|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
30-267 |
0e+00 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 508.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGM 109
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLSQI 267
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-242 |
7.37e-154 |
|
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: 427.33 E-value: 7.37e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGM 109
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
28-269 |
9.76e-126 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 357.96 E-value: 9.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 28 VAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-----------ND 96
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 LKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIA 176
Cdd:COG4598 87 RRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 177 RALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
250
....*....|...
gi 489053699 257 HERTRLFLSQILH 269
Cdd:COG4598 247 SERLRQFLSSSLK 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-267 |
2.94e-117 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 335.52 E-value: 2.94e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGM 109
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLSQI 267
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-268 |
7.17e-98 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 287.03 E-value: 7.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIE------LTNDLKKIDE 102
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarsLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMN 182
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRL 262
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 489053699 263 FLSQIL 268
Cdd:PRK11264 243 FLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
30-268 |
1.18e-95 |
|
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: 281.33 E-value: 1.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-----------DLK 98
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 99 KIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQH 257
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 489053699 258 ERTRLFLSQIL 268
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
30-269 |
2.24e-93 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 278.50 E-value: 2.24e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGErIV-VAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKID--E 102
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT-ALSERElrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMN 182
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTR 261
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
....*...
gi 489053699 262 LFLSQILH 269
Cdd:COG1135 239 RFLPTVLN 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
29-265 |
9.42e-91 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 268.42 E-value: 9.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG--IELTNDL--KKIDEVR 104
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPseKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPdEFFDNPQHERTRLFL 264
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAFAHYL 240
|
.
gi 489053699 265 S 265
Cdd:COG4161 241 S 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
29-265 |
1.04e-89 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 265.72 E-value: 1.04e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG----IELTNDLKKIDEVR 104
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEfFDNPQHERTRLFL 264
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTEAFKNYL 240
|
.
gi 489053699 265 S 265
Cdd:PRK11124 241 S 241
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
26-264 |
3.96e-87 |
|
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: 259.14 E-value: 3.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVR 104
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPqHERTRLF 263
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQF 240
|
.
gi 489053699 264 L 264
Cdd:COG1127 241 L 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
27-245 |
9.82e-87 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 257.66 E-value: 9.82e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYG----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKID 101
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 EVRRE-VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALC 180
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 181 MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQ 245
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
29-265 |
1.18e-86 |
|
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: 258.38 E-value: 1.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEE-----HQKGKIVVDGIELTNDLKKIDEV 103
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 104 RREVGMVFQHFNLFPhLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQ----ANKYPGQLSGGQQQRVAIARAL 179
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHER 259
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*.
gi 489053699 260 TRLFLS 265
Cdd:TIGR00972 239 TEDYIS 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-268 |
3.08e-86 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 257.59 E-value: 3.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT----------- 94
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 95 NDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQAN-KYPGQLSGGQQQRV 173
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 174 AIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|....*
gi 489053699 254 NPQHERTRLFLSQIL 268
Cdd:PRK10619 242 NPQSPRLQQFLKGSL 256
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-267 |
6.89e-82 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 254.83 E-value: 6.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 24 SKTEVAIEITNMHKWY-----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DL 97
Cdd:COG1123 255 AAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKIDEVRREVGMVFQH-FN-LFPHLTILEncTLA-PIWVRK-MPKKQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQR 172
Cdd:COG1123 335 RSLRELRRRVQMVFQDpYSsLNPRMTVGD--IIAePLRLHGlLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 173 VAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
250
....*....|....*.
gi 489053699 252 FDNPQHERTRLFLSQI 267
Cdd:COG1123 493 FANPQHPYTRALLAAV 508
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
30-256 |
2.54e-81 |
|
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: 244.03 E-value: 2.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKID--EV 103
Cdd:cd03258 2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-LLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 104 RREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
29-267 |
5.55e-81 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 243.81 E-value: 5.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWY-GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-NDLKKIDEVRRE 106
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENcTLA------PIW--VRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTN-VLAgrlgrtSTWrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVeqnspdefFDNPQH 257
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVV--------FDGPPA 232
|
250
....*....|
gi 489053699 258 ERTRLFLSQI 267
Cdd:COG3638 233 ELTDAVLREI 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
30-269 |
6.90e-81 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 247.02 E-value: 6.90e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVR 104
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLF 263
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*.
gi 489053699 264 LSQILH 269
Cdd:PRK11153 241 IQSTLH 246
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
30-242 |
1.04e-79 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 239.70 E-value: 1.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVR 104
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 RE-VGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQI 242
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
30-256 |
2.97e-79 |
|
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: 238.77 E-value: 2.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNM-HKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVG 108
Cdd:COG1122 1 IELENLsFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK--KNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQhfN----LFpHLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:COG1122 79 LVFQ--NpddqLF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-251 |
8.60e-78 |
|
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: 235.54 E-value: 8.60e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE-FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTND-LKKIDEVRREV 107
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTLA-----PIW--VRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALC 180
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrSTWrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 181 MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
30-241 |
1.31e-77 |
|
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: 232.85 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGM 109
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApiwvrkmpkkqaeeiamhylervkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
30-256 |
2.57e-77 |
|
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: 233.93 E-value: 2.57e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKID--EVRREV 107
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS-GLSEAElyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTLapiWVR---KMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAF---PLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF--DNPQ 256
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
26-256 |
8.74e-77 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 236.92 E-value: 8.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEV-- 103
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-------RDVTGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 104 -RREVGMVFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCM 181
Cdd:COG3842 75 eKRNVGMVFQDYALFPHLTVAEN--VAfGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 182 NPKVMLFDEPTSALDP----EMVKEVLDTmvsLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG3842 153 EPRVLLLDEPLSALDAklreEMREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
30-244 |
1.91e-76 |
|
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: 231.25 E-value: 1.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGM 109
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:cd03259 77 VFQDYALFPHLTVAEN--IAfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
30-256 |
3.13e-75 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 232.73 E-value: 3.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKkideVR-REVG 108
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP----PReRRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILEN--CTLApiwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:COG1118 79 FVFQHYALFPHMTVAENiaFGLR---VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 187 LFDEPTSALD----PEMVKEVLDTmvsLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG1118 156 LLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
24-244 |
4.11e-75 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 229.21 E-value: 4.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 24 SKTEVAIEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKK 99
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 100 IDEVRREVGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 180 CMNPKVMLFDEPTSALDP----EMVKEVLDTmvsLAAEGMTMICVTHEMGFARQVANRVIFMDQ--GQIVE 244
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-265 |
1.32e-74 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 228.00 E-value: 1.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 24 SKTEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ-----KGKIVVDGIELTNdlK 98
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIYD--P 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 99 KID--EVRREVGMVFQHFNLFPHlTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQA----NKYPGQLSGGQQQR 172
Cdd:COG1117 84 DVDvvELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 173 VAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|...
gi 489053699 253 DNPQHERTRLFLS 265
Cdd:COG1117 242 TNPKDKRTEDYIT 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
30-251 |
1.66e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 226.87 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKkidEVRREVGM 109
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA---EVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
30-251 |
2.61e-73 |
|
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: 223.60 E-value: 2.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQK-----GKIVVDGIELTNDLKKIDEVR 104
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPhLTILENCTLAPiWVRKM-PKKQAEEIAMHYLERVKIPEQANK--YPGQLSGGQQQRVAIARALCM 181
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 182 NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
29-264 |
9.43e-73 |
|
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: 222.76 E-value: 9.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGE----FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKidEVR 104
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--AFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQH----FNlfPHLTILEncTLA-PIWVRKMPKKQAEEIAMhyLERVKIPEQ-ANKYPGQLSGGQQQRVAIARA 178
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDR--ILAePLRIHGLPDREERIAEL--LEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQH 257
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*..
gi 489053699 258 ERTRLFL 264
Cdd:COG1124 233 PYTRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-246 |
9.54e-72 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 219.68 E-value: 9.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRR 105
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 -EVGMVFQH----FNlfPHLTILEncTLA-PIWVRKMPKKQAE--EIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIA 176
Cdd:cd03257 82 kEIQMVFQDpmssLN--PRMTIGE--QIAePLRIHGKLSKKEArkEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 177 RALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQN 246
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
45-263 |
2.21e-70 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 217.51 E-value: 2.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 122
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:cd03294 120 LENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 203 VLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLF 263
Cdd:cd03294 199 MQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
29-257 |
2.79e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 217.63 E-value: 2.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVG 108
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:COG3839 79 MVFQSYALYPHMTVYEN--IAfPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 188 FDEPTSALDPEMvkevldtMVSLAAE--------GMTMICVTHEmgfarQV-----ANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:COG3839 157 LDEPLSNLDAKL-------RVEMRAEikrlhrrlGTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDR 224
|
...
gi 489053699 255 PQH 257
Cdd:COG3839 225 PAN 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
30-253 |
4.78e-69 |
|
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: 213.31 E-value: 4.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFH-VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRREV 107
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTLA--------PIWVRKMPKKQaEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
30-245 |
7.91e-69 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 211.95 E-value: 7.91e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVRR 105
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKV 185
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 186 MLFDEPTSALDpEMVKEVL-DTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQ--GQIVEQ 245
Cdd:cd03293 153 LLLDEPFSALD-ALTREQLqEELLDIWREtGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-265 |
9.18e-69 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 215.30 E-value: 9.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ---KGKIVVDGIELTN-DLKKID 101
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 EVR-REVGMVFQH----FNlfPHLTILEncTLA-PIWV-RKMPKKQAEEIAMHYLERVKIP---EQANKYPGQLSGGQQQ 171
Cdd:COG0444 82 KIRgREIQMIFQDpmtsLN--PVMTVGD--QIAePLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 172 RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
250
....*....|....*
gi 489053699 251 FFDNPQHERTRLFLS 265
Cdd:COG0444 238 LFENPRHPYTRALLS 252
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-244 |
1.57e-68 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 211.06 E-value: 1.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFH-VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLK--KIDEVRRE 106
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
30-266 |
5.56e-68 |
|
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: 210.62 E-value: 5.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFH-VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKIDEV--RRE 106
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQDPVelRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQ--ANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLF 263
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 489053699 264 LSQ 266
Cdd:cd03295 236 VGA 238
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
45-255 |
5.07e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 212.66 E-value: 5.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 122
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRRKkMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP----E 198
Cdd:COG4175 123 LENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrE 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 199 MVKEVLDtmvsLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:COG4175 202 MQDELLE----LQAKlKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
27-256 |
6.19e-66 |
|
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: 213.61 E-value: 6.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWY--GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ---KGKIVVDGIELTNdlKKID 101
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE--LSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 EVRREVGMVFQHF--NLFPhLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:COG1123 80 LRGRRIGMVFQDPmtQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
30-264 |
1.46e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 206.48 E-value: 1.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE-FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEV--RRE 106
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDG----EDIRDLDPVelRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKI-PEQ-ANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLdPEEyRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPeMVKEVL-DTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRL 262
Cdd:COG1125 157 ILLMDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
..
gi 489053699 263 FL 264
Cdd:COG1125 236 FV 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
44-241 |
5.77e-65 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 201.93 E-value: 5.77e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQHFNL-FPHLTI 122
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVGLVFQNPDDqFFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:cd03225 94 EEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 489053699 203 VLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:cd03225 173 LLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
30-256 |
1.38e-64 |
|
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: 201.70 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGM 109
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
30-256 |
3.55e-63 |
|
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: 198.04 E-value: 3.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDE-VRREVG 108
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG--LPPHEiARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENCTLAP---------IWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVAAqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
30-255 |
4.48e-62 |
|
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: 199.11 E-value: 4.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEVRREVGM 109
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGG----RDITRLPPQKRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCT--LAPiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAygLKN---RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 188 FDEPTSALDPEmVKEVLDT-MVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:TIGR03265 158 LDEPLSALDAR-VREHLRTeIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
45-264 |
5.67e-61 |
|
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: 196.61 E-value: 5.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRR-EVGMVFQHFNLFPHLTI 122
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKqSPVELREVRRkKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPiWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 203 VLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFL 264
Cdd:TIGR01186 168 MQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-252 |
6.04e-61 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 193.42 E-value: 6.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY--GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlKKIDEVRREV 107
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE-ENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQH-FNLFPHLTI-------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFF 252
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
29-256 |
1.35e-60 |
|
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: 191.78 E-value: 1.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEVRREVG 108
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDATDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENCTLA----PIWVRKmPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGlrvkPRSERP-PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-261 |
5.68e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.60 E-value: 5.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 25 KTEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVR 104
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNL---FPhLTILE---NCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:COG1121 75 RRIGYVPQRAEVdwdFP-ITVRDvvlMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEqNSPDEFFDNPQHE 258
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLS 232
|
...
gi 489053699 259 RTR 261
Cdd:COG1121 233 RAY 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
30-254 |
8.57e-59 |
|
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: 186.49 E-value: 8.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKKIDEVRREVGM 109
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEeiamhyLERV-----KIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG-AYARRRAKRKAR------LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-244 |
1.38e-58 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 186.10 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 21 MQVSkTEVAIEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnd 96
Cdd:COG4181 1 MSSS-SAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 lkKIDE-----VRRE-VGMVFQHFNLFPHLTILENCTLaPIWVRKMPkkQAEEIAMHYLERVKIPEQANKYPGQLSGGQQ 170
Cdd:COG4181 78 --ALDEdararLRARhVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 171 QRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVE 244
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
30-242 |
2.62e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 184.63 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGM 109
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHlTILENctLAPIWVRKmPKKQAEEIAMHYLERVKIPEQANKYP-GQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:COG4619 79 VPQEPALWGG-TVRDN--LPFPFQLR-ERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-264 |
3.41e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 185.34 E-value: 3.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVlrDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlkKIDEVRREVGM 109
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT----ALPPAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApiwVRkmP--------KKQAEEIAmhylERVKIPEQANKYPGQLSGGQQQRVAIARALCM 181
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLG---LR--PglkltaeqRAQVEQAL----ERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 182 NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERT 260
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
....
gi 489053699 261 RLFL 264
Cdd:COG3840 227 AAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-265 |
5.85e-58 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 184.85 E-value: 5.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHvLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKKIdevRREVGM 109
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-LPPE---KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 190 EPTSALDPEmVKEVLDTMVSLAAE--GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLS 265
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
41-256 |
7.13e-58 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 185.73 E-value: 7.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKK-IDEVRREVGMVFQhfnlFPH 119
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKDLRKKVGLVFQ----FPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 -----LTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:TIGR04521 93 hqlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 194 ALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
30-251 |
7.94e-58 |
|
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: 184.68 E-value: 7.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlKKIDEVRREVGM 109
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR---KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
26-256 |
1.72e-57 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 184.09 E-value: 1.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRR 105
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 eVGMV--FQHFNLFPHLTILENCTLA--------------PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQ 169
Cdd:COG0411 79 -LGIArtFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 170 QQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSP 248
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 489053699 249 DEFFDNPQ 256
Cdd:COG0411 238 AEVRADPR 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
29-250 |
3.73e-57 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 183.32 E-value: 3.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRRE 106
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR----DLASLSrrELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILEncTLA-------PIWVRkmPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRE--LVAlgryphlGLFGR--PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
30-242 |
6.04e-57 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 179.90 E-value: 6.04e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdevRREVGM 109
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV---KRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENctlapiwvrkmpkkqaeeiamhyLErvkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03230 78 LPEEPSLYENLTVREN-----------------------LK--------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
30-244 |
8.71e-57 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 180.91 E-value: 8.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGiELTNDLKKIDevrREVGM 109
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-RDVTDLPPKD---RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
29-269 |
1.66e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.90 E-value: 1.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEVRREVG 108
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENCTLApiwVRKMPKKQ---AEEI---AMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMN 182
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFG---LTVLPRRErpnAAAIkakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTR 261
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVL 234
|
....*...
