggiMDYDAMY-LRAQK----LLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIeDTTPAQ 223
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI-GTRPAA 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-223 |
1.61e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 6 RNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhNKKTDMNELRRNIGMVFQ 85
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 86 HFYLYPHKTVLQNITLA--PIKVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDE 163
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 164 PTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIeDTTPAQ 223
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI-ATQPLA 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
118-228 |
1.88e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.68 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGIPEKANV---YPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAK-EGMTMVVV 193
Cdd:PRK15093 136 AIELLHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLI 215
|
90 100 110
....*....|....*....|....*....|....*
gi 489402728 194 THEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:PRK15093 216 SHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
40-228 |
1.89e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.39 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 40 GKSTLLRCINqleaitdgGLIVQNTEVHNKK---TDMNELR-----------RNIGMVFQH--FYLYPHKTVLQNITLA- 102
Cdd:COG4170 45 GKSLIAKAIC--------GITKDNWHVTADRfrwNGIDLLKlsprerrkiigREIAMIFQEpsSCLDPSAKIGDQLIEAi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 103 PIKVNKVS----KEEAEKTAMFYLEKVGIPE-KA--NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGE 175
Cdd:COG4170 117 PSWTFKGKwwqrFKWRKKRAIELLHRVGIKDhKDimNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQ 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 176 VLDVMKTLAK-EGMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:COG4170 197 IFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
76-215 |
2.59e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQ---HFYLYPHKTVLQNITLAPI----KVNKVSKEEAEKTAMFYLEKVGI----PEKAnvyPHQLSGGQQQ 144
Cdd:PRK13549 336 IAQGIAMVPEdrkRDGIVPVMGVGKNITLAALdrftGGSRIDDAAELKTILESIQRLKVktasPELA---IARLSGGNQQ 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDpemIG---EVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
137-220 |
2.89e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
....
gi 489402728 217 EDTT 220
Cdd:PRK09700 489 QILT 492
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
41-195 |
3.45e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGglivqntevhnkKTDMNELRRnigMVF--QHFYLyPHKTVLQNITLaPIKVNKVSKEEAEKTa 118
Cdd:COG4178 402 KSTLLRAIAGLWPYGSG------------RIARPAGAR---VLFlpQRPYL-PLGTLREALLY-PATAEAFSDAELREA- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 mfyLEKVGIP-------EKANvYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEvldVMKTLAKE--GMT 189
Cdd:COG4178 464 ---LEAVGLGhlaerldEEAD-WDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA---LYQLLREElpGTT 536
|
....*.
gi 489402728 190 MVVVTH 195
Cdd:COG4178 537 VISVGH 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
133-195 |
5.18e-13 |
|
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: 64.87 E-value: 5.18e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 133 VYP--HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKtlaKEGMTMVVVTH 195
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
41-228 |
6.02e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.82 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRNIGMVFQHFYLYPhKTVLQNITLAPIKVNKVSKEEAEKTAMF 120
Cdd:PRK10789 354 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPFLFS-DTVANNIALGRPDATQQEIEHVARLASV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKanvYPHQ-------LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLaKEGMTMVVV 193
Cdd:PRK10789 431 HDDILRLPQG---YDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIIS 506
|
170 180 190
....*....|....*....|....*....|....*
gi 489402728 194 THEMGFAREvADRILFMDDGQIIEDTTPAQFFANP 228
Cdd:PRK10789 507 AHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
138-230 |
6.99e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHE----MGfareVADRILFMDDG 213
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREG 472
|
90
....*....|....*..
gi 489402728 214 QIIEDTTPAQffANPEQ 230
Cdd:PRK11288 473 RIAGELAREQ--ATERQ 487
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
41-196 |
7.13e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCI-NQLEAITDGGLIVQNtevhNKKTDMNELRRnIGMVFQHFYLYPHKTVLQNITLAPIK--VNKVSKEEAEKT 117
Cdd:PLN03211 107 KSTLLNALaGRIQGNNFTGTILAN----NRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLrlPKSLTKQEKILV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVGIPE-----KANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVV 192
Cdd:PLN03211 182 AESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVT 261
|
....
gi 489402728 193 VTHE 196
Cdd:PLN03211 262 SMHQ 265
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-215 |
8.27e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 8.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
122-243 |
9.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 122 LEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAR 201
Cdd:PRK15056 127 LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVT 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489402728 202 EVADRILfMDDGQIIEDTTPAQFFANPEQERArlfLSRVLNH 243
Cdd:PRK15056 207 EFCDYTV-MVKGTVLASGPTETTFTAENLELA---FSGVLRH 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
139-223 |
1.42e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 139 SGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
....*
gi 489402728 219 TTPAQ 223
Cdd:COG1134 228 GDPEE 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
138-233 |
3.15e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDvmKTLAKEGM----TMVVVTHEMGFAREVaDRILFMDDG 213
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGG 837
|
90 100 110
....*....|....*....|....*....|...
gi 489402728 214 QIIE----------DTTPAQF---FANPEQERA 233
Cdd:TIGR00957 838 KISEmgsyqellqrDGAFAEFlrtYAPDEQQGH 870
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
125-223 |
3.34e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.42 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 125 VGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREV 203
Cdd:PRK10575 135 VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARY 214
|
90 100
....*....|....*....|
gi 489402728 204 ADRILFMDDGQIIEDTTPAQ 223
Cdd:PRK10575 215 CDYLVALRGGEMIAQGTPAE 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
41-195 |
3.63e-12 |
|
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: 63.15 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLeAITDGGLIVQNTEVHNKKTDmnELRRNIGMVFQHFYLYPHKTVLQNIT-LAPIKvnkvskEEAEKTAM 119
Cdd:TIGR01189 39 KTTLLRILAGL-LRPDSGEVRWNGTPLAEQRD--EPHENILYLGHLPGLKPELSALENLHfWAAIH------GGAQRTIE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 120 FYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP---EMIGEVLDvmKTLAKEGMTmVVVTH 195
Cdd:TIGR01189 110 DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKagvALLAGLLR--AHLARGGIV-LLTTH 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
138-229 |
5.19e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVaDRILFMDDGQIIE 217
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKE 819
|
90
....*....|..
gi 489402728 218 DTTPAQFFANPE 229
Cdd:PLN03232 820 EGTFAELSKSGS 831
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-220 |
5.95e-12 |
|
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: 64.76 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYG-NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNkkTDMNELRRNIG 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPhKTVLQNITLAPIKvnKVSKEEAEKTAMFY-----LEKV--GIPEKANVYPHQLSGGQQQRVAIARGLAM 154
Cdd:TIGR01193 552 YLPQEPYIFS-GSILENLLLGAKE--NVSQDEIWAACEIAeikddIENMplGYQTELSEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 155 QPEIMLFDEPTSALDpeMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVaDRILFMDDGQIIEDTT 220
Cdd:TIGR01193 629 DSKVLILDESTSNLD--TITEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
91-218 |
6.13e-12 |
|
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: 64.46 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 91 PHKTVLQNITLAPIK-------VNKVSKEEAEKTAMFYLE-KVGIPEKANVyphQLSGGQQQRVAIARGLAMQPEIMLFD 162
Cdd:TIGR02633 352 PILGVGKNITLSVLKsfcfkmrIDAAAELQIIGSAIQRLKvKTASPFLPIG---RLSGGNQQKAVLAKMLLTNPRVLILD 428
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 163 EPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
138-214 |
7.26e-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: 7.26e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPE--IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREvADRILFMDDGQ 214
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-221 |
8.50e-12 |
|
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: 62.51 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVN-KYYGNFQ-VLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:cd03244 3 IEFKNVSlRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDI--SKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPhKTVLQNitLAPIkvNKVSKEEAEKTamfyLEKVGIPEKANVYPHQL-----------SGGQQQRVAIA 149
Cdd:cd03244 81 SIIPQDPVLFS-GTIRSN--LDPF--GEYSDEELWQA----LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPEmiGEVLdVMKTLAKE--GMTMVVVTHE----MGFarevaDRILFMDDGQIIEDTTP 221
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE--TDAL-IQKTIREAfkDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
138-227 |
9.05e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDvmKTLAKE--GMTMVVVTHEMGFAREVaDRILFMDDGQI 215
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDElrGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
90
....*....|..
gi 489402728 216 IEDTTPAQFFAN 227
Cdd:PLN03130 818 KEEGTYEELSNN 829
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
72-222 |
1.12e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMnELRRNIGMVFQHFYLYPHKTVLQNITL-ApiKVNKVSKEEAEK--TAMfyLEKVGIPEKANVYPHQLSGGQQQRVAI 148
Cdd:NF033858 334 DI-ATRRRVGYMSQAFSLYGELTVRQNLELhA--RLFHLPAAEIAArvAEM--LERFDLADVADALPDSLPLGIRQRLSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 149 ArgLAM--QPEIMLFDEPTSALDP-------EMIGEvldvmktLAKE-GMTMVVVTHEMGFArEVADRILFMDDGQIIED 218
Cdd:NF033858 409 A--VAVihKPELLILDEPTSGVDPvardmfwRLLIE-------LSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLAS 478
|
....
gi 489402728 219 TTPA 222
Cdd:NF033858 479 DTPA 482
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-217 |
1.43e-11 |
|
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: 61.39 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEA--ITDGGLIVQNTEVHNKktDMNE-LRRNIGMVFQHfylyphktvlqnitlaPIKVNKVskeeaekT 117
Cdd:cd03217 39 KSTLAKTIMGHPKyeVTEGEILFKGEDITDL--PPEErARLGIFLAFQY----------------PPEIPGV-------K 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 118 AMFYLEKVgipekaNVyphQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH-E 196
Cdd:cd03217 94 NADFLRYV------NE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQ 164
|
170 180
....*....|....*....|.
gi 489402728 197 MGFAREVADRILFMDDGQIIE 217
Cdd:cd03217 165 RLLDYIKPDRVHVLYDGRIVK 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
40-217 |
1.58e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 40 GKSTLLrciNQLEAIT-----DGGLIVQNTEVHNKKTDMNElRRNIGMVFQHFYLYPHKTVLQNITLApikvNKVSK--- 111
Cdd:NF040905 39 GKSTLM---KVLSGVYphgsyEGEILFDGEVCRFKDIRDSE-ALGIVIIHQELALIPYLSIAENIFLG----NERAKrgv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 112 ---EEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM 188
Cdd:NF040905 111 idwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGI 190
|
170 180
....*....|....*....|....*....