gi 489053699 262 LFLSQILH 269
Cdd:PRK10851 235 EFMGEVNR 242
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
31-256 |
1.94e-56 |
|
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: 180.95 E-value: 1.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 31 EITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDE-VRREVGM 109
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPPHRiARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPiWVRKMPKKQAEEIAM--HYLERVKipEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGA-YARRDRAEVRADLERvyELFPRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-268 |
4.73e-56 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 180.42 E-value: 4.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGIELTNDLKKID 101
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 EVRREVGMVFQHFNLFPHLTILENCTLApIWVRKM--PKKQAEEIAMHYLERV----KIPEQANKYPGQLSGGQQQRVAI 175
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 176 ARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
250
....*....|...
gi 489053699 256 QHERTRLFLSQIL 268
Cdd:PRK14267 240 EHELTEKYVTGAL 252
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
32-237 |
5.48e-54 |
|
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: 173.57 E-value: 5.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 32 ITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRRE-VGM 109
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRKmPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFM 237
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
31-241 |
6.47e-54 |
|
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: 171.66 E-value: 6.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 31 EITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMV 110
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 111 FQhfnlfphltilenctlapiwvrkmpkkqaeeiamhylervkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-250 |
8.68e-54 |
|
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: 185.04 E-value: 8.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 15 EVDRSKMQVSKTEVAIEITNMHKWYGEFH--VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIe 92
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 93 ltnDLKKID--EVRREVGMVFQHFNLFpHLTILENCTLapiWVRKMPKKQAEEIAmhylERVKIPEQANKYP-------- 162
Cdd:COG2274 538 ---DLRQIDpaSLRRQIGVVLQDVFLF-SGTIRENITL---GDPDATDEEIIEAA----RLAGLHDFIEALPmgydtvvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 163 ---GQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQvANRVIFMDQ 239
Cdd:COG2274 607 eggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDK 684
|
250
....*....|.
gi 489053699 240 GQIVEQNSPDE 250
Cdd:COG2274 685 GRIVEDGTHEE 695
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
30-241 |
3.66e-53 |
|
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: 171.66 E-value: 3.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY-GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGiELTNDL--KKIDEVRRE 106
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAG-EDVNRLrgRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-267 |
8.48e-53 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 174.53 E-value: 8.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 23 VSKTEVAIEITNMHKWY-----------GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGI 91
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 92 ELTN-DLKKIDEVRREVGMVFQ--HFNLFPHLTILEncTLA-PIWVRKM-PKKQAEEIAMHYLERVKI-PEQANKYPGQL 165
Cdd:COG4608 81 DITGlSGRELRPLRRRMQMVFQdpYASLNPRMTVGD--IIAePLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 166 SGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260
....*....|....*....|...
gi 489053699 245 QNSPDEFFDNPQHERTRLFLSQI 267
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAV 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
40-264 |
1.46e-52 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 178.72 E-value: 1.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL----EEHQKGKIVVDGIELTN-DLKKIDEVR-REVGMVFQH 113
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGlSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 ----FNlfPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANK---YPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:COG4172 101 pmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFL 264
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
30-241 |
5.37e-52 |
|
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: 167.17 E-value: 5.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFH--VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRR 105
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV----DLRDLDleSLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFpHLTILENctlapiwvrkmpkkqaeeiamhylervkIpeqankypgqLSGGQQQRVAIARALCMNPKV 185
Cdd:cd03228 77 NIAYVPQDPFLF-SGTIREN----------------------------I----------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 186 MLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQvANRVIFMDQGQ 241
Cdd:cd03228 118 LILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
30-255 |
1.06e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 172.82 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGM 109
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApiwvRKMPKKQAEEIA---MHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFG----LRMQKTPAAEITprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-269 |
4.79e-51 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 167.40 E-value: 4.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGieltNDLKKID--E 102
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDG----QDIFKMDviE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRREVGMVFQHFNLFPHLTILENCTLAPIWVRKM-PKKQAEEIAMHYLERVKIPEQA----NKYPGQLSGGQQQRVAIAR 177
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 178 ALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQH 257
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
250
....*....|..
gi 489053699 258 ERTRLFLSQILH 269
Cdd:PRK14247 239 ELTEKYVTGRLY 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-261 |
1.02e-50 |
|
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: 173.72 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWY-----------GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQkGKIVVDGIELTN 95
Cdd:COG4172 273 PPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 96 -DLKKIDEVRREVGMVFQ----HFNlfPHLTILEncTLA-PIWV--RKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLS 166
Cdd:COG4172 352 lSRRALRPLRRRMQVVFQdpfgSLS--PRMTVGQ--IIAeGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 167 GGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:COG4172 428 GGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQ 507
|
250
....*....|....*.
gi 489053699 246 NSPDEFFDNPQHERTR 261
Cdd:COG4172 508 GPTEQVFDAPQHPYTR 523
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
45-193 |
8.81e-50 |
|
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: 160.89 E-value: 8.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdeVRREVGMVFQHFNLFPHLTILE 124
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS--LRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 125 NCTLAPIwVRKMPKKQAEEIAMHYLERVKIPEQAN----KYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
44-242 |
1.29e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 162.97 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN--DLKKIDEVRREVGMVFQHFNLFPHLT 121
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:NF038007 100 IFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489053699 202 EVLDTMVSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQI 242
Cdd:NF038007 179 AVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-242 |
5.68e-49 |
|
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: 161.04 E-value: 5.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY-GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLKK--IDEVRRE 106
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMhYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPA-ALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-245 |
8.32e-49 |
|
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: 160.35 E-value: 8.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVlrDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGM 109
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA----APPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMhYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
39-240 |
2.01e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 159.62 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVRREVGMVFQHFNL-- 116
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 -FPhLTILE----NCTLAPIWVRKMPKKQAEEIaMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:cd03235 82 dFP-ISVRDvvlmGLYGHKGLFRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQG 240
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
37-250 |
2.32e-48 |
|
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: 162.17 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 37 KWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlKKIDEVRREVGMVFQHFNL 116
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV---REPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 FPHLTILENCTL-APIWvrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSAL 195
Cdd:TIGR01188 78 DEDLTGRENLEMmGRLY--GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 196 DPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
44-250 |
3.72e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.03 E-value: 3.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFpHLT 121
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTleSLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLAPI------------------WVRKMPKKQAEEIAmhylER-VKipeqankypgqLSGGQQQRVAIARALCMN 182
Cdd:COG1132 430 IRENIRYGRPdatdeeveeaakaaqaheFIEALPDGYDTVVG----ERgVN-----------LSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDE 250
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
27-256 |
3.93e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 160.54 E-value: 3.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFH--VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVR 104
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQH-FNLFPHLTI-------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIA 176
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 177 RALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGM-TMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
.
gi 489053699 256 Q 256
Cdd:PRK13632 234 E 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
31-245 |
8.07e-48 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 156.83 E-value: 8.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 31 EITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLKKIdEVRREVGMV 110
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPK-ELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 111 FQhfnlfphltilenctlapiwvrkmpkkqaeeiamhYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
45-264 |
9.39e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 163.28 E-value: 9.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 122
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 203 VLDTMVSLAAEGM-TMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFL 264
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
28-250 |
1.56e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 166.09 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 28 VAIEITNMH-KWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVRRE 106
Cdd:COG4988 335 PSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--DPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFpHLTILENCTLApiwvrkmpKKQAEEIAMHY-LERVKIPEQANKYPG-----------QLSGGQQQRVA 174
Cdd:COG4988 413 IAWVPQNPYLF-AGTIRENLRLG--------RPDASDEELEAaLEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 175 IARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDE 250
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
30-255 |
2.41e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 161.04 E-value: 2.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEvrREVGM 109
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQ--RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApiwvRKMPKKQAEEIAMHY---LERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG----LKMLGVPKEERKQRVkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
44-250 |
4.22e-47 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 164.94 E-value: 4.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKiDEVRREVGMVFQHfnlfPHL--- 120
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDE-DDLRRRIAVVPQR----PHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 121 TILENCTLApiwvrkmpKKQAEEIAM-HYLERVKIPEQANKYPG-----------QLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:COG4987 424 TLRENLRLA--------RPDATDEELwAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSlAAEGMTMICVTHEM-GFARqvANRVIFMDQGQIVEQNSPDE 250
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLaGLER--MDRILVLEDGRIVEQGTHEE 555
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
39-255 |
7.75e-47 |
|
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: 159.88 E-value: 7.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVlrDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKID---EvRREVGMVFQHFN 115
Cdd:COG4148 11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlppH-RRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 LFPHLTILENCT--LAPIWVRKMPKKQAEEIAM----HYLERvkipeqankYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG4148 88 LFPHLSVRGNLLygRKRAPRAERRISFDEVVELlgigHLLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-243 |
1.37e-46 |
|
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: 154.76 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKV---MRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKID--EVRREVGMVFQHFNLFPH 119
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlpPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 LTILENCTLAPIWVRKMPKK-QAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPE 198
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRiSVDEL----LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489053699 199 MVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
62-267 |
2.36e-46 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 157.66 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQA 141
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 142 EEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICV 220
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVFV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489053699 221 THEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLSQI 267
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-265 |
2.78e-46 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 155.32 E-value: 2.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGIELTNDLKKI 100
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 101 DEVRREVGMVFQHFNLFPhLTILENCT----LAPIWVRKMPKKQAEE--IAMHYLERVKipEQANKYPGQLSGGQQQRVA 174
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVyglrLKGIKDKQVLDEAVEKslKGASIWDEVK--DRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 175 IARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
250
....*....|.
gi 489053699 255 PQHERTRLFLS 265
Cdd:PRK14239 238 PKHKETEDYIS 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
30-255 |
5.78e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 158.07 E-value: 5.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKIDEVRREVGM 109
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----DLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 190 EPTSALDPE----MVKEVLDTmvsLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK11607 175 EPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-243 |
2.53e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 154.47 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG-----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-------------EEHQKGKIVVDGI 91
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 92 ELTND---------LKKIDEVRREVGMVFQ--HFNLFPHlTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQ-AN 159
Cdd:PRK13651 83 VLEKLviqktrfkkIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 160 KYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQ 239
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....
gi 489053699 240 GQIV 243
Cdd:PRK13651 241 GKII 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-256 |
5.57e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 152.54 E-value: 5.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE-FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVG 108
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFN--LFPHlTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK13639 82 IVFQNPDdqLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
30-250 |
1.05e-43 |
|
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: 147.65 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG--EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdevRREV 107
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---RQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTL-APIwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
34-250 |
1.36e-43 |
|
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: 151.42 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 34 NMHKWYGEFHVlrDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKID--EVRREVGMVF 111
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEKRRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 112 QHFNLFPHLTILENctLAPIWVRKMPKKQ----AEEIAM----HYLERvkipeqankYPGQLSGGQQQRVAIARALCMNP 183
Cdd:TIGR02142 82 QEARLFPHLSVRGN--LRYGMKRARPSERrisfERVIELlgigHLLGR---------LPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
31-265 |
1.52e-43 |
|
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: 147.67 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 31 EITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKIDEVRREVGMV 110
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-KLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 111 FQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIamhyLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI----YELFPVLKEmLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFfdnpQHERTRLFLS 265
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
30-245 |
2.32e-43 |
|
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: 146.57 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGeRIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIEltnDLKKIDEVRREVGM 109
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD---VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILEncTLAPI-WVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 189 DEPTSALDPEMvKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:cd03264 155 DEPTAGLDPEE-RIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
45-252 |
3.45e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 148.24 E-value: 3.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQH-FNLFPHLTI- 122
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRRQVGMVFQNpDNQFVGATVq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 ------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PRK13635 101 ddvafgLEN--------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 197 PEMVKEVLDTMVSLAAEGM-TMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-244 |
4.02e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.87 E-value: 4.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndLKKIDEVRR 105
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 E-VGMVFQHFNLFPHLTILENctlapIWVRKMPK-------KQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIAR 177
Cdd:COG1129 79 AgIAIIHQELNLVPNLSVAEN-----IFLGREPRrgglidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 178 ALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVG 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-256 |
5.81e-43 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 149.79 E-value: 5.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 34 NMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGiELTNDLKKIDevrREVGMVFQH 113
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-KRMNDVPPAE---RGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 FNLFPHLTILENCT----LAPIWVRKMPKK--QAEEIAM--HYLERvkipeqankYPGQLSGGQQQRVAIARALCMNPKV 185
Cdd:PRK11000 84 YALYPHLSVAENMSfglkLAGAKKEEINQRvnQVAEVLQlaHLLDR---------KPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 186 MLFDEPTSALDP----EMVKEVLDTMVSLaaeGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK11000 155 FLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-264 |
6.11e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 147.12 E-value: 6.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 21 MQVSKT-EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG--IELTNDL 97
Cdd:PRK14246 1 MEAGKSaEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKIDEV--RREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERV----KIPEQANKYPGQLSGGQQQ 171
Cdd:PRK14246 81 FQIDAIklRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 172 RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|...
gi 489053699 252 FDNPQHERTRLFL 264
Cdd:PRK14246 240 FTSPKNELTEKYV 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
44-254 |
7.76e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 147.16 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIElTNDLKKIDEVRREVGMVFQHFNLFPHLTIL 123
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 E--------NCTLAPIWVRKmpkkQAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSAL 195
Cdd:PRK13633 104 EedvafgpeNLGIPPEEIRE----RVDES----LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 196 DPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-249 |
1.16e-42 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 146.16 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEF----HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkkidEVR 104
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-----GAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 RevGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDP---EMVKEVLDTMVSLAAEGMTMIcvTHEMGFARQVANRVIFMD--QGQIVEQNSPD 249
Cdd:COG4525 155 FLLMDEPFGALDAltrEQMQELLLDVWQRTGKGVFLI--THSVEEALFLATRLVVMSpgPGRIVERLELD 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
44-243 |
2.40e-42 |
|
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: 143.55 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKiDEVRREVGMVFQH--FNLFPHlT 121
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKA-KERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:cd03226 89 VREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489053699 202 EVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-254 |
2.74e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 145.96 E-value: 2.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG-----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVR 104
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQH--FNLFPHlTILENCTLAPIwVRKMPKKQAEEIAMHYLERVKIP--EQANKYPGQLSGGQQQRVAIARALC 180
Cdd:PRK13637 83 KKVGLVFQYpeYQLFEE-TIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 181 MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
30-266 |
2.92e-42 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 145.37 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY---------GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-NDLKK 99
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 100 idevR-REVGMVFQHFN--LFPHLTI---LEnctlAP-IWVRKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQ 171
Cdd:COG4167 85 ----RcKHIRMIFQDPNtsLNPRLNIgqiLE----EPlRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 172 RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAE 236
|
250
....*....|....*..