gi 489402728 189 TMVVVTHEMGFAREVADRILFMDDGQIIE 217
Cdd:NF040905 191 TSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-217 |
2.08e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYG--NFQVlKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVHNKktDMNELRRNI 80
Cdd:PRK10522 323 LELRNVTFAYQdnGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE--QPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHktvlqniTLAPikvnkvSKEEAEKTAMF-YLEKVGIPEKANVYPH-----QLSGGQQQRVAIARGLAM 154
Cdd:PRK10522 400 SAVFTDFHLFDQ-------LLGP------EGKPANPALVEkWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 155 QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFArEVADRILFMDDGQIIE 217
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
138-222 |
3.87e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAM---------QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRI 207
Cdd:PRK13547 146 LSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRI 225
|
90
....*....|....*
gi 489402728 208 LFMDDGQIIEDTTPA 222
Cdd:PRK13547 226 AMLADGAIVAHGAPA 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
41-218 |
5.03e-11 |
|
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: 60.62 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLivqntEVHNKKTDMNELrrniGMVFQhfylyPHKTVLQNITLAPIkVNKVSKEEAEKTAMF 120
Cdd:cd03220 61 KSTLLRLLAGIYPPDSGTV-----TVRGRVSSLLGL----GGGFN-----PELTGRENIYLNGR-LLGLSRKEIDEKIDE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFA 200
Cdd:cd03220 126 IIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSI 205
|
170
....*....|....*...
gi 489402728 201 REVADRILFMDDGQIIED 218
Cdd:cd03220 206 KRLCDRALVLEKGKIRFD 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
138-215 |
1.26e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.26e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-213 |
1.54e-10 |
|
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: 60.80 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVhnkKTDMNELRRNIGMVFQ------------HFYLYPhktvlqnitlapiKVNK 108
Cdd:TIGR01257 1978 KTTTFKMLTGDTTVTSGDATVAGKSI---LTNISDVHQNMGYCPQfdaiddlltgreHLYLYA-------------RLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 109 VSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM 188
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180
....*....|....*....|....*
gi 489402728 189 TMVVVTHEMGFAREVADRILFMDDG 213
Cdd:TIGR01257 2122 AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-216 |
2.43e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRC---INQLEAitdGGLIVQNTEVH-NKKTDMNElrRNIGMVFQHFYLYPHKTVLQNITLAPIKVNKVSK----- 111
Cdd:PRK10762 43 KSTMMKVltgIYTRDA---GSILYLGKEVTfNGPKSSQE--AGIGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwkk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 112 --EEAEKtamfYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMT 189
Cdd:PRK10762 118 myAEADK----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRG 193
|
170 180
....*....|....*....|....*..
gi 489402728 190 MVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK10762 194 IVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
138-221 |
3.45e-10 |
|
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: 57.81 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKeGMTMVVVTHEMgfaREVA--DRILFMDDGQI 215
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEV 201
|
....*.
gi 489402728 216 IEDTTP 221
Cdd:cd03369 202 KEYDHP 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
138-213 |
4.17e-10 |
|
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: 57.73 E-value: 4.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD--VMKTLAKEGMTMVVVTHEMGFAREvADRILFMDDG 213
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
41-196 |
4.38e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.80 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKTDmnELRRNIGMVFQHFYLYpHKTVLQNITLaPIKVNKVSKEEAEKTAmf 120
Cdd:PRK10247 46 KSTLLKIVASLISPTSGTLLFEGEDISTLKPE--IYRQQVSYCAQTPTLF-GDTVYDNLIF-PWQIRNQQPDPAIFLD-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPE---KANVypHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHE 196
Cdd:PRK10247 120 DLERFALPDtilTKNI--AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-223 |
5.46e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.93 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCInqleaitdGGLIVQNTEVHNKKTDMN-----ELRRNIGMVFQHFYLYPHKTVLQNITL-APikvNKVSKEEA 114
Cdd:COG4138 35 KSTLLARM--------AGLLPGQGEILLNGRPLSdwsaaELARHRAYLSQQQSPPFAMPVFQYLALhQP---AGASSEAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 115 EKTAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLaMQ--PEI------MLFDEPTSALDPEMIGEVLDVMKTLAKE 186
Cdd:COG4138 104 EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVL-LQvwPTInpegqlLLLDEPMNSLDVAQQAALDRLLRELCQQ 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 489402728 187 GMTMVVVTHEMGFAREVADRILFMDDGQIIEDTTPAQ 223
Cdd:COG4138 183 GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
94-216 |
6.32e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 94 TVLQNITLApiKVNKVSK-----EEAE-KTAMFYLEKVGIpeKA-NVYPH--QLSGGQQQRVAIARGLAMQPEIMLFDEP 164
Cdd:NF040905 356 DIKRNITLA--NLGKVSRrgvidENEEiKVAEEYRKKMNI--KTpSVFQKvgNLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 165 TSALDpemIG---EVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:NF040905 432 TRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
138-216 |
7.29e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLakEGmTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
74-218 |
9.26e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 74 NELRRNIGMVF-QHFYLYPHktvlqnitLAPI-------KVNKVSKEEAEKTAMFYLEKVGIPEKANVYPHQLSGGQQQR 145
Cdd:COG4586 91 KEFARRIGVVFgQRSQLWWD--------LPAIdsfrllkAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMR 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 146 VAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
41-195 |
1.27e-09 |
|
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: 56.35 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLEAITDGGLIVQNTEVHNKKtdmNELRRNIGMVFQHFYLYPHKTVLQNIT-LAPIKvnkvSKEEAEKTam 119
Cdd:cd03231 39 KTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLYLGHAPGIKTTLSVLENLRfWHADH----SDEQVEEA-- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 120 fyLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTH 195
Cdd:cd03231 110 --LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
138-216 |
1.31e-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: 57.64 E-value: 1.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmigEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
138-230 |
1.36e-09 |
|
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: 56.65 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLA-KEGMTMVVVTHEMGFAREVADRILFMdDGQII 216
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAeNNEKTAFVVEHDIIMIDYLADRLIVF-EGEPS 194
|
90
....*....|....
gi 489402728 217 EDTTpaqffANPEQ 230
Cdd:cd03237 195 VNGV-----ANPPQ 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-212 |
1.98e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 72 DMNELRRNIGMVFQHFYLYpHKTVLQNITLAPikvNKVSKEEAEKTAMF-----YLEKVGIPEKANVYPH--QLSGGQQQ 144
Cdd:PTZ00265 1290 NLKDLRNLFSIVSQEPMLF-NMSIYENIKFGK---EDATREDVKRACKFaaideFIESLPNKYDTNVGPYgkSLSGGQKQ 1365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPEmiGEVLdVMKTLA----KEGMTMVVVTHEMGFAREvADRILFMDD 212
Cdd:PTZ00265 1366 RIAIARALLREPKILLLDEATSSLDSN--SEKL-IEKTIVdikdKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
76-226 |
2.53e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.04 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 76 LRRNIGMVFQHFYLYPhKTVLQNITLApikvnkvsKEEAEKTAMFYLEKVGIPEKANVYP-----------HQLSGGQQQ 144
Cdd:PRK10790 413 LRQGVAMVQQDPVVLA-DTFLANVTLG--------RDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQ 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 145 RVAIARGLAMQPEIMLFDEPTSALDPemiGEVLDVMKTLA--KEGMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPA 222
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDS---GTEQAIQQALAavREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQ 559
|
....
gi 489402728 223 QFFA 226
Cdd:PRK10790 560 QLLA 563
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
137-197 |
2.65e-09 |
|
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: 56.72 E-value: 2.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGE---VLDVMKTLAKEGMTMVVVTHEM 197
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
138-230 |
2.83e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIE 217
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
90
....*....|...
gi 489402728 218 DTTPAQffANPEQ 230
Cdd:COG3845 483 EVPAAE--ATREE 493
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
41-217 |
3.37e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.46 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCI--NQLEAITDGglivqntEVHNKKTDMNEL------RRNIGMVFQhfylYPH-----------KTVLQNITL 101
Cdd:COG0396 39 KSTLAKVLmgHPKYEVTSG-------SILLDGEDILELspderaRAGIFLAFQ----YPVeipgvsvsnflRTALNARRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 102 APIKVNKVSKEEAEKtamfyLEKVGIPEK-----ANVyphQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEV 176
Cdd:COG0396 108 EELSAREFLKLLKEK-----MKELGLDEDfldryVNE---GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489402728 177 LDVMKTLAKEGMTMVVVTHemgFAR----EVADRILFMDDGQIIE 217
Cdd:COG0396 180 AEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
122-195 |
3.93e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 3.93e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 122 LEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKT-LAKEGMtMVVVTH 195
Cdd:PRK13539 112 LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGI-VIAATH 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
137-207 |
5.91e-09 |
|
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: 55.07 E-value: 5.91e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGEVLDVMKT---LAKEGMTMVVVTHEMGFAREVADRI 207
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD---IKQRLNAARLireLAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
137-218 |
7.78e-09 |
|
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: 54.26 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
...
gi 489402728 216 IED 218
Cdd:cd03267 233 LYD 235
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-221 |
8.36e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.54 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQ---PEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAReVADRILFM---- 210
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgpeg 248
|
90
....*....|...
gi 489402728 211 --DDGQIIEDTTP 221
Cdd:cd03271 249 gdGGGQVVASGTP 261
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
138-216 |
1.17e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmigEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-197 |
1.81e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.81e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGE---VLDVMKTLAkEGMTMVVVTHEM 197
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-208 |
1.86e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRIL 208
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-207 |
2.66e-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: 52.19 E-value: 2.66e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGM-TMVVVTHEMGFAREVADRI 207
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRI 142
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
130-216 |
3.09e-08 |
|
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: 52.26 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 130 KANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMT-MVVVTHEMGFAREVADRI 207
Cdd:cd03233 111 KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVlKTTtFVSLYQASDEIYDLFDKV 190
|
....*....