gi 489053699 251 FFDNPQHERT-RLFLSQ 266
Cdd:COG4167 237 VFANPQHEVTkRLIESH 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-265 |
4.64e-42 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 144.92 E-value: 4.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 22 QVSKTEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEE-----HQKGKIVVDGIELTNd 96
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 lKKID--EVRREVGMVFQHFNLFPHlTILENCTLAPiWVRKMpKKQAEEIAMHYLERVKIPEQAN---KYPGQ-LSGGQQ 170
Cdd:PRK14243 82 -PDVDpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKdklKQSGLsLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 171 QRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQVANRVIFMD---------QGQ 241
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGY 236
|
250 260
....*....|....*....|....
gi 489053699 242 IVEQNSPDEFFDNPQHERTRLFLS 265
Cdd:PRK14243 237 LVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
30-250 |
5.11e-42 |
|
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: 143.91 E-value: 5.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG-EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVG 108
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRE--VTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFpHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQ----LSGGQQQRVAIARALCMNPK 184
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMgfaRQVAN--RVIFMDQGQIVEQNSPDE 250
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL---STIVNadKIIVLKDGRIVERGTHEE 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
40-227 |
6.05e-42 |
|
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: 142.18 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFN--LF 117
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 pHLTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:TIGR01166 83 -AADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFA 227
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-250 |
6.32e-42 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 143.28 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtndLKKIDEVRREVGM 109
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTL-APIWvrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIhARLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 189 DEPTSALDP---EMVKEVLDTMVslAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:cd03265 156 DEPTIGLDPqtrAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-253 |
6.43e-42 |
|
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: 143.13 E-value: 6.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFH-VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLKKIdEVRREVG 108
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRK-SLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHlTILENCTLA-PIWVRKMPKKQAEEIAMHYLERvKIPEQANKYPGQ----LSGGQQQRVAIARALCMNP 183
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGrPNATDEEVIEAAKEAGAHDFIM-KLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-243 |
1.03e-41 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 140.64 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKKIDEVRREVGM 109
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-ASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQhfnlfphltilenctlapiwvrkmpkkqaeeiamhylervkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-243 |
1.31e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 149.02 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGEriVVA--GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlkkI--- 100
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGE--IHAllGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-----Irsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 101 -DEVRREVGMVFQHFNLFPHLTILENCTLA--PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIAR 177
Cdd:COG3845 75 rDAIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 178 ALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
45-256 |
4.30e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 143.05 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDL--KKIDEVRREVGMVFQhfnlFPHLTI 122
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPiwVRKMPK------KQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSAL 195
Cdd:PRK13641 99 FENTVLKD--VEFGPKnfgfseDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 196 DPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
44-253 |
4.31e-41 |
|
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: 141.47 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDE--VRREVGMVFQHFNLFpHLT 121
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLALADPawLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLAPiwvRKMPKKQAEEIA----MHYLERvKIPEQANKYPGQ----LSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:cd03252 92 IRDNIALAD---PGMSMERVIEAAklagAHDFIS-ELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 194 ALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
45-256 |
5.23e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 142.85 E-value: 5.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN--DLKKIDEVRREVGMVFQhfnlFPHLTI 122
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPIWVRKM----PKKQAEEIAMHYLERVKIPEQA-NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:PRK13634 99 FEETVEKDICFGPMnfgvSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 198 EMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
45-240 |
5.86e-41 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 141.06 E-value: 5.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVRREVGMVFQHFNLFPHLTILE 124
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 125 NCTLAPIWV-RKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEV 203
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 489053699 204 LDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQG 240
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
45-255 |
9.69e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 141.66 E-value: 9.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIElTNDLKKIDEVRREVGMVFQHfnlfPHLTIL- 123
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLVGIVFQN----PETQFVg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 -----------ENCTLAPIWVRKMPKKQAEEIAmhyLERVKipeqaNKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:PRK13644 93 rtveedlafgpENLCLPPIEIRKRVDRALAEIG---LEKYR-----HRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 193 SALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
49-250 |
2.15e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 139.33 E-value: 2.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 49 NLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkkIDEVRREVGMVFQHFNLFPHLTILENCTL 128
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT----TPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 129 --AP-IWVRKMPKKQAEEIAmhylERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLD 205
Cdd:PRK10771 95 glNPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489053699 206 TMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK10771 171 LVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
44-256 |
2.75e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 140.71 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL---EEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQH-FNLFPH 119
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 LTI-------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:PRK13640 100 ATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 193 SALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
41-243 |
6.56e-40 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 137.72 E-value: 6.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFp 118
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLDpaDLRRNIGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLApiwvrkMPKKQAEEIaMHYLERVKIPEQANKYP----------GQ-LSGGQQQRVAIARALCMNPKVML 187
Cdd:cd03245 91 YGTLRDNITLG------APLADDERI-LRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 188 FDEPTSALD---PEMVKEVLDTMvslaAEGMTMICVTHEMGFArQVANRVIFMDQGQIV 243
Cdd:cd03245 164 LDEPTSAMDmnsEERLKERLRQL----LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
30-223 |
6.99e-40 |
|
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: 137.23 E-value: 6.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLkkiDEVRREVGM 109
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLapiWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG4133 80 LGHADGLKPELTVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHE 223
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-252 |
8.20e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 139.48 E-value: 8.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG---EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVRRE 106
Cdd:PRK13650 5 IEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQH-FNLFPHLTI-------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:PRK13650 83 IGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGfarQVA--NRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-250 |
1.08e-39 |
|
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: 145.87 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 15 EVDRSKMQVSKTEVAIEITNMHKWYGE--FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIe 92
Cdd:TIGR03797 437 EVDEAKTDPGKLSGAIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQ- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 93 ltnDLKKID--EVRREVGMVFQHFNLFPHlTILEN-CTLAPI-----W-----------VRKMPkkqaeeIAMHYLervk 153
Cdd:TIGR03797 516 ---DLAGLDvqAVRRQLGVVLQNGRLMSG-SIFENiAGGAPLtldeaWeaarmaglaedIRAMP------MGMHTV---- 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 154 IPEQAnkypGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVldtMVSLAAEGMTMICVTHEMGFARQvANR 233
Cdd:TIGR03797 582 ISEGG----GTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV---SESLERLKVTRIVIAHRLSTIRN-ADR 653
|
250
....*....|....*..
gi 489053699 234 VIFMDQGQIVEQNSPDE 250
Cdd:TIGR03797 654 IYVLDAGRVVQQGTYDE 670
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
45-265 |
1.08e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 140.48 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-NDLKKIDEVRREVGMVFQhfNLFPHL--- 120
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkADPEAQKLLRQKIQIVFQ--NPYGSLnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 121 ----TILEnctlAPIWVR-KMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK11308 109 kkvgQILE----EPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 195 LDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLS 265
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
29-255 |
1.09e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 141.13 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWY-GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGiELTNDLKKIDevrREV 107
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-RVVNELEPAD---RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENctLApiW---VRKMPKkqaEEIAmhylERV-------KIPEQANKYPGQLSGGQQQRVAIAR 177
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN--MA--YglkIRGMPK---AEIE----ERVaeaarilELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 178 ALCMNPKVMLFDEPTSALDP----EMVKEVLDTMVSLAAegmTMICVTHEMGFARQVANRVIFMDQGQIvEQ-NSPDEFF 252
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVA-EQiGTPVEVY 223
|
...
gi 489053699 253 DNP 255
Cdd:PRK11650 224 EKP 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-245 |
1.23e-39 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 136.91 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlkKIDEVRREVGMVFQHFNLFPHLTI 122
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT----GLAPYQRPVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLA---PIWVRKMPKKQAEEIAmhylERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEM 199
Cdd:TIGR01277 88 RQNIGLGlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489053699 200 VKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:TIGR01277 164 REEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
41-241 |
1.39e-39 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 137.18 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEV------RREVGMVFQHF 114
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPReilalrRRTIGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 NLFPHLTILEnCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:COG4778 103 RVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489053699 194 ALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:COG4778 182 SLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
47-267 |
3.01e-39 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 139.46 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 47 DINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRREVGMVFQH--FNLFPHLTIL 123
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 EncTLA-PIWVRKmPKKQAEEIAmhylERVK--------IPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK15079 119 E--IIAePLRTYH-PKLSRQEVK----DRVKammlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 195 LDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLSQI 267
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
45-252 |
3.54e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 137.57 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDL--KKIDEVRREVGMVFQhfnlFPHLTI 122
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknKDIKQIRKKVGLVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPIWVRK----MPKKQAEEIAMHYLERVKIPEQA-NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:PRK13649 99 FEETVLKDVAFGPqnfgVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
44-250 |
8.39e-39 |
|
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: 143.34 E-value: 8.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKIDEV--RREVGMVFQHFNLFPHlT 121
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV----DLAIADPAwlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLAPiwvrkmPKKQAEEI--------AMHYLERVK--IPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:TIGR01846 547 IRDNIALCN------PGAPFEHVihaaklagAHDFISELPqgYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
30-245 |
1.21e-38 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 134.33 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlkkiDEVRREVGM 109
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD------IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCT-LAPIwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQL--KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
30-250 |
1.48e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.56 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG---IELTNDlkKIDE 102
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGqdvATLDAD--ALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRRE-VGMVFQHFNLFPHLTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCM 181
Cdd:PRK10535 83 LRREhFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 182 NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQIVeQNSPDE 250
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-RNPPAQ 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
41-255 |
2.14e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 136.90 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGI--------------ELTNDLKKIDEVRRE 106
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelitnPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQ--HFNLFPHlTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
30-245 |
2.28e-38 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 133.50 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkkiDEVRREVGM 109
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN----IEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILEN----CTLAPIwvrkmPKKQAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKV 185
Cdd:cd03268 77 LIEAPGFYPNLTARENlrllARLLGI-----RKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 186 MLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
41-254 |
2.82e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 135.52 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEV---RREVGMVFQ--HFN 115
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 LFPHlTILENCTLAPIWVRKmPKKQAEEIAMHYLERVKIPEQ-ANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 195 LDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
44-253 |
2.82e-38 |
|
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: 133.90 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLK--KIDEVRREVGMVFQHFNLFpHLT 121
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVRdyTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwVRKMPKKQAEEIA--MHYLERV-KIPEQANKYPGQ----LSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:cd03251 92 VAENIAYG---RPGATREEVEEAAraANAHEFImELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 195 LDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:cd03251 169 LDTESERLVQAALERL-MKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-254 |
4.74e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 134.37 E-value: 4.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-------EEHQK--GKIVVDGIELTNDL 97
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksaGSHIEllGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKideVRREVGMVFQHFNLFPHLTILENCTLA-----PIW---VRKMPKKQAEEiAMHYLERVKIPEQANKYPGQLSGGQ 169
Cdd:PRK09984 82 RK---SRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 170 QQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSL-AAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSP 248
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
....*.
gi 489053699 249 DEfFDN 254
Cdd:PRK09984 238 QQ-FDN 242
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
44-250 |
1.26e-37 |
|
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: 132.28 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLKkIDEVRREVGMVFQHFNLFPhLTIL 123
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLN-LRWLRSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLApiwvrKMPKKQAEEI-----AMHYLERVKIPEQANKYPG----QLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:cd03249 95 ENIRYG-----KPDATDEEVEeaakkANIHDFIMSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 195 LDPE---MVKEVLDTmvslAAEGMTMICVTHEMGfARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:cd03249 170 LDAEsekLVQEALDR----AMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
38-243 |
1.62e-37 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 130.75 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 38 WYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCIN--RLEEHQKGKIVVDGIELtndlkKIDEVRREVGMVFQHFN 115
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL-----DKRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 LFPHLTILEnctlapiwvrkmpkkqaeeiAMHYLERVKipeqankypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSAL 195
Cdd:cd03213 93 LHPTLTVRE--------------------TLMFAAKLR----------GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489053699 196 DPEMVKEVLDTMVSLAAEGMTMICVTH----EMgFarQVANRVIFMDQGQIV 243
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-264 |
1.72e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 132.85 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 23 VSKTEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQkGKIVVDG-IELTND----- 96
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrVEFFNQniyer 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 LKKIDEVRREVGMVFQHFNLFPhLTILENCTLAPIWVRKMPKKQAEEIAMHYLERV----KIPEQANKYPGQLSGGQQQR 172
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 173 VAIARALCMNPKVMLFDEPTSALDP--EMVKEVLDTMVSLAAEgMTMICVTHEMGFARQVANRVIFMDQ-----GQIVEQ 245
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEF 237
|
250
....*....|....*....
gi 489053699 246 NSPDEFFDNPQHERTRLFL 264
Cdd:PRK14258 238 GLTKKIFNSPHDSRTREYV 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
41-252 |
3.11e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 132.98 E-value: 3.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKK--IDEVRREVGMVFQhfnlFP 118
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLAPIWVR----KMPKKQAEEIAMHYLERVKIPEQA-NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 194 ALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-265 |
4.36e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 132.14 E-value: 4.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCINRLEE-----HQKGKIVVDGIELTNdLKKIDEVRREVGMVFQHFNLFPhLTILENcTLAPIWVRKM 136
Cdd:PRK14271 54 GPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFN-YRDVLEFRRRVGMLFQRPNPFP-MSIMDN-VLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 137 -PKKQAEEIAMHYLERV----KIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLa 211
Cdd:PRK14271 131 vPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL- 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489053699 212 AEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLS 265
Cdd:PRK14271 210 ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-242 |
4.63e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 131.72 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 32 ITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGkivvdgiELTNDLKKIDEVRREVGMVF 111
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAGTAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 112 QHFNLFPHLTILENCTLApiwVRKMPKKQAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLG---LKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-253 |
6.79e-37 |
|
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: 137.16 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 2 SAQSALQQSGIGIEVDRSKMQVSKTEVAIEITNMHKWYG--EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLE 79
Cdd:TIGR02203 303 AAESLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 80 EHQKGKIVVDGIELTnDLKkIDEVRREVGMVFQHFNLFPHlTILENCTLAPIwvRKMPKKQAEE-IAMHYLERV--KIPE 156
Cdd:TIGR02203 383 EPDSGQILLDGHDLA-DYT-LASLRRQVALVSQDVVLFND-TIANNIAYGRT--EQADRAEIERaLAAAYAQDFvdKLPL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 157 QANKYPGQ----LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGfARQVAN 232
Cdd:TIGR02203 458 GLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKAD 535
|
250 260
....*....|....*....|.