gi 489402728 208 LFMDDGQII 216
Cdd:cd03233 191 LVLYEGRQI 199
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-223 |
6.94e-08 |
|
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: 52.71 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGL---AMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAReVADRILFM---- 210
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIK-TADYIIDLgpeg 908
|
90
....*....|....*
gi 489402728 211 --DDGQIIEDTTPAQ 223
Cdd:TIGR00630 909 gdGGGTVVASGTPEE 923
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-210 |
1.03e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFM 210
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
41-213 |
1.09e-07 |
|
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: 50.32 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCinqLEAITDGGLIVQNTEVHNKKTDMNeLRRNIGMVFQHFYLYPHKTVLQNITLApikvnkvskeeaektamf 120
Cdd:cd03232 46 KTTLLDV---LAGRKTAGVITGEILINGRPLDKN-FQRSTGYVEQQDVHSPNLTVREALRFS------------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 ylekvgipekANVypHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMG-- 198
Cdd:cd03232 104 ----------ALL--RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSas 171
|
170
....*....|....*.
gi 489402728 199 -FarEVADRILFMDDG 213
Cdd:cd03232 172 iF--EKFDRLLLLKRG 185
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
138-208 |
1.14e-07 |
|
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: 52.09 E-value: 1.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRIL 208
Cdd:COG1245 456 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
135-195 |
1.17e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 50.73 E-value: 1.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 135 PHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTH 195
Cdd:COG2401 134 FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
122-200 |
1.63e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.19 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 122 LEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGmTMVVVT--HEMGF 199
Cdd:PRK13538 114 LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQG-GMVILTthQDLPV 192
|
.
gi 489402728 200 A 200
Cdd:PRK13538 193 A 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-213 |
1.98e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLeaiTDGGLIVQNTEVHNKKTDMNELRRNIGMVFQHFYLYPHKTVLQNITLAPI--KVNKVSKEEaektA 118
Cdd:TIGR00956 802 KTTLLNVLAER---VTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYlrQPKSVSKSE----K 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEK--------------VGIP-EKANVYphqlsggQQQRVAIARGLAMQPEIMLF-DEPTSALDPEMIGEVLDVMKT 182
Cdd:TIGR00956 875 MEYVEEvikllemesyadavVGVPgEGLNVE-------QRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRK 947
|
170 180 190
....*....|....*....|....*....|....
gi 489402728 183 LAKEGMTMVVVTHE---MGFarEVADRILFMDDG 213
Cdd:TIGR00956 948 LADHGQAILCTIHQpsaILF--EEFDRLLLLQKG 979
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-201 |
2.90e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYG---NFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTevHN-KKTDMNELRR 78
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNlKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 79 NIGMVFQHFYLYPHkTVLQNI--TLAPIK-------------------VNKVSKEEAEKTAMFYL--------------- 122
Cdd:PTZ00265 461 KIGVVSQDPLLFSN-SIKNNIkySLYSLKdlealsnyynedgndsqenKNKRNSCRAKCAGDLNDmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 123 --------------EKVGIPEKANVYP-----------HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmiGEVL 177
Cdd:PTZ00265 540 nyqtikdsevvdvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK--SEYL 617
|
250 260
....*....|....*....|....*...
gi 489402728 178 dVMKTL----AKEGMTMVVVTHEMGFAR 201
Cdd:PTZ00265 618 -VQKTInnlkGNENRITIIIAHRLSTIR 644
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-222 |
3.71e-07 |
|
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: 50.18 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 40 GKSTLLRCINQLEAITDGGLIVQNTEVHnkKTDMNELRRNIGMVFQHFYLYPHktvlqnitLAPIKvnkvsKEEAEKTAM 119
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVT--ADNREAYRQLFSAVFSDFHLFDR--------LLGLD-----GEADPARAR 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 120 FYLEKVGIPEKANVYPH-----QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP--------EMIGEvldvmktLAKE 186
Cdd:COG4615 435 ELLERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLPE-------LKAR 507
|
170 180 190
....*....|....*....|....*....|....*..
gi 489402728 187 GMTMVVVTH-EMGFarEVADRILFMDDGQIIEDTTPA 222
Cdd:COG4615 508 GKTVIAISHdDRYF--DLADRVLKMDYGKLVELTGPA 542
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
139-227 |
3.85e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 139 SGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGEVLDVMKTLAKE--GMTMVVVTHEMGFAREvADRILFMDDGQII 216
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
|
90
....*....|.