gi 489053699 233 RVIFMDQGQIVEQNSPDEFFD 253
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLA 556
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-248 |
9.08e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.40 E-value: 9.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGE-FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREV 107
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFN--LFPhLTILENCTLAPIWVRkMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKV 185
Cdd:PRK13647 82 GLVFQDPDdqVFS-STVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 186 MLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSP 248
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
44-268 |
1.01e-36 |
|
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: 131.08 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRREVGMVFQH----FNlfP 118
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQDspsaVN--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTI-------LENCTlapiwvrKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:TIGR02769 104 RMTVrqiigepLRHLT-------SLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNpQHERTRLFLSQIL 268
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVL 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
34-268 |
1.32e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 130.43 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 34 NMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIE-LTNDLKKIDEVRR------E 106
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALSEAERrrllrtE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHF--NLFPHLTILENctlapIWVRKMPKKQ-----AEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARA 178
Cdd:PRK11701 91 WGFVHQHPrdGLRMQVSAGGN-----IGERLMAVGArhygdIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQH 257
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
250
....*....|.
gi 489053699 258 ERTRLFLSQIL 268
Cdd:PRK11701 246 PYTQLLVSSVL 256
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
43-250 |
1.35e-36 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 137.30 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFpHL 120
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGV----DIRQIDpaDLRRNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 121 TILENCTLApiwvrkMPKKQAEEIaMHYLERVKIPEQANKYP----------GQ-LSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:TIGR03375 554 TLRDNIALG------APYADDEEI-LRAAELAGVTEFVRRHPdgldmqigerGRsLSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR03375 627 EPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPKDQ 685
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-265 |
2.18e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 131.00 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGEriVVA--GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlkkiDEVRR- 105
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGE--IFGllGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------PEDRRr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 ------EVGmvfqhfnLFPHLTILENCT-LAPIwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:COG4152 73 igylpeERG-------LYPKMKVGEQLVyLARL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDnpQHE 258
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QFG 221
|
....*..
gi 489053699 259 RTRLFLS 265
Cdd:COG4152 222 RNTLRLE 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-250 |
3.22e-36 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 129.05 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRlEEHQ--KGKIVVDGIEL--TNdlkkIDE 102
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPtyGNDVRLFGERRggED----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRREVGMV--FQHFNLFPHLTILE------NCTLApIWVRkmPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVA 174
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLDvvlsgfFDSIG-LYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 175 IARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEG-MTMICVTH---EM--GFarqvaNRVIFMDQGQIVEQNSP 248
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGPK 227
|
..
gi 489053699 249 DE 250
Cdd:COG1119 228 EE 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-269 |
4.21e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.97 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE-FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVG 108
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQH--FNLFPhLTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERT-RLFL 264
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKvNLRL 243
|
....*
gi 489053699 265 SQILH 269
Cdd:PRK13636 244 PRIGH 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-250 |
4.66e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.08 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT----NDLKKidevRR 105
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspWELAR----RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVgmVFQHFNL-FPhLTILEnctlapiwVRKM-------PKKQAEEIAMHYLERVKIPEQANK-YPgQLSGGQQQRVAIA 176
Cdd:COG4559 78 AV--LPQHSSLaFP-FTVEE--------VVALgraphgsSAAQDRQIVREALALVGLAHLAGRsYQ-TLSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 177 RALC-------MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPD 249
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225
|
.
gi 489053699 250 E 250
Cdd:COG4559 226 E 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-249 |
6.61e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 128.66 E-value: 6.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVRREVG 108
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-------KPVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 189 DEPTSALDP---EMVKEVLDTMvsLAAEGMTMICVTHEMGFARQVANRVIFM--DQGQIVEQNSPD 249
Cdd:PRK11248 153 DEPFGALDAftrEQMQTLLLKL--WQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVERLPLN 216
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
30-268 |
7.10e-36 |
|
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: 128.41 E-value: 7.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQKGKIVVDGIELTNDLKKIDEVRR--- 105
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLaGRLAPDHGTATYIMRSGAELELYQLSEAERrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 ---EVGMVFQH------FNLFPHLTILENctLAPIWVRKMPKKQAEeiAMHYLERVKIPE-QANKYPGQLSGGQQQRVAI 175
Cdd:TIGR02323 84 mrtEWGFVHQNprdglrMRVSAGANIGER--LMAIGARHYGNIRAT--AQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 176 ARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
250
....*....|....
gi 489053699 255 PQHERTRLFLSQIL 268
Cdd:TIGR02323 240 PQHPYTQLLVSSIL 253
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
41-267 |
9.17e-36 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 134.60 E-value: 9.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG--IELTNDlKKIDEVRREVGMVFQ--HFNL 116
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSP-GKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 FPHLTILENcTLAPIWVRKM-PKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK10261 415 DPRQTVGDS-IMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 195 LDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLSQI 267
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
30-255 |
1.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 128.38 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNM-HKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVG 108
Cdd:PRK13652 4 IETRDLcYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK--ENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFN--LFPHlTILENCTLAPIWVrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK13652 82 LVFQNPDdqIFSP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-245 |
1.93e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.43 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGE----FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKID 101
Cdd:PRK10584 3 AENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG----QPLHQMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 EVRR------EVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAI 175
Cdd:PRK10584 79 EEARaklrakHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 176 ARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDqGQIVEQ 245
Cdd:PRK10584 158 ARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-250 |
3.13e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 28 VAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQkGKIVVDGIELTnDLKKIDEVRRe 106
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPDS-GEVRLNGRPLA-DWSPAELARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNL-FPhLTILEnctlapiwVRKM-------PKKQAEEIAMHYLERVKIPEQANK-YPgQLSGGQQQRVAIAR 177
Cdd:PRK13548 78 RAVLPQHSSLsFP-FTVEE--------VVAMgraphglSRAEDDALVAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 178 ALC------MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
44-242 |
1.86e-34 |
|
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: 122.32 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFPHlT 121
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDpnELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCtlapiwvrkmpkkqaeeiamhylervkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:cd03246 92 IAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489053699 202 EVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQI 242
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
45-235 |
2.00e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 123.36 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCIN-RLEEH--QKGKIVVDGIELTndlkKIDEVRREVGMVFQHFNLFPHLT 121
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLT----ALPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLA-PiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMV 200
Cdd:COG4136 93 VGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 489053699 201 KEVLDTMVS-LAAEGMTMICVTHEMGfARQVANRVI 235
Cdd:COG4136 170 AQFREFVFEqIRQRGIPALLVTHDEE-DAPAAGRVL 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-245 |
2.34e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.77 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 33 TNMHKWYGE----FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT--NDLKKIDEVRRE 106
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSL-AAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQ 245
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
45-252 |
3.60e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.85 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN--DLKKIDEVRREVGMVFQhfnlFPHLTI 122
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQ----FPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPIWVRK----MPKKQAEEIAMHYLERVKIPEQA-NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:PRK13643 98 FEETVLKDVAFGPqnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-253 |
8.99e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 124.94 E-value: 8.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 24 SKTEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlKKIDEV 103
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP---ARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 104 RREVGMVFQHFNLFPHLTILENCTLAPIWVRkMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
37-243 |
1.40e-33 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 121.61 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 37 KWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQ--KGKIVVDGIELtndlkKIDEVRREVGMVFQH 113
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPR-----KPDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 FNLFPHLTILENCTLAPIWV--RKMPKKQAEEIAMHYLER-VKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRlpRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMG---FarQVANRVIFMDQGQIV 243
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-265 |
3.03e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 126.74 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 21 MQVSKTEVAIEITN--MHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQkGKIVVDGIELTN-DL 97
Cdd:PRK15134 276 LDVEQLQVAFPIRKgiLKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKIDEVRREVGMVFQHFN--LFPHLTILEncTLAP---IWVRKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQ 171
Cdd:PRK15134 355 RQLLPVRHRIQVVFQDPNssLNPRLNVLQ--IIEEglrVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 172 RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
250
....*....|....*
gi 489053699 251 FFDNPQHERTRLFLS 265
Cdd:PRK15134 513 VFAAPQQEYTRQLLA 527
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
30-243 |
3.21e-33 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 120.55 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtndLKKIDEVRR 105
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFPHLTILENCT-------LApiwvRKMPKKQAEEIAmhylERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEyfaglygLK----GDELTARLEELA----DRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 179 LCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-244 |
6.89e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.95 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDEVRREVGMVFQH----FNlfP 118
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDsisaVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:PRK10419 105 RKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489053699 198 EMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
30-262 |
1.24e-32 |
|
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: 119.18 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEvRREVGM 109
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--LPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VF--QHFNLFPHLTILENcTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:cd03218 78 GYlpQEASIFRKLTVEEN-ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRL 262
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-244 |
1.76e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.41 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVdGIELtndlkkidevrrEVGM 109
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHF-NLFPHLTILEnctlapiWVRKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:COG0488 383 FDQHQeELDPDKTVLD-------ELRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 188 FDEPTSALDPEMvKEVLDTMvsLAA-EGmTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:COG0488 456 LDEPTNHLDIET-LEALEEA--LDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-243 |
2.62e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.42 E-value: 2.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG-----EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKkidEVR 104
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LP---EYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 RE--VGMVFQHFNL--FPHLTILENCTLA-------------PIWVRKMPKKQAEEIAMHyLE-RVKIPEqankypGQLS 166
Cdd:COG1101 78 RAkyIGRVFQDPMMgtAPSMTIEENLALAyrrgkrrglrrglTKKRRELFRELLATLGLG-LEnRLDTKV------GLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 167 GGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
44-248 |
4.16e-32 |
|
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: 117.59 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFPHlT 121
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV----DISKIGlhDLRSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENctLAPIwvrkmpKKQAEEIAMHYLERVKIPEQANKYPGQL-----------SGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:cd03244 94 IRSN--LDPF------GEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 191 PTSALDPE---MVKEVLDTMVSlaaeGMTMICVTHE----MGFarqvaNRVIFMDQGQIVEQNSP 248
Cdd:cd03244 166 ATASVDPEtdaLIQKTIREAFK----DCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
44-264 |
6.70e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.89 E-value: 6.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGIELTN-DLKKIDEVR-REVGMVFQH--F 114
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHaSEQTLRGVRgNKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 NLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANK---YPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFL 264
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
40-267 |
1.45e-31 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 122.66 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRR------------EV 107
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgaDM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQH--FNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQA---NKYPGQLSGGQQQRVAIARALCMN 182
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTR 261
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
....*.
gi 489053699 262 LFLSQI 267
Cdd:PRK10261 267 ALLAAV 272
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-237 |
5.62e-31 |
|
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: 120.47 E-value: 5.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNM-HKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKiDEVRREV 107
Cdd:TIGR02857 321 SLEFSGVsVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA-DADA-DSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHlTILENCTLA-PIWVRKMPKKQAEEIAMHYLERVkIPEQANKYPGQ----LSGGQQQRVAIARALCMN 182
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLArPDASDAEIREALERAGLDEFVAA-LPQGLDTPIGEggagLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVTHEMGFARqVANRVIFM 237
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
48-255 |
1.04e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 115.09 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKKIDEVRREVGMVFQHFNLFPHLTILENCT 127
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIARMGVVRTFQHVRLFREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 128 LA----------------PIWVRKmpKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:PRK11300 103 VAqhqqlktglfsgllktPAFRRA--ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
42-264 |
1.09e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 116.38 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 42 FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHqKGKIVVDGIELTN-DLKKIDEVRR------EVGMVFQH- 113
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGqDLQRISEKERrnlvgaEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 -FNLFPHLT----ILENCTLAPIWVRKMPKKQAEEIamhyLERVKIPEQANK---YPGQLSGGQQQRVAIARALCMNPKV 185
Cdd:PRK11022 99 mTSLNPCYTvgfqIMEAIKVHQGGNKKTRRQRAIDL----LNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 186 MLFDEPTSALDPEMVKEVLDTMVSLA-AEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFL 264
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
38-222 |
1.28e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 119.39 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 38 WYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQHFNLF 117
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 pHLTILENCTLApiwvrkmpKKQA-EEIAMHYLERVKIPEQANKYPG-----------QLSGGQQQRVAIARALCMNPKV 185
Cdd:TIGR02868 422 -DTTVRENLRLA--------RPDAtDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 489053699 186 MLFDEPTSALDPEMVKEVLDTMVSlAAEGMTMICVTH 222
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
45-256 |
2.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKidEVRREVGMVFQH-FNLFPHLTI- 122
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE--KLRKHIGIVFQNpDNQFVGSIVk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 ------LENctlapiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PRK13648 103 ydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 197 PEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-243 |
2.61e-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: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWygefHVLRDINLKVMRGErIV-VAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndLKKIDEVRR 105
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EvGMVF-----QHFNLFPHLTILENCTLAPI----WVRKMPKKQAEEIAMHYLERVKI----PEQAnkyPGQLSGGQQQR 172
Cdd:COG1129 327 A-GIAYvpedrKGEGLVLDLSIRENITLASLdrlsRGGLLDRRRERALAEEYIKRLRIktpsPEQP---VGNLSGGNQQK 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 173 VAIARALCMNPKVMLFDEPTSALDpemV---KEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:COG1129 403 VVLAKWLATDPKVLILDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
44-255 |
3.64e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 118.67 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKIDEV--RREVGMVFQHFNLFPHlT 121
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwVRKMPKKQAEEIAMHYLERVKIPEQANKYP-------GQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:TIGR00958 571 VRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 195 LDPEMVKEVLDTMvslAAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:TIGR00958 648 LDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
45-250 |
4.96e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 118.14 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKI--DEVRREVGMVFQHFNLFpHLTI 122
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVtrASLRRNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENctlapIWVRKmPKKQAEEI--------AMHYLERvkipeQANKYP-------GQLSGGQQQRVAIARALCMNPKVML 187
Cdd:PRK13657 426 EDN-----IRVGR-PDATDEEMraaaeraqAHDFIER-----KPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 188 FDEPTSALDPEM---VKEVLDTMVslaaEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK13657 495 LDEATSALDVETeakVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-250 |
5.65e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 117.62 E-value: 5.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 22 QVSKTEVAIEITNMHKWY--GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKK 99
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ----PIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 100 IDE--VRREVGMVFQHFNLFPHlTILENCTLApiwvrkmpKKQA-EEIAMHYLERVKIPEQANKYPG----------QLS 166
Cdd:PRK11160 407 YSEaaLRQAISVVSQRVHLFSA-TLRDNLLLA--------APNAsDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 167 GGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAeGMTMICVTHemgfaRQVA----NRVIFMDQGQI 242
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH-----RLTGleqfDRICVMDNGQI 551
|
....*...
gi 489053699 243 VEQNSPDE 250
Cdd:PRK11160 552 IEQGTHQE 559
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
30-250 |
6.52e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 112.48 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGM 109
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT--TPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQ--HFNL------------FPH----LTilenctlapiwvrkmpkKQAEEI---AMHYLErvkIPEQANKYPGQLSGG 168
Cdd:COG4604 80 LRQenHINSrltvrelvafgrFPYskgrLT-----------------AEDREIideAIAYLD---LEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 169 QQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNS 247
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
...