gi 489402728 217 EDTTPAQFFAN 227
Cdd:PLN03130 1452 EFDTPENLLSN 1462
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-227 |
6.62e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAmqPEIM----LFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFArEVADRILFMD-- 211
Cdd:PRK00635 477 LSGGEQERTALAKHLG--AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGpg 553
|
90 100
....*....|....*....|
gi 489402728 212 ----DGQIIEDTTPAQFFAN 227
Cdd:PRK00635 554 agifGGEVLFNGSPREFLAK 573
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
75-215 |
6.69e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 75 ELRRNIGMVFQHFYL-YPHKTVLQNITLA----PIKVNKVSKEEAEKTAMFYLEKVGIPEK-ANVYPHQLSGGQQQRVAI 148
Cdd:PRK10938 333 DIKKHIGYVSSSLHLdYRVSTSVRNVILSgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALI 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 149 ARGLAMQPEIMLFDEPTSALDP---EMIGEVLDVMKTlakEGMT-MVVVTHEMGFARE-VADRILFMDDGQI 215
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETqLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-216 |
1.09e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCInqlEAITDGGLIVQNTEVHNKKTDMNELRRN-------IGMVFQHFylyPHKTVLQNITLAP------IKVN 107
Cdd:TIGR00956 100 CSTLLKTI---ASNTDGFHIGVEGVITYDGITPEEIKKHyrgdvvyNAETDVHF---PHLTVGETLDFAArcktpqNRPD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 108 KVSKEE-AEKTAMFYLE----------KVGipekaNVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEV 176
Cdd:TIGR00956 174 GVSREEyAKHIADVYMAtyglshtrntKVG-----NDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEF 248
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 177 LDVMKTLAKEGMTMVVVT--HEMGFAREVADRILFMDDGQII 216
Cdd:TIGR00956 249 IRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-210 |
1.15e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.15e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 136 HQLSGGQQQRVAIARGLAMQPE----IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFArEVADRILFM 210
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELA-ELADKLIHI 153
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2-229 |
1.26e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.19 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQntevhnkktdmNELRrnIG 81
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-----------GKLR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 82 MVFQHFYLYPHK--TVLQNITLAPikvnKVSKEEaektAMFYLEKVGIPEKANVYPHQLSGGQQQRVAIARGLAMQPEIM 159
Cdd:PRK09544 71 YVPQKLYLDTTLplTVNRFLRLRP----GTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 160 LFDEPTSALDPEMIGEVLDVMKTLAKE-GMTMVVVTHEMGFAREVADRILFMdDGQIIEDTTPAQFFANPE 229
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
138-207 |
1.30e-06 |
|
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: 47.64 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489402728 138 LSGGQQQRVAIARGLAMQPE--IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREvADRI 207
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHV 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-216 |
2.14e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCInqleaitdGGLIVQNTEVHNKKTDMNELRRN----------------IGM-VFQhfYLYPHKTVLQNITLAP 103
Cdd:PRK03695 35 KSTLLARM--------AGLLPGSGSIQFAGQPLEAWSAAelarhraylsqqqtppFAMpVFQ--YLTLHQPDKTRTEAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 104 IKVNKVSkeeaektamfylEKVGIPEKANVYPHQLSGGQQQRVAIArGLAMQ--PEI------MLFDEPTSALDpemIGE 175
Cdd:PRK03695 105 SALNEVA------------EALGLDDKLGRSVNQLSGGEWQRVRLA-AVVLQvwPDInpagqlLLLDEPMNSLD---VAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489402728 176 V--LD-VMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK03695 169 QaaLDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
41-208 |
4.29e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLeAITDGGLIVQNTEvHNKKTDMNelrRNIGMVFQHFYLYPHKTVLQNITLapikVNKVSKEEAEKTAMF 120
Cdd:PRK13543 50 KTTLLRVLAGL-LHVESGQIQIDGK-TATRGDRS---RFMAYLGHLPGLKADLSTLENLHF----LCGLHGRRAKQMPGS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 121 YLEKVGIPEKANVYPHQLSGGQQQRVAIARgLAMQPE-IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGF 199
Cdd:PRK13543 121 ALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPApLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYA 199
|
....*....
gi 489402728 200 AREVADRIL 208
Cdd:PRK13543 200 APPVRTRML 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-227 |
6.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 39 SGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNIGMVFQHFYLYPhKTVLQNITlaPIkvnkvsKEEAEKTA 118
Cdd:PLN03232 1273 AGKSSMLNALFRIVELEKGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFS-GTVRFNID--PF------SEHNDADL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 119 MFYLEKVGIPEKANVYPHQL-----------SGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMigEVLdVMKTLAKE- 186
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRT--DSL-IQRTIREEf 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489402728 187 -GMTMVVVTHEMGFAREvADRILFMDDGQIIEDTTPAQFFAN 227
Cdd:PLN03232 1419 kSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-217 |
6.66e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQII 216
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
.
gi 489402728 217 E 217
Cdd:PRK10938 215 E 215
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
138-228 |
6.83e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEmIGE--VLDV-MKTLAkeGMTMVVVTHEMGFArEVADRILFMDDGQ 214
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAH-VGErvVEECfLGALA--GKTRVLATHQVHVV-PRADYVVALGDGR 858
|
90
....*....|....
gi 489402728 215 IIEDTTPAQFFANP 228
Cdd:PTZ00243 859 VEFSGSSADFMRTS 872
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
96-195 |
7.70e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.84 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 96 LQNITLAPIKVNKVSKEEAEKTAMFYLEKVGIPekanVYPHQLSGGQQQ---RVAIARGLAMQPEIMLFDEPTSALDPEM 172
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGGGGE----LPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKL 274
|
90 100
....*....|....*....|...
gi 489402728 173 IGEVLDVMKTLAKEGMTMVVVTH 195
Cdd:pfam13304 275 LRRLLELLKELSRNGAQLILTTH 297
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
138-195 |
7.77e-06 |
|
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: 46.28 E-value: 7.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEvldvMKTLAKE-GMTMVVVTH 195
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY----MYRLCREfGITLFSVSH 637
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-208 |
1.01e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489402728 138 LSGGQQQRVAIARGL---AMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAReVADRIL 208
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-226 |
2.28e-05 |
|
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: 45.32 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYY--GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTEVhnKKTDMNELRRNI 80
Cdd:TIGR00957 1285 VEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI--AKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPHKTvlqNITLAPIkvNKVSKEE---AEKTAMFYLEKVGIPEKANvypHQ-------LSGGQQQRVAIAR 150
Cdd:TIGR00957 1363 TIIPQDPVLFSGSL---RMNLDPF--SQYSDEEvwwALELAHLKTFVSALPDKLD---HEcaeggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 151 GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTlAKEGMTMVVVTHEMGFAREVAdRILFMDDGQIIEDTTPAQFFA 226
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
132-219 |
3.23e-05 |
|
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: 42.75 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 132 NVYPHQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD------VMKTLAKEGMTMVVVTHEMGFAREVAD 205
Cdd:smart00382 55 GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
90
....*....|....
gi 489402728 206 RILFmdDGQIIEDT 219
Cdd:smart00382 135 RRRF--DRRIVLLL 146
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
127-216 |
3.41e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 127 IPEKANVyphqLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIgEVLDVmkTLAKEGMTMVVVTHEMGFAREVADR 206
Cdd:PRK15064 432 IKKSVKV----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATR 504
|
90
....*....|
gi 489402728 207 ILFMDDGQII 216
Cdd:PRK15064 505 IIEITPDGVV 514
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
138-216 |
5.07e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGF-AREVADRILFMD-DGQI 215
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKrGGQV 1099
|
.
gi 489402728 216 I 216
Cdd:PLN03140 1100 I 1100
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
137-182 |
8.55e-05 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 40.30 E-value: 8.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 137 QLSGGQQQR---VAIARGLAMQ----------PEIMLFDEPTSALDPEMIGEVLDVMKT 182
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
80-215 |
1.01e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQHF--YLYPHKTVLQNIT-LAPikvnkvskEEAEKTAMFYLEKVGIP-EKANVYPHQLSGGQQQRVAIARGLAMQ 155
Cdd:PRK10636 377 LGYFAQHQleFLRADESPLQHLArLAP--------QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQR 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489402728 156 PEIMLFDEPTSALDpemigevLDVMKTLAK-----EGmTMVVVTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK10636 449 PNLLLLDEPTNHLD-------LDMRQALTEalidfEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
139-233 |
1.23e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 139 SGGQQQRVAIARGLAMQPEIMLFDEPTSALDpemIGEVLDVMKTLAKEGMTMVVVTHEMGFAREVADRILFMDDGQIIED 218
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
90
....*....|....*
gi 489402728 219 TTPAQFFanpEQERA 233
Cdd:PRK10636 228 TGNYSSF---EVQRA 239
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-215 |
1.46e-04 |
|
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: 42.15 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYY--GNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLeAITDGGliVQNTEVHNKKTDMNELRRNI 80
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGD--IQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 81 GMVFQHFYLYPhKTVLQNitLAPikVNKVSKEEAEKTAmfylEKVGIPEKANVYPHQL-----------SGGQQQRVAIA 149
Cdd:cd03289 80 GVIPQKVFIFS-GTFRKN--LDP--YGKWSDEEIWKVA----EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 150 RGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTlAKEGMTMVVVTHEMGFAREvADRILFMDDGQI 215
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
138-214 |
1.49e-04 |
|
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: 42.15 E-value: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD--VMKTLAKEgmTMVVVTHEMGFAREvADRILFMDDGQ 214
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
137-207 |
1.91e-04 |
|
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: 41.05 E-value: 1.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489402728 137 QLSGGQQQ------RVAIARGLAMQPEIMLFDEPTSALDPEMIGEVL-DVMK-TLAKEGMTMVVVTHEmgfaREVADRI 207
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEeRKSQKNFQLIVITHD----EELVDAA 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
138-213 |
2.55e-04 |
|
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: 41.82 E-value: 2.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLD--VMKTLAKEgmTMVVVTHEMGFAREvADRILFMDDG 213
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-229 |
3.21e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIAR--GLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMGFAREvADRILFM----- 210
Cdd:TIGR00630 489 LSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRA-ADYVIDIgpgag 567
|
90 100
....*....|....*....|
gi 489402728 211 -DDGQIIEDTTPAQFFANPE 229
Cdd:TIGR00630 568 eHGGEVVASGTPEEILANPD 587
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
114-215 |
4.01e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 114 AEKTAMFYLEKVGIPEKANVYP-HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVmktLAKEGMTMVV 192
Cdd:PRK15064 131 AEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
90 100
....*....|....*....|...