gi 489053699 248 PDE 250
Cdd:COG4604 220 PEE 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
26-253 |
7.99e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndlKKIDEVRR 105
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFPHLTILENCTlapIWVR--KMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLL---VFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
30-267 |
8.12e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.94 E-value: 8.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIEL-TNDLKKIDEVRREVG 108
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 189 DEPTSALDPemvkEVLDTMVSLAAE-----GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHeRTRLF 263
Cdd:PRK11831 168 DEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQF 242
|
....
gi 489053699 264 LSQI 267
Cdd:PRK11831 243 LDGI 246
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
30-245 |
9.03e-30 |
|
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: 110.10 E-value: 9.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE--FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlkKIDEVRREV 107
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD---LEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFpHLTILENCTLapiwvrkmpkkqaeeiamhylervkipeqankypgQLSGGQQQRVAIARALCMNPKVML 187
Cdd:cd03247 78 SVLNQRPYLF-DTTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSlAAEGMTMICVTHEM-GFARqvANRVIFMDQGQIVEQ 245
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLtGIEH--MDKILFLENGKIIMQ 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-250 |
1.22e-29 |
|
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: 116.44 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWY-----GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVV----DGIELTNdlKKI 100
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK--PGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 101 DE---VRREVGMVFQHFNLFPHLTILENCTLApIWVrKMPKKQAEEIAMHYLERVKIPEQA-----NKYPGQLSGGQQQR 172
Cdd:TIGR03269 358 DGrgrAKRYIGILHQEYDLYPHRTVLDNLTEA-IGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 173 VAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-256 |
2.66e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.89 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGEriVVA--GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDE-VRRE 106
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGE--IVGllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENcTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTmICVT----HEMgfaRQVANRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRET---LGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-250 |
2.92e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.26 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEvrREVGm 109
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD----KPISMLSS--RQLA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 vfQHFNLFP-HLTILENCTLA-----------PIWVRKMPKKQAE-EIAMhylERVKIPEQANKYPGQLSGGQQQRVAIA 176
Cdd:PRK11231 76 --RRLALLPqHHLTPEGITVRelvaygrspwlSLWGRLSAEDNARvNQAM---EQTRINHLADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 177 RALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-243 |
2.93e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.35 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 38 WYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKK--IDEVRREVGMVFQHFN 115
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR-LKNreVPFLRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 LFPHLTILENCTLaPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSAL 195
Cdd:PRK10908 90 LLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489053699 196 DPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-242 |
4.23e-29 |
|
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: 108.67 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWygefHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndLKKIDEVRRE 106
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT--RRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 vGMVF-----QHFNLFPHLTILENCTLapiwvrkmpkkqaeeiamhylervkipeqankyPGQLSGGQQQRVAIARALCM 181
Cdd:cd03215 76 -GIAYvpedrKREGLVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLAR 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 182 NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
44-250 |
7.75e-29 |
|
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: 114.53 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKI--DEVRREVGMVFQHFNLFpHLT 121
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ----DIRDVtqASLRAAIGIVPQDTVLF-NDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILEN-------CTLAPIW-----------VRKMPKKQAEEIAmhylER-VKipeqankypgqLSGGQQQRVAIARALCMN 182
Cdd:COG5265 448 IAYNiaygrpdASEEEVEaaaraaqihdfIESLPDGYDTRVG----ERgLK-----------LSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSlAAEGMTMICVTHemgfaR----QVANRVIFMDQGQIVEQNSPDE 250
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALRE-VARGRTTLVIAH-----RlstiVDADEILVLEAGRIVERGTHAE 578
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
30-250 |
2.14e-28 |
|
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: 107.87 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-NDLKKIdevrrevG 108
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKI-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFNLFPHLTILEN----CTLapiwvRKMPKKQAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:TIGR03740 74 SLIESPPLYENLTARENlkvhTTL-----LGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
34-262 |
2.24e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.44 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 34 NMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLKKIDEVRREVGMVFQH 113
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 FNLFPHLTILENcTLAPIWVRK-MPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:PRK10895 87 ASIFRRLSVYDN-LMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 193 SALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRL 262
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-242 |
5.81e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 32 ITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDgieltNDLKkidevrreVGMVF 111
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGLR--------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 112 QHFNLFPHLTILENCT--LAPIW---------VRKMPKKQAEEIAMHYLE-------------RVKI--------PEQAN 159
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgDAELRaleaeleelEAKLAEPDEDLERLAELQeefealggweaeaRAEEilsglgfpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 160 KYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkEVLDTMvsLAAEGMTMICVTHEMGFARQVANRVIFMDQ 239
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLEEF--LKNYPGTVLVVSHDRYFLDRVATRILELDR 224
|
...
gi 489053699 240 GQI 242
Cdd:COG0488 225 GKL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-250 |
6.00e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.47 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWY----------------------GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKI 86
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 87 VVDGieltndlkkidevrR-----EVGMVFQhfnlfPHLTILENCTL-APIW--VRKMPKKQAEEIAM-----HYLER-V 152
Cdd:COG1134 84 EVNG--------------RvsallELGAGFH-----PELTGRENIYLnGRLLglSRKEIDEKFDEIVEfaelgDFIDQpV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 153 KipeqankypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVAN 232
Cdd:COG1134 145 K----------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|....*...
gi 489053699 233 RVIFMDQGQIVEQNSPDE 250
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEE 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
39-228 |
1.61e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.62 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlkkidevRREVGMVFQHFNL-- 116
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-------------GARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 -FPhLTILENCTLApIWVRKMP----KKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEP 191
Cdd:NF040873 69 sLP-LTVRDLVAMG-RWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 489053699 192 TSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFAR 228
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
44-253 |
3.84e-27 |
|
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: 110.21 E-value: 3.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFPHlT 121
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF----SLKDIDrhTLRQFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwvrKMPKKQAEEIaMHYLERVKIPEQANKYP-----------GQLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:TIGR01193 564 ILENLLLG-----AKENVSQDEI-WAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAEgmTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDEFFD 253
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLD 697
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
46-265 |
4.72e-27 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 105.17 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 46 RDINLKVMRGERIVVAGPSGSGKStmIRCINRLE------EHQKGKIVVDGIELT-NDLKKidevrREVGMVFQH----F 114
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVApCALRG-----RKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 NlfPHLTI----LENCtlapiwvRKMPKKQAEEIAMHYLERVKIPEQA---NKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:PRK10418 93 N--PLHTMhthaRETC-------LALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRLFLS 265
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
47-257 |
5.35e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.73 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 47 DINLKVMRGERIVVAGPSGSGKSTMIRCINRL---EEHQKGKIVVDGIELTN-DLKKIDEVRRE-VGMVFQH--FNLFPH 119
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNlPEKELNKLRAEqISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 LTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPE---QANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PRK09473 114 MRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 197 PEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQH 257
Cdd:PRK09473 194 VTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSH 255
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
43-254 |
8.59e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 108.98 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQK--GKIVVDGIELTNDlkkidEVRREVGMVFQHFNLFPH 119
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKgsGSVLLNGMPIDAK-----EMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 LTILENCTLA-----PiwvRKMPKKQAEEIAMHYLERVKIPEQANKYPGQ------LSGGQQQRVAIARALCMNPKVMLF 188
Cdd:TIGR00955 114 LTVREHLMFQahlrmP---RRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTH-------EMgFarqvaNRVIFMDQGQIVEQNSPDE---FFDN 254
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPDQavpFFSD 260
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
62-243 |
9.48e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.50 E-value: 9.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKID---EVRReVGMVFQHFNLFPHLTILENCTLApiWVRKMPK 138
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppEKRR-IGYVFQDARLFPHYKVRGNLRYG--MAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 139 KQAEEIAM----HYLERvkipeqankYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE- 213
Cdd:PRK11144 108 QFDKIVALlgiePLLDR---------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREi 178
|
170 180 190
....*....|....*....|....*....|
gi 489053699 214 GMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
39-250 |
1.66e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.91 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKidEVRREVGMVFQHFNLFP 118
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK--EVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLA-----PIWVRKmpKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:PRK10253 95 DITVQELVARGryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 194 ALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-254 |
1.74e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.42 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 28 VAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKKIDEVRREV 107
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTLAPIWVRKmpKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVML 187
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAER--DQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-250 |
4.21e-26 |
|
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: 106.43 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ--KGKIV-------------------- 87
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 88 -------------VDGIELTNDLKKidEVRREVGMVFQH-FNLFPHLTILENcTLAPIWVRKMPKKQAEEIAMHYLERVK 153
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRR--RIRKRIAIMLQRtFALYGDDTVLDN-VLEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 154 IPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLA-AEGMTMICVTHEMGFARQVAN 232
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*...
gi 489053699 233 RVIFMDQGQIVEQNSPDE 250
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDE 255
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
45-252 |
5.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVRREVGMVFQH-FNLFPHLTIL 123
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLApIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEV 203
Cdd:PRK13642 101 DDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489053699 204 LDTMVSLAAE-GMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
44-252 |
1.10e-25 |
|
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: 105.60 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DlkkIDEVRREVGMVFQHFNLFPHlTI 122
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwD---REELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENctlapiwVRKMPKKQAEEI-------AMHYLervkIPEQANKY-------PGQLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:COG4618 423 AEN-------IARFGDADPEKVvaaaklaGVHEM----ILRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 189 DEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
48-250 |
1.10e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 105.70 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQkGKIVVDGIELTN-DLKkidEVRREVGMVFQHFNLFpHLTILENC 126
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRElDPE---SWRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 127 TLApiwvrkmpKKQA-EEIAMHYLERVKIPEQANKYP-----------GQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK11174 444 LLG--------NPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 195 LDPEMVKEVLDTMVSlAAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDE 250
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-261 |
2.75e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 101.02 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHK-------WYGEFHV--LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDL 97
Cdd:PRK15112 2 ETLLEVRNLSKtfryrtgWFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKIDEVRreVGMVFQ--HFNLFPHLTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKI-PEQANKYPGQLSGGQQQRVA 174
Cdd:PRK15112 82 YSYRSQR--IRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 175 IARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSL-AAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
....*...
gi 489053699 254 NPQHERTR 261
Cdd:PRK15112 240 SPLHELTK 247
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
30-241 |
3.76e-25 |
|
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: 97.13 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDgieltndlkkidevrrevgm 109
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 vfqhfnlfPHLTILenctlapiwvrkmpkkqaeeiamhYLErvkipeqankypgQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:cd03221 61 --------STVKIG------------------------YFE-------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLaaEGmTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY--PG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
39-244 |
1.10e-24 |
|
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: 97.99 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG-----IELtndlkkidevrrevGMVFQh 113
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGL--------------GGGFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 fnlfPHLTILEN----CTLAPIWVRKMPKKQAE-----EIAMHYLERVKipeqankypgQLSGGQQQRVAIARALCMNPK 184
Cdd:cd03220 97 ----PELTGRENiylnGRLLGLSRKEIDEKIDEiiefsELGDFIDLPVK----------TYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-243 |
2.87e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtNDLKKIDEVRREVGM 109
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLAPIWVRK------MPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
44-242 |
4.05e-24 |
|
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: 96.77 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndLKKIDEVRREVGMVFQHFNLFPHlTIL 123
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS--QYEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLApiwVRKMPKKQAEEIAMHYLERVKIPEQANKYP-------GQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:cd03248 106 DNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489053699 197 PEMvKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQI 242
Cdd:cd03248 183 AES-EQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
15-247 |
1.18e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 99.71 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 15 EVDRSKMQVSKTEVAIEITNMHKWY--GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIE 92
Cdd:PRK11176 327 EKDEGKRVIERAKGDIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 93 LTNdlKKIDEVRREVGMVFQHFNLFpHLTILENCTLAP--IWVRKMPKKQAEEI-AMHYLErvKIPEQANKYPGQ----L 165
Cdd:PRK11176 407 LRD--YTLASLRNQVALVSQNVHLF-NDTIANNIAYARteQYSREQIEEAARMAyAMDFIN--KMDNGLDTVIGEngvlL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 166 SGGQQQRVAIARALCMNPKVMLFDEPTSALDPE---MVKEVLDTMvslaAEGMTMICVTHEMGFARQvANRVIFMDQGQI 242
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTEserAIQAALDEL----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
....*
gi 489053699 243 VEQNS 247
Cdd:PRK11176 557 VERGT 561
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
44-248 |
2.72e-23 |
|
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: 94.02 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltnDLKKID--EVRREVGMVFQHFNLFPHlT 121
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPleDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENctLAPiwvrkMPKKQAEEIamhyLERVKIPEQANkypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:cd03369 98 IRSN--LDP-----FDEYSDEEI----YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489053699 202 EVLDTMVSLAAeGMTMICVTHEMgfaRQVA--NRVIFMDQGQIVEQNSP 248
Cdd:cd03369 163 LIQKTIREEFT-NSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-250 |
3.96e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKidEVRREVGM 109
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR--AASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQH----FNL----------FPHLTILENCTLApiwvrkmpKKQAEEIAMhylERVKIPEQANKYPGQLSGGQQQRVAI 175
Cdd:PRK09536 82 VPQDtslsFEFdvrqvvemgrTPHRSRFDTWTET--------DRAAVERAM---ERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 176 ARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
40-242 |
6.26e-23 |
|
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: 97.42 E-value: 6.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN-DLKKIDevrREVGMVFQHFNLFP 118
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFG---KHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HlTILENCTlapiwvRKMPKKQAEEI-------AMHYLeRVKIPEQANKYPGQ----LSGGQQQRVAIARALCMNPKVML 187
Cdd:TIGR01842 406 G-TVAENIA------RFGENADPEKIieaaklaGVHEL-ILRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 188 FDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQI 242
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
30-249 |
6.81e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.59 E-value: 6.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGIELTNdlKKIDE-VRRE 106
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITD--LPPEErARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTIlenctlapiwvrkmpkkqaeeiaMHYLERVkipeqaNKypgQLSGGQQQRVAIARALCMNPKVM 186
Cdd:cd03217 79 IFLAFQYPPEIPGVKN-----------------------ADFLRYV------NE---GFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTH-EMGFARQVANRVIFMDQGQIVEQNSPD 249
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
44-241 |
9.36e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 92.53 E-value: 9.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCInrLEE--HQKGKIVVDGIE--------LTND--------LKKIDEVR- 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEleKLSGSVSVPGSIayvsqepwIQNGtirenilfGKPFDEERy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVgmvfqhfnlfphltiLENCTLAPIwVRKMPKKQAEEIAmhylERvkipeqankypG-QLSGGQQQRVAIARALCMNP 183
Cdd:cd03250 98 EKV---------------IKACALEPD-LEILPDGDLTEIG----EK-----------GiNLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMV-SLAAEGMTMICVTHEMGFARQvANRVIFMDQGQ 241
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
55-237 |
4.98e-22 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 95.33 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 55 GERIVVAGPSGSGKSTMIRCI-NRLEEHQ-KGKIvvdgieLTNDLKKIDEVRREVGMVFQHFNLFPHLTILEncTLAPIW 132
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTI------LANNRKPTKQILKRTGFVTQDDILYPHLTVRE--TLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 133 VRKMPKKQAEEIAMHYLERVkIPEQA----------NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESV-ISELGltkcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190
....*....|....*....|....*....|....*
gi 489053699 203 VLDTMVSLAAEGMTMICVTHemgfarQVANRVIFM 237
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMH------QPSSRVYQM 273
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
44-222 |
6.06e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVV-DGIELtndlkkidevrrevgmvfqhfnLF----P 118
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILencTLA-----PIWVRKMPKKQAEEIamhyLERVKIP-------EQANkYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:COG4178 436 YLPLG---TLReallyPATAEAFSDAELREA----LEAVGLGhlaerldEEAD-WDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*.
gi 489053699 187 LFDEPTSALDPEMVKEVLdTMVSLAAEGMTMICVTH 222
Cdd:COG4178 508 FLDEATSALDEENEAALY-QLLREELPGTTVISVGH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-244 |
1.67e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWygEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-----NDLKK- 99
Cdd:PRK09700 262 HETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 100 ---IDEVRREVGmvfqhfnLFPHLTILENCTLAP------------IWVRKMPKKQAEEiamhylERVKIP---EQANKY 161
Cdd:PRK09700 340 mayITESRRDNG-------FFPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAEN------QRELLAlkcHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 162 PGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
...
gi 489053699 242 IVE 244
Cdd:PRK09700 487 LTQ 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
41-222 |
2.03e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 89.25 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDgieltndlkkidevrrevgmvfqhfnlFPHL 120
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------------VPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 121 TILENCTLAPIWVRKMPKKQAEEIamhyLERVKIPEQAN--KYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPE 198
Cdd:COG2401 95 QFGREASLIDAIGRKGDFKDAVEL----LNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*
gi 489053699 199 MVKEVLDTMVSLAAE-GMTMICVTH 222
Cdd:COG2401 171 TAKRVARNLQKLARRaGITLVVATH 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
48-248 |
3.16e-21 |
|
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: 93.15 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLkkiDEVRREVGMVFQHFNLFPHLTILENCT 127
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL---DAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 128 L-APIWVRKMPKKQAEEIAMhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDT 206
Cdd:TIGR01257 1026 FyAQLKGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489053699 207 MVSLAAeGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSP 248
Cdd:TIGR01257 1104 LLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
44-222 |
1.32e-20 |
|
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: 85.67 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlkkidevRREVGMVFQHfnlfPHLTIL 123
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-------------GEDLLFLPQR----PYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 encTLApiwvrkmpkkqaEEIAmhylervkipeqankYPGQ--LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:cd03223 79 ---TLR------------EQLI---------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 489053699 202 EVLDTmvsLAAEGMTMICVTH 222
Cdd:cd03223 129 RLYQL---LKELGITVISVGH 146
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
44-223 |
1.64e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQHFNLFPHlTIL 123
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST--LKPEIYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLaPIWVRKmpkKQAEEIAM-HYLERVKIPEQA-NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVK 201
Cdd:PRK10247 99 DNLIF-PWQIRN---QQPDPAIFlDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|...
gi 489053699 202 EVLDTMVSLAAE-GMTMICVTHE 223
Cdd:PRK10247 175 NVNEIIHRYVREqNIAVLWVTHD 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-254 |
1.11e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 21 MQVSKTEVA--IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdLK 98
Cdd:PRK15439 1 MQTSDTTAPplLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-LT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 99 KIDEVRREVGMVFQHFNLFPHLTILENctlapIWVRkMPKKQAEEIAMHYLER-----VKIPEQAnkypGQLSGGQQQRV 173
Cdd:PRK15439 80 PAKAHQLGIYLVPQEPLLFPNLSVKEN-----ILFG-LPKRQASMQKMKQLLAalgcqLDLDSSA----GSLEVADRQIV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 174 AIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFD 253
Cdd:PRK15439 150 EILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
.
gi 489053699 254 N 254
Cdd:PRK15439 230 D 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
40-222 |
5.21e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVRREVGmvfqHFN-LFP 118
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--DVAEACHYLG----HRNaMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLapiWVRKmpKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPE 198
Cdd:PRK13539 87 ALTVAENLEF---WAAF--LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....
gi 489053699 199 MVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAATH 185
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
31-244 |
8.45e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.81 E-value: 8.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 31 EITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGIELTNdlKKIDE-VRREV 107
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILE--LSPDErARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQH---------FNLFphLTILENCTLAPIWVRKMpKKQAEEiamhYLERVKIPEQ-ANKY--PGqLSGGQQQRVAI 175
Cdd:COG0396 80 FLAFQYpveipgvsvSNFL--RTALNARRGEELSAREF-LKLLKE----KMKELGLDEDfLDRYvnEG-FSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 176 ARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHemgFAR----QVANRVIFMDQGQIVE 244
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
39-252 |
1.28e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHfnlfP 118
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLAPIW--VRKMPKKQAEeIAMHYLERVKI--PEQANKYPGQ-LSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:PRK13638 87 EQQIFYTDIDSDIAfsLRNLGVPEAE-ITRRVDEALTLvdAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 194 ALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFF 252
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
30-244 |
2.04e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.25 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGE--FHVlRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTndLKKIDEVRREV 107
Cdd:PRK10522 323 LELRNVTFAYQDngFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--AEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENctlapiwvrkmpKKQAEEIAMHYLERVKIPEQANKYPG-----QLSGGQQQRVAIARALCMN 182
Cdd:PRK10522 400 SAVFTDFHLFDQLLGPEG------------KPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 183 PKVMLFDEPTSALDPEMVKEV-LDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQIVE 244
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-243 |
2.30e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.11 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGIELTNDLKKiDEVRREV 107
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASNIR-DTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEI---AMHYLERVKIPEQANKYP-GQLSGGQQQRVAIARALCMNP 183
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
30-261 |
2.81e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 82.65 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHkwyGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEhqKGKIVVD-----GIELTN----DLKK 99
Cdd:COG4170 11 IEIDTPQ---GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKD--NWHVTADrfrwnGIDLLKlsprERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 100 IdeVRREVGMVFQHFN--LFPHLTILE-------NCTL-APIWVRKMPKKQaeeIAMHYLERVKIPEQA---NKYPGQLS 166
Cdd:COG4170 86 I--IGREIAMIFQEPSscLDPSAKIGDqlieaipSWTFkGKWWQRFKWRKK---RAIELLHRVGIKDHKdimNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 167 GGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAA-EGMTMICVTHEMGFARQVANRVIFMDQGQIVEQ 245
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250
....*....|....*.
gi 489053699 246 NSPDEFFDNPQHERTR 261
Cdd:COG4170 241 GPTEQILKSPHHPYTK 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-242 |
3.55e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.72 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWY-GEFHVLR--DINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ-KGKIVVDG--IELTNDLKKI 100
Cdd:TIGR02633 255 DVILEARNLTCWDvINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQAI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 101 D-------EVRREVGMVfqhfnlfPHLTILENCTLAPI--WVRKMPKKQAEE--IAMHYLERVKIPEQANKYP-GQLSGG 168
Cdd:TIGR02633 335 RagiamvpEDRKRHGIV-------PILGVGKNITLSVLksFCFKMRIDAAAElqIIGSAIQRLKVKTASPFLPiGRLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 169 QQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-222 |
4.45e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGIELTndLKKI-DEVRRE 106
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQ--ASNIrDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHLTILENCTLAPIWVR-------KMPKKqAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARAL 179
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPggimdydAMYLR-AQKL----LAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489053699 180 CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-242 |
5.01e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIE---------LTNDLKKIDEVRREVGMVFQhfn 115
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtrspqdgLANGIVYISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 lfphLTILENCTLAPIwvRKMPKK------QAEEIAM-HYLE--RVKIPEQaNKYPGQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK10762 345 ----MSVKENMSLTAL--RYFSRAggslkhADEQQAVsDFIRlfNIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
44-243 |
5.46e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGErIV-VAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEvRREVGMVF-----QHFNLF 117
Cdd:COG3845 273 ALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG--LSPRE-RRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 PHLTILENCTLAPIWVRKMPK------KQAEEIAMHYLER--VKIPEQANKyPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
47-242 |
6.37e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 47 DINLKVMRGERIVVAGPSGSGKSTMIRCI-----NRLEehqkGKIVVDG--IELTNDLKKID-------EVRREVGMVfq 112
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRWE----GEIFIDGkpVKIRNPQQAIAqgiamvpEDRKRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 113 hfnlfPHLTILENCTLAPI---WVRKMPKKQAEE-IAMHYLERVKI----PEQAnkyPGQLSGGQQQRVAIARALCMNPK 184
Cdd:PRK13549 354 -----PVMGVGKNITLAALdrfTGGSRIDDAAELkTILESIQRLKVktasPELA---IARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
27-245 |
6.90e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.84 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTnDLKkIDEVRRE 106
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQ-LDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 VGMVFQHFNLFPHlTILENCTLAPIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQ----LSGGQQQRVAIARALCMN 182
Cdd:PRK10789 391 LAVVSQTPFLFSD-TVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMvSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQIVEQ 245
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNL-RQWGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQR 530
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
45-250 |
1.07e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQkGKIVVDGIELtNDLKkIDEVRREVGMVFQHFnlfPHLTILe 124
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPL-SDWS-AAELARHRAYLSQQQ---SPPFAM- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 125 nctlaPIW------VRKMPKKQAEEIAMHYL-ERVKIpeqANKYP---GQLSGGQQQRVAIARALC-----MNP--KVML 187
Cdd:COG4138 85 -----PVFqylalhQPAGASSEAVEQLLAQLaEALGL---EDKLSrplTQLSGGEWQRVRLAAVLLqvwptINPegQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 188 FDEPTSALDpemV--KEVLDTMVS-LAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:COG4138 157 LDEPMNSLD---VaqQAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
44-251 |
2.39e-17 |
|
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: 81.53 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQHFNLFP----- 118
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK--IGLHDLRFKITIIPQDPVLFSgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCTLAPIWVrkmpkkqAEEIAmHYLERV-----KIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTS 193
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWW-------ALELA-HLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 194 ALDPEmVKEVLDTMVSLAAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDEF 251
Cdd:TIGR00957 1451 AVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
45-225 |
2.43e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKidevrREVGMVFQHFNL---FPHLt 121
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK-----NLVAYVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 iLENCTLAPI-----WVRKmPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PRK15056 97 -VEDVVMMGRyghmgWLRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180
....*....|....*....|....*....
gi 489053699 197 PEMVKEVLDTMVSLAAEGMTMICVTHEMG 225
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
45-224 |
2.90e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIEL--TNDLKKIDEvrrEVGMVFQHFNLFPHLTI 122
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAA---GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENctlapIWVRKMP-------KKQAEEIAMHYLERVKI---PEQANKYpgqLSGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:PRK11288 97 AEN-----LYLGQLPhkggivnRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|..
gi 489053699 193 SALDPEMVKEVLDTMVSLAAEGMTMICVTHEM 224
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-243 |
4.39e-17 |
|
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: 78.14 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 14 IEVD--RSKMQVSKTEVAIEITNMHKWYGEFH---VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVV 88
Cdd:cd03267 1 IEVSnlSKSYRVYSKEPGLIGSLKSLFKRKYReveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 89 DGIEltnDLKKIDEVRREVGMVF-QHFNLFPHLTILENCTL-APIWvrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLS 166
Cdd:cd03267 81 AGLV---PWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLlAAIY--DLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 167 GGQQQRVAIARALCMNPKVMLFDEPTSALD---PEMVKEVLDTMVslAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
45-244 |
5.93e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.83 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGIELT-NDLKkiDEVRREVGMVFQHFNLFPHLT 121
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRfKDIR--DSEALGIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENctlapIWVRKMPKK-------QAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:NF040905 95 IAEN-----IFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489053699 195 LDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVE 244
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
41-243 |
8.50e-17 |
|
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: 76.53 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQK--GKIVVDGIeltnDLKKIDEV-RREVGMVFQHFNL 116
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGI----PYKEFAEKyPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 FPHLTILEncTLApiWVRKMpkkqaeeiamhylervkipeQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:cd03233 95 FPTLTVRE--TLD--FALRC--------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489053699 197 PEMVKEVLDTMVSLA-AEGMT-MICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:cd03233 151 SSTALEILKCIRTMAdVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-260 |
9.80e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 78.21 E-value: 9.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIeltNDLKKIDEVRREVGMVF-QHFNLF 117
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY---VPFKRRKEFARRIGVVFgQRSQLW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 PHLTILEN-CTLAPIWvrKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:COG4586 109 WDLPAIDSfRLLKAIY--RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 197 P---EMVKEVLDTMVslAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERT 260
Cdd:COG4586 187 VvskEAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
40-222 |
1.18e-16 |
|
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: 75.86 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltNDLKKIDEVRREVGMVFQHFN-LFP 118
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG----TPLAEQRDEPHENILYLGHLPgLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLTILENCT-LAPIwvrkmpkKQAEEIAMH-YLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:TIGR01189 87 ELSALENLHfWAAI-------HGGAQRTIEdALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*.
gi 489053699 197 PEMVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
40-222 |
1.76e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.61 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 40 GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGielTNDLKKIDEVRREVGMVFQHFNLFPH 119
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 120 LTILENCTLapiWVRKMPKKQAEEIamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEM 199
Cdd:cd03231 88 LSVLENLRF---WHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 489053699 200 VKEVLDTMVSLAAEGMTMICVTH 222
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
46-242 |
6.02e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 46 RDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdevRREVGMVF-----QHFNLFPHL 120
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ---RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 121 TILEN-CTLA----PIWVRkmPKKQAEeiamhYLER------VKIpEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFD 189
Cdd:PRK15439 357 PLAWNvCALThnrrGFWIK--PARENA-----VLERyrralnIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489053699 190 EPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
136-251 |
8.72e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.93 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 136 MPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGM 215
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 489053699 216 TMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEF 251
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
45-254 |
1.13e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVdgieltndlkkideVRREVGMVFQHFNLFpHLTILE 124
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV--------------IRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 125 NCTLAPIWVRKMPKKQAEEIAMHY-------LERVKIPEQANkypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:PLN03232 698 NILFGSDFESERYWRAIDVTALQHdldllpgRDLTEIGERGV----NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
45-253 |
2.01e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.14 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG-IELTNDLKKIDEVRREVGMVFQH-FNLFPHLTI 122
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsVAYVPQQAWIQNDSLRENILFGKaLNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTLAPIwVRKMPKKqaeeiamhylERVKIPEQANkypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:TIGR00957 734 LEACALLPD-LEILPSG----------DRTEIGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 203 VLDTMVslAAEGM----TMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDEFFD 253
Cdd:TIGR00957 799 IFEHVI--GPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
44-269 |
2.42e-15 |
|
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: 74.12 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG-IELTNDLKKIDEVRREVGMVFQ-HFNLFPHLT 121
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFSWIMPGTIKENIIFGvSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwvrkmpkkqaEEIAmhylervKIPEQANKYPGQ----LSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:cd03291 132 VVKACQLE------------EDIT-------KFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQI--------VEQNSPD--------EFFDNPQHERTR 261
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSyfygtfseLQSLRPDfssklmgyDTFDQFSAERRN 271
|
....*...