gi 489402728 193 VTHEMGFAREVADRILFMDDGQI 215
Cdd:PRK15064 208 ISHDRHFLNSVCTHMADLDYGEL 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-242 |
4.20e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAM---QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMgfarEV---ADRILfmd 211
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktADWII--- 899
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489402728 212 D---------GQIIEDTTPAQFFANPEQERARlFLSRVLN 242
Cdd:COG0178 900 DlgpeggdggGEIVAEGTPEEVAKVKASYTGR-YLKEYLE 938
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-215 |
4.90e-04 |
|
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: 40.69 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 3 IEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEAITDGGLIVQNTeVHnkktdmnelrrnIGM 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-VK------------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 83 VFQ-HFYLYPHKTVLQNIT--LAPIKVNKVSKEEAEKTAMFYL------EKVGipekanvyphQLSGGQQQRVAIARGLA 153
Cdd:TIGR03719 390 VDQsRDALDPNKTVWEEISggLDIIKLGKREIPSRAYVGRFNFkgsdqqKKVG----------QLSGGERNRVHLAKTLK 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489402728 154 MQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKegmTMVVVTHEMGFAREVADRIL-FMDDGQI 215
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFAG---CAVVISHDRWFLDRIATHILaFEGDSHV 519
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
124-235 |
4.97e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.76 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 124 KVGIPEKANVYPHQLSGGQQQRVAIARGLAM-------QPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHE 196
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489402728 197 MGFAREV-ADRILFMDDGQiiEDTTPAQFFANPEQERARL 235
Cdd:COG3593 229 PHLLSEVpLENIRRLRRDS--GGTTSTKLIDLDDEDLRKL 266
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-217 |
5.22e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 2 LIEFRNVNKYYGNFQVLKNINVQVKKGEVVVVVGPSGSGKSTLLRCINQLEA--ITDGGLIVQNTEVHNKKTDMNElRRN 79
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERA-HLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 80 IGMVFQhfylYPHK-TVLQNITLAPIKVNKVSKEE--AEKTAMFYLEKvgIPEKANVY---PHQL--------SGGQQQR 145
Cdd:CHL00131 86 IFLAFQ----YPIEiPGVSNADFLRLAYNSKRKFQglPELDPLEFLEI--INEKLKLVgmdPSFLsrnvnegfSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489402728 146 VAIARGLAMQPEIMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHemgFARE----VADRILFMDDGQIIE 217
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIK 232
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-242 |
5.38e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPE---IMLFDEPTSALDPEMIGEVLDVMKTLAKEGMTMVVVTHEMgfarEV---ADRILfmd 211
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNL----DViktADWII--- 903
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489402728 212 D---------GQIIEDTTPAQFFANPEQERARlFLSRVLN 242
Cdd:PRK00349 904 DlgpeggdggGEIVATGTPEEVAKVEASYTGR-YLKPVLE 942
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
137-226 |
5.59e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 137 QLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDP-------EMIGEVLDvmktlAKEGMTMVVVTHEMgfarEVADR--- 206
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRA-----ERPGMSVLVATAYM----EEAERfdw 206
|
90 100
....*....|....*....|
gi 489402728 207 ILFMDDGQIIEDTTPAQFFA 226
Cdd:NF033858 207 LVAMDAGRVLATGTPAELLA 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
136-215 |
8.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 136 HQLSGGQQQRVAIARGLAMQPEIMLFDEPTSALDPEMIgEVLDVMKTLAKEGMTMvvVTHEMGFAREVADRILFMDDGQI 215
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EALIQGLVLFQGGVLM--VSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
138-226 |
1.11e-03 |
|
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: 39.12 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 138 LSGGQQQRVAIARGLAMQPEIMLFDEPTSALDpeMIGE-VLDVMKTLAKEGMTMVVVTHEMGFAREvADRILFMDDGQII 216
Cdd:cd03288 157 FSVGQRQLFCLARAFVRKSSILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
90
....*....|
gi 489402728 217 EDTTPAQFFA 226
Cdd:cd03288 234 ECDTPENLLA 243
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
137-186 |
2.91e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.01 E-value: 2.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489402728 137 QLSGGQQQRVAIARGLAMQ---PEIM-LFDEPTSALDPEMIGEVLDVMKTLAKE 186
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdPAPFyLFDEIDAALDAQYRTAVANMIKELSDG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
41-170 |
3.08e-03 |
|
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: 38.74 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 41 KSTLLRCINQLeAITDGGliVQNTEVHNKKTDMNELRRNIGMVFQHFYLYPhKTVLQNitLAPIKvnKVSKEEAEKTAmf 120
Cdd:TIGR01271 1258 KSTLLSALLRL-LSTEGE--IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFS-GTFRKN--LDPYE--QWSDEEIWKVA-- 1327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 121 ylEKVGIPEKANVYPHQL-----------SGGQQQRVAIARGLAMQPEIMLFDEPTSALDP 170
Cdd:TIGR01271 1328 --EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
139-227 |
4.24e-03 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 37.58 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489402728 139 SGGQQQRVAIARGLAMQPEIMLFDEPTSA-----LDPEM----------IGEVLDVMKTLAKE-GMTMVVVTHEMGFARE 202
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMqalvskdkepITPFVDRVRSLYDDlGVSTILVVGGSGDYLD 238
|
90 100
....*....|....*....|....*
gi 489402728 203 VADRILFMDDGQIIEDTTPAQFFAN 227
Cdd:pfam09818 239 VADTVILMDEYRPSDVTEEAKEIAE 263
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
135-195 |
9.33e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.14 E-value: 9.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489402728 135 PHQLSGGQQQRVAIARGLAmqpeiMLFDepTSALDPEMIGEVLDVMKTLAkegmtmvVVTH 195
Cdd:COG0419 156 IETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA-------IITH 202
|
|
| |