gi 489053699 262 LFLSQILH 269
Cdd:cd03291 272 SILTETLR 279
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
165-254 |
4.10e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVE 244
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
90
....*....|
gi 489053699 245 QNSPDEFFDN 254
Cdd:PLN03130 820 EGTYEELSNN 829
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
52-250 |
4.78e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 52 VMRGERIVVAGPSGSGKSTMIRCINRLEEHqKGKIVVDGIEL----TNDLKKI-----DEVRREVGM-VFQHFNLFPHlt 121
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLeawsAAELARHraylsQQQTPPFAMpVFQYLTLHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ilencTLAPIwvrkmpkkQAEEIAMHYL-ERVKIPEQANKYPGQLSGGQQQRVAIArALCM------NP--KVMLFDEPT 192
Cdd:PRK03695 96 -----DKTRT--------EAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVLqvwpdiNPagQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 193 SALDPEMVKeVLDTMVS-LAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK03695 162 NSLDVAQQA-ALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
48-267 |
1.52e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.14 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCInrleehqkGKIVVDGIELTNDLKKIDEV----------RREVG----MVFQH 113
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAI--------CGVTKDNWRVTADRMRFDDIdllrlsprerRKLVGhnvsMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 114 FN--LFPHLTILENCTLA-PIWVRKMPKKQA----EEIAMHYLERVKIPEQAN---KYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK15093 98 PQscLDPSERVGRQLMQNiPGWTYKGRWWQRfgwrKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSL-AAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFDNPQHERTRL 262
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
....*
gi 489053699 263 FLSQI 267
Cdd:PRK15093 258 LIRAI 262
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
62-250 |
2.40e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdeVRREVGMVFQHFNLFPHLTILEnctLAPI----W----- 132
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEGMTVRE---LVAIgrypWhgalg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 133 -VRKMPKKQAEE-IAMhylerVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSL 210
Cdd:PRK10575 119 rFGAADREKVEEaISL-----VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489053699 211 AAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDE 250
Cdd:PRK10575 194 SQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
48-244 |
2.45e-14 |
|
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: 72.52 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkKIDEVRREVGMVFQHFNLFPHLTILENCT 127
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NREAYRQLFSAVFSDFHLFDRLLGLDGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 128 LapiwvrkmpkkqaEEIAMHYLERVKIpeqANKYP---G-----QLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEM 199
Cdd:COG4615 429 D-------------PARARELLERLEL---DHKVSvedGrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489053699 200 VK----EVLdtmVSLAAEGMTMICVTH-EMGFarQVANRVIFMDQGQIVE 244
Cdd:COG4615 493 RRvfytELL---PELKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
43-241 |
2.70e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVV-DGIEltndlkkidevrreVGMVFQHFNLFPHLT 121
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIK--------------VGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwVRKMPKKQAE--EIAMHYLE-----------------------------RVKIPEQANKYP------GQ 164
Cdd:TIGR03719 85 VRENVEEG---VAEIKDALDRfnEISAKYAEpdadfdklaaeqaelqeiidaadawdldsQLEIAMDALRCPpwdadvTK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkEVLDTMvsLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERH--LQEYPGTVVAVTHDRYFLDNVAGWILELDRGR 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-254 |
3.50e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWY--GEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT----NDLKKIDE 102
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 VRREVGMVFQ---HFNLFPhltiLENCTLAPIWvrkmpkkqaeeiamHYLERVKIPEQANKYPGQL-----------SGG 168
Cdd:PLN03232 1314 IIPQSPVLFSgtvRFNIDP----FSEHNDADLW--------------EALERAHIKDVIDRNPFGLdaevseggenfSVG 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 169 QQQRVAIARALCMNPKVMLFDEPTSALDPEmVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSP 248
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVDVR-TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSP 1453
|
....*.
gi 489053699 249 DEFFDN 254
Cdd:PLN03232 1454 QELLSR 1459
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-243 |
4.89e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 32 ITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtnDLKKIDE-VRREVGMV 110
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEaLENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 111 FQHFNLFPHLTILENctlapIWVRKMPKKQ--AEEIAMH-----YLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNP 183
Cdd:PRK10982 79 HQELNLVLQRSVMDN-----MWLGRYPTKGmfVDQDKMYrdtkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-245 |
6.50e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 26 TEVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKiDEVRR 105
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK-SSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFPHLTILENCTLAPIWVRKMP----KKQAEEiAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCM 181
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRFGridwKKMYAE-ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 182 NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ-IVEQ 245
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
84-249 |
1.53e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 84 GKIVVDGIELTN-DLKkidEVRREVGMVFQHFNLFpHLTILENCTLAPIWVRKMPKKQAEEIAM--HYLERV--KIPEQA 158
Cdd:PTZ00265 1277 GKILLDGVDICDyNLK---DLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAidEFIESLpnKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 159 NKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEG-MTMICVTHEMGFARQVANRVIFm 237
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVF- 1431
|
170
....*....|..
gi 489053699 238 dqgqiveqNSPD 249
Cdd:PTZ00265 1432 --------NNPD 1435
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
52-240 |
1.58e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 52 VMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELtndLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPi 131
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA- 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 132 WVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLA 211
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 489053699 212 AEGMTMICVTHEMGFARQVANRVIFMDQG 240
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-222 |
2.07e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVL-RDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlKKIDEVRREVgmvfqHFNLF---- 117
Cdd:PRK13538 14 RILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDEY-----HQDLLylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 -----PHLTILENctLApiWVRKMPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:PRK13538 82 qpgikTELTALEN--LR--FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 489053699 193 SALDPEMVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-243 |
3.08e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKiDEVRREVGM 109
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ-DPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VF-----------QHFNLFPHLTILenctLAPIWVRKMPKK--QAEEIAMHY------------LERVKIPeqANKYPGQ 164
Cdd:PRK11147 83 VYdfvaegieeqaEYLKRYHDISHL----VETDPSEKNLNElaKLQEQLDHHnlwqlenrinevLAQLGLD--PDAALSS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkEVLDTMVsLAAEGmTMICVTHEMGFARQVANRVIFMDQGQIV 243
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETI-EWLEGFL-KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-256 |
3.12e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQHFNLFPHlTIL 123
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA--YGLRELRRQFSMIPQDPVLFDG-TVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 EN------CTLAPIW-------VRKMPKKQAEEIAMHYLErvkipeQANKYpgqlSGGQQQRVAIARALCM-NPKVMLFD 189
Cdd:PTZ00243 1402 QNvdpfleASSAEVWaalelvgLRERVASESEGIDSRVLE------GGSNY----SVGQRQLMCMARALLKkGSGFILMD 1471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 190 EPTSALDPEMVKEVLDTMVSlAAEGMTMICVTHEMGFARQVaNRVIFMDQGQIVEQNSPDEFFDNPQ 256
Cdd:PTZ00243 1472 EATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
48-243 |
3.64e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 48 INLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlKKIDEVRRevGMVF-----QHFNLFPHLTI 122
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR-SPRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 LENCTlapIWVRK--------MPKKQAEEIAMHYLERVKI----PEQAnkyPGQLSGGQQQRVAIARALCMNPKVMLFDE 190
Cdd:PRK11288 349 ADNIN---ISARRhhlragclINNRWEAENADRFIRSLNIktpsREQL---IMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 191 PTSALDPEMVKEVLDTMVSLAAEGMTMICVTHE----MGfarqVANRVIFMDQGQIV 243
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIA 475
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-251 |
3.84e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIvvdgieltndlkKIDEvRREVG 108
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSE-NANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQ-HFNLFPH-LTILEnctlapiWVRKMPKKQAEEIAMH-YLERVKIP-EQANKYPGQLSGGQQQRVAIARALCMNPK 184
Cdd:PRK15064 386 YYAQdHAYDFENdLTLFD-------WMSQWRQEGDDEQAVRgTLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489053699 185 VMLFDEPTSALDPEMVkEVLDTMVSLaAEGmTMICVTHEMGFARQVANRVIFMDQGQIVE-QNSPDEF 251
Cdd:PRK15064 459 VLVMDEPTNHMDMESI-ESLNMALEK-YEG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEY 523
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-269 |
5.22e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.78 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDG-IELTNDLKKIDEVRREVGMVFQ-HFNLFPHLT 121
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrISFSPQTSWIMPGTIKDNIIFGlSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwvrkmpkkqaEEIAmhylervKIPEQANKYPGQ----LSGGQQQRVAIARALCMNPKVMLFDEPTSALDP 197
Cdd:TIGR01271 521 VIKACQLE------------EDIA-------LFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 198 EMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQI--------VEQNSPD--------EFFDNPQHERTR 261
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCyfygtfseLQAKRPDfsslllglEAFDNFSAERRN 660
|
....*...
gi 489053699 262 LFLSQILH 269
Cdd:TIGR01271 661 SILTETLR 668
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-245 |
5.93e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 2 SAQSALQQSGIGIE-----VDRSKMQVSKTEVA-----IEITNMHKWYGEFH-VLRDINLKVMRGERIVVAGPSGSGKST 70
Cdd:PRK10790 303 TQQSMLQQAVVAGErvfelMDGPRQQYGNDDRPlqsgrIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKST 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 71 MIRCINRLEEHQKGKIVVDGIELTNDLKKIdeVRREVGMVFQH-----FNLFPHLTI------------LENCTLAPiWV 133
Cdd:PRK10790 383 LASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVAMVQQDpvvlaDTFLANVTLgrdiseeqvwqaLETVQLAE-LA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 134 RKMPKkqaeeiAMHylerVKIPEQANKypgqLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP---EMVKEVLdtmvSL 210
Cdd:PRK10790 460 RSLPD------GLY----TPLGEQGNN----LSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQAL----AA 521
|
250 260 270
....*....|....*....|....*....|....*
gi 489053699 211 AAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQ 245
Cdd:PRK10790 522 VREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
44-252 |
1.68e-12 |
|
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: 65.70 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNdlKKIDEVRREVGMVFQ---------HF 114
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--LPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 NLFPHLTilenCTLAPIWvrkmpkkQAEEIAmhylervKIPEQANKYPGQL-----------SGGQQQRVAIARALCMNP 183
Cdd:cd03288 114 NLDPECK----CTDDRLW-------EALEIA-------QLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 184 KVMLFDEPTSALDpeMVKE-VLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFF 252
Cdd:cd03288 176 SILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-226 |
2.34e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINrlEEHQKGkivvdgieLTNDL----------KKIDEVRREVG 108
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT--GDHPQG--------YSNDLtlfgrrrgsgETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 109 MVFQHFnlfpHLTILENCTLAPIWV----------RKMPKKQaEEIAMHYLERVKIPEQANKYPGQ-LSGGQQQRVAIAR 177
Cdd:PRK10938 340 YVSSSL----HLDYRVSTSVRNVILsgffdsigiyQAVSDRQ-QKLAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVR 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 178 ALCMNPKVMLFDEPTSALDP---EMVKEVLDTMVSlaaEGMTMI------------CVTHEMGF 226
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETQLlfvshhaedapaCITHRLEF 475
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-238 |
3.67e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.35 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 35 MHKWYGEFHvlrdinLKV-----MRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIvvdGIELTNDLKKIDEVRREVGM 109
Cdd:cd03237 6 MKKTLGEFT------LEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFnLFphlTILENCTLAPIWVRKMPKK-QAEEIamhyLERvKIPEqankypgqLSGGQQQRVAIARALCMNPKVMLF 188
Cdd:cd03237 77 TVRDL-LS---SITKDFYTHPYFKTEIAKPlQIEQI----LDR-EVPE--------LSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489053699 189 DEPTSALDPE---MVKEVLDTMVsLAAEGmTMICVTHEMGFARQVANRVIFMD 238
Cdd:cd03237 140 DEPSAYLDVEqrlMASKVIRRFA-ENNEK-TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-196 |
5.06e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIvvdgieltndlKKIDEVRreVGMVFQHFNLFP 118
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR--IGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 119 HLtilenctlaPIWVRKM----PKKQAEEIaMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:PRK09544 81 TL---------PLTVNRFlrlrPGTKKEDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 489053699 195 LD 196
Cdd:PRK09544 151 VD 152
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
30-244 |
1.24e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.12 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGIELtndLKKIDEVRREV 107
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESI---LDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 G--MVFQHFNLFPHLTILENCTLAPIWVRK-MPKKQAE-----EIAMHYLERVKI-PEQANKYPGQ-LSGGQQQRVAIAR 177
Cdd:CHL00131 85 GifLAFQYPIEIPGVSNADFLRLAYNSKRKfQGLPELDpleflEIINEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 178 ALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHemgFARQ----VANRVIFMDQGQIVE 244
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIK 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
45-223 |
1.45e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 61.88 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEE--HQKGKIVVDGIELTNDLkkidevRREVGMVFQHFNLFPHLTi 122
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNF------QRSTGYVEQQDVHSPNLT- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 lenctlapiwVRkmpkkqaEEIAMHYLERvkipeqankypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:cd03232 96 ----------VR-------EALRFSALLR------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 489053699 203 VLDTMVSLAAEGMTMICVTHE 223
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQ 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
45-244 |
1.93e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 45 LRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTND--LKKID-------EVRREVGmvfqhfn 115
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaNEAINhgfalvtEERRSTG------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 116 LFPHLTILENCTLAPIWV----------RKMPKKQAEEI-AMhyleRVKIPEQANKYpGQLSGGQQQRVAIARALCMNPK 184
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNyknkvglldnSRMKSDTQWVIdSM----RVKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489053699 185 VMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ---IVE 244
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVD 474
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
44-248 |
3.82e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCinrLEEHQKGKIVVDGIELTND-------LKKIDEVR----REV----- 107
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKA---LAGDLTGGGAPRGARVTGDvtlngepLAAIDAPRlarlRAVlpqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 --GMVFQHFNL-----FPHltilenctlapiwVRK--MPKKQAEEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARA 178
Cdd:PRK13547 93 qpAFAFSAREIvllgrYPH-------------ARRagALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 179 LCM---------NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSP 248
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
30-240 |
3.98e-11 |
|
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: 61.19 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITN-MHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCInrLEEHQK--GKIVVDGIELTNDLKKIDEVRRE 106
Cdd:cd03290 1 VQVTNgYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTleGKVHWSNKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 --VGMVFQHFNLFpHLTILENCTLAPIWVRKMPKKQAEEIAMH-------YLERVKIPEQANkypgQLSGGQQQRVAIAR 177
Cdd:cd03290 79 ysVAYAAQKPWLL-NATVEENITFGSPFNKQRYKAVTDACSLQpdidllpFGDQTEIGERGI----NLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 178 ALCMNPKVMLFDEPTSALDPEMVKEVLDTMV--SLAAEGMTMICVTHEMGFARQvANRVIFMDQG 240
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMQEGIlkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
44-222 |
4.61e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDlkkidEVRREVGMVFQHFNLFPHLTIL 123
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-----DRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 EN----CTLAPIWVRKMPKKQaeeiamhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEM 199
Cdd:PRK13543 101 ENlhflCGLHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180
....*....|....*....|....*
gi 489053699 200 VKeVLDTMVS--LAAEGMTMIcVTH 222
Cdd:PRK13543 173 IT-LVNRMISahLRGGGAALV-TTH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-244 |
6.51e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 20 KMQVSKTE----VAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRC-INRLEEhQKGKIVVdGIELt 94
Cdd:PRK11147 306 KMQVEEASrsgkIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHC-GTKL- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 95 ndlkkidevrrEVGMVFQH-FNLFPHLTILENctLApiwvrkmPKKQAEEI------AMHYLE-------RVKIPEQAnk 160
Cdd:PRK11147 383 -----------EVAYFDQHrAELDPEKTVMDN--LA-------EGKQEVMVngrprhVLGYLQdflfhpkRAMTPVKA-- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 161 ypgqLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkEVLDTMvsLAAEGMTMICVTHEMGFarqVANRV----IF 236
Cdd:PRK11147 441 ----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF---VDNTVtecwIF 510
|
....*...
gi 489053699 237 MDQGQIVE 244
Cdd:PRK11147 511 EGNGKIGR 518
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
30-255 |
7.24e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYG---EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGielTNDLKKIDEV--R 104
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLKwwR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 105 REVGMVFQHFNLFPH---------------LTILEN------------------CTLAP----------------IWVRK 135
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNsiknnikyslyslkdLEALSNyynedgndsqenknkrnsCRAKCagdlndmsnttdsnelIEMRK 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 136 MPKKQAEEIAMHYLERVKIPEQANKYP-----------GQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVL 204
Cdd:PTZ00265 540 NYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489053699 205 DTMVSLAA-EGMTMICVTHEMGFARqVANRVIFMDQGQIVEQNSPDEFFDNP 255
Cdd:PTZ00265 620 KTINNLKGnENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
41-267 |
9.22e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 41 EFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI-NRLEEHQKGK---IVVDGIELtNDLKKidEVRREVGMVFQHFNL 116
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFHIGVegvITYDGITP-EEIKK--HYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 FPHLTILEncTLAPIWVRKMP-------------KKQAEEIAMHY-LERVKIPEQANKYPGQLSGGQQQRVAIARALCMN 182
Cdd:TIGR00956 150 FPHLTVGE--TLDFAARCKTPqnrpdgvsreeyaKHIADVYMATYgLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 183 PKVMLFDEPTSALDP----EMVKeVLDTMVSL--AAEGMTMICVTHEmgfARQVANRVIFMDQGQIVEQNSPD---EFFD 253
Cdd:TIGR00956 228 AKIQCWDNATRGLDSatalEFIR-ALKTSANIldTTPLVAIYQCSQD---AYELFDKVIVLYEGYQIYFGPADkakQYFE 303
|
250
....*....|....*....
gi 489053699 254 N-----PQHERTRLFLSQI 267
Cdd:TIGR00956 304 KmgfkcPDRQTTADFLTSL 322
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
27-250 |
9.25e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELT-NDLkkidEVRR 105
Cdd:NF033858 264 EPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDI----ATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 106 EVGMVFQHFNLFPHLTILENCTL-APIWvrKMPKKQAEE-IA-MhyLERVKIPEQANKYPGQLSGGQQQRVAIARALCMN 182
Cdd:NF033858 340 RVGYMSQAFSLYGELTVRQNLELhARLF--HLPAAEIAArVAeM--LERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 183 PKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFArQVANRVIFMDQGQIVEQNSPDE 250
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
44-197 |
1.02e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEhQKGKIVVDGIELtnDLKKIDEVRREVGMVFQHF--------- 114
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSW--NSVTLQTWRKAFGVIPQKVfifsgtfrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 NLFPHltilENCTLAPIWvrkmpkKQAEEIAMHylervKIPEQankYPGQL-----------SGGQQQRVAIARALCMNP 183
Cdd:TIGR01271 1311 NLDPY----EQWSDEEIW------KVAEEVGLK-----SVIEQ---FPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372
|
170
....*....|....
gi 489053699 184 KVMLFDEPTSALDP 197
Cdd:TIGR01271 1373 KILLLDEPSAHLDP 1386
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
62-223 |
1.05e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCinrLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPiWVRKmPKKQA 141
Cdd:TIGR00956 796 GASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSA-YLRQ-PKSVS 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 142 EEIAMHYLERV-KIPEQaNKY-------PGQ-LSGGQQQRVAIARALCMNPKVMLF-DEPTSALDPEMVKEVLDTMVSLA 211
Cdd:TIGR00956 871 KSEKMEYVEEViKLLEM-ESYadavvgvPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLA 949
|
170
....*....|..
gi 489053699 212 AEGMTMICVTHE 223
Cdd:TIGR00956 950 DHGQAILCTIHQ 961
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-223 |
1.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.58 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKideVRREVGM 109
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT---YQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 VFQHFNLFPHLTILENCTLapiwvrkmpKKQAEEIAMHYLERVKI--PEQANKYP-GQLSGGQQQRVAIARALCMNPKVM 186
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLY---------DIHFSPGAVGITELCRLfsLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 489053699 187 LFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHE 223
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-254 |
1.26e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTN----DLKKIDEVRREVGMVFQ---HFNL 116
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGIIPQAPVLFSgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 117 FP---H-----LTILENCTLAPIwVRKMPKKQAEEIAmhylervkipEQANKYpgqlSGGQQQRVAIARALCMNPKVMLF 188
Cdd:PLN03130 1334 DPfneHndadlWESLERAHLKDV-IRRNSLGLDAEVS----------EAGENF----SVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 189 DEPTSALD-------PEMVKEVLD--TMVSLAAEGMTMI-CvthemgfarqvaNRVIFMDQGQIVEQNSPDEFFDN 254
Cdd:PLN03130 1399 DEATAAVDvrtdaliQKTIREEFKscTMLIIAHRLNTIIdC------------DRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-243 |
1.26e-10 |
|
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: 61.10 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGielTNDLKKIDEVRRe 106
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---TVKLAYVDQSRD- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 vgmvfqhfNLFPHLTILENCT--LAPIWV--RKMPKKQaeeiamhYLER--VKIPEQaNKYPGQLSGGQQQRVAIARALC 180
Cdd:TIGR03719 396 --------ALDPNKTVWEEISggLDIIKLgkREIPSRA-------YVGRfnFKGSDQ-QKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 181 MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAaeGMTMIcVTHEMGFARQVANRVI-FMDQGQIV 243
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVV-ISHDRWFLDRIATHILaFEGDSHVE 520
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-198 |
2.38e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 22 QVSKTEVAIEITNMHKWYGEFHvlrdinLKV-----MRGERIVVAGPSGSGKSTMIRCINRLEEHQKGkivvdgiELTND 96
Cdd:COG1245 334 REKEEETLVEYPDLTKSYGGFS------LEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 LK---KIDEVRREVGMVFQhfnlfphlTILENCTLAPI---WVRkmpkkqaEEIAmhylERVKIPEQANKYPGQLSGGQQ 170
Cdd:COG1245 401 LKisyKPQYISPDYDGTVE--------EFLRSANTDDFgssYYK-------TEII----KPLGLEKLLDKNVKDLSGGEL 461
|
170 180
....*....|....*....|....*...
gi 489053699 171 QRVAIARALCMNPKVMLFDEPTSALDPE 198
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
35-235 |
3.16e-10 |
|
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: 57.97 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 35 MHKWYGEFHVLRDINlKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIDevrrevgmvfqhf 114
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 115 nlfphltilenctlapiwvrkmpkkqaeeiamhylervkipeqankypgqLSGGQQQRVAIARALCMNPKVMLFDEPTSA 194
Cdd:cd03222 72 --------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489053699 195 LDPEMVKEVLDTMVSLAAEGM-TMICVTHEMGFARQVANRVI 235
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-235 |
3.50e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 24 SKTEVAIEITNMHKWYGEFHvlrdinLKVM-----RGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDgieltndLK 98
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDFS------LEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------LK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 99 ---KIDEVRREVGMVfqhfnlfphltilenctlapiwVRKMPKKQAEEIAMHY-----LERVKIPEQANKYPGQLSGGQQ 170
Cdd:PRK13409 402 isyKPQYIKPDYDGT----------------------VEDLLRSITDDLGSSYykseiIKPLQLERLLDKNVKDLSGGEL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489053699 171 QRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-GMTMICVTHEMGFARQVANRVI 235
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
44-263 |
3.84e-10 |
|
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: 59.10 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEeHQKGKIVVDGIELtnDLKKIDEVRREVGMVFQHFNLFPHlTIL 123
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSW--NSVPLQKWRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLAPIWVRKMPKKQAEEIAMHylervKIPEQankYPGQL-----------SGGQQQRVAIARALCMNPKVMLFDEPT 192
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEVGLK-----SVIEQ---FPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 193 SALDPeMVKEVLDTMVSLAAEGMTMICVTHEMGfARQVANRVIFMDQGQIVEQNSPDEFFDNPQH--------ERTRLF 263
Cdd:cd03289 167 AHLDP-ITYQVIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEKSHfkqaispsDRLKLF 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
54-236 |
4.97e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 54 RGERIVVAGPSGSGKSTMIRCI-NRLEEHQKGKIVVDGieltndlkkidevrrevgmvfqhfnlfphltilenctlapiw 132
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 133 vrkmpkkqaeEIAMHYLERVKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLD------T 206
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180 190
....*....|....*....|....*....|
gi 489053699 207 MVSLAAEGMTMICVTHEMGFARQVANRVIF 236
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-243 |
5.57e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 27 EVAIEITN---MHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGkstmircinRLE-----------EHQKGKIVVDG-- 90
Cdd:NF040905 255 EVVFEVKNwtvYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAG---------RTElamsvfgrsygRNISGTVFKDGke 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 91 IELTNDLKKID-------EVRREVGMVFQHfnlfphlTILENCTLAPIwvRKMPKK----QAEEI--AMHYLERVKIpeq 157
Cdd:NF040905 326 VDVSTVSDAIDaglayvtEDRKGYGLNLID-------DIKRNITLANL--GKVSRRgvidENEEIkvAEEYRKKMNI--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 158 anKYP------GQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQVA 231
Cdd:NF040905 394 --KTPsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMC 471
|
250
....*....|..
gi 489053699 232 NRVIFMDQGQIV 243
Cdd:NF040905 472 DRIYVMNEGRIT 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
43-241 |
1.92e-09 |
|
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: 55.41 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTmircinrleehqkgkIVVDGIELTNDLKKIDEVRRevgmvfqhfnLFPHLTI 122
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLYASGKARLISFLPK----------FSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 123 ----LENCTlapiwvrkmpkkqaeEIAMHYLErvkiPEQAnkyPGQLSGGQQQRVAIARALCMNPK--VMLFDEPTSALD 196
Cdd:cd03238 64 fidqLQFLI---------------DVGLGYLT----LGQK---LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489053699 197 PEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVIFMDQGQ 241
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
59-223 |
8.34e-09 |
|
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: 54.15 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 59 VVAGPSGSGKSTMIRCIN-----RLEEHQKGKIVVDgieltnDLKKIDEVRREVGMVFQHFN-----LFPHLTILENCtl 128
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltgELPPNSKGGAHDP------KLIREGEVRAQVKLAFENANgkkytITRSLAILENV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 129 apIWVRKmpkkqaEEIamhyleRVKIPEQankyPGQLSGGQQQ------RVAIARALCMNPKVMLFDEPTSALDPEMVKE 202
Cdd:cd03240 98 --IFCHQ------GES------NWPLLDM----RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|...
gi 489053699 203 VLDTMVS--LAAEGMTMICVTHE 223
Cdd:cd03240 160 SLAEIIEerKSQKNFQLIVITHD 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
43-241 |
9.88e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVV-DGIEltndlkkidevrreVGMVFQHFNLFPHLT 121
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIK--------------VGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLApiwVRKMPKKQAE--EIAMHYLE-----------------------------RVKIPEQANKYP------GQ 164
Cdd:PRK11819 87 VRENVEEG---VAEVKAALDRfnEIYAAYAEpdadfdalaaeqgelqeiidaadawdldsQLEIAMDALRCPpwdakvTK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkEVLDTMvsLAAEGMTMICVTHEMGFARQVANRVIFMDQGQ 241
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQF--LHDYPGTVVAVTHDRYFLDNVAGWILELDRGR 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-261 |
1.14e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.56 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 1 MSAQSALQQSGIGIEVDRSKM-QVSKTEVAIEITNMHKWYGEFHV-----LRDINLKVMRGERIVVAGPSGSGKSTMIRC 74
Cdd:PTZ00243 626 TDYGSPSSASRHIVEGGTGGGhEATPTSERSAKTPKMKTDDFFELepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQS 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 75 INRLEEHQKGKIVVDgieltndlkkidevrREVGMVfqhfnlfPHLTILENCTlapiwVR--------KMPKKQAEEIAM 146
Cdd:PTZ00243 706 LLSQFEISEGRVWAE---------------RSIAYV-------PQQAWIMNAT-----VRgnilffdeEDAARLADAVRV 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 147 HYLE----------RVKIPEQANkypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMT 216
Cdd:PTZ00243 759 SQLEadlaqlggglETEIGEKGV----NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKT 834
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489053699 217 MICVTHEMGFARQvANRVIFMDQGQIVEQNSPDEFFDNPQHERTR 261
Cdd:PTZ00243 835 RVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
43-235 |
1.77e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.42 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMI----------RCINRLEE------HQKGKIVVDGIE-----LTNDLKKID 101
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarqflGQMDKPDVDSIEglspaIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 102 E-VRREVGMVFQHFN----LFPHLTILEncTLapiwvrkmpkKQAEEIAMHYLervkipeQANKYPGQLSGGQQQRVAIA 176
Cdd:cd03270 89 RnPRSTVGTVTEIYDylrlLFARVGIRE--RL----------GFLVDVGLGYL-------TLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 177 RALCMNPKVML--FDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANRVI 235
Cdd:cd03270 150 TQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
62-224 |
3.16e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 62 GPSGSGKSTMIRCI--------NRLEEHQKGKIVVD---GIELTNDLKKIDEVRREVGMVFQHFNLFPHL---TILENct 127
Cdd:cd03236 33 GPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAvkgKVGEL-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 128 lapiwVRKMPKKQAEEIAMHYLERVKIPEQANKypgQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTM 207
Cdd:cd03236 111 -----LKKKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLI 182
|
170
....*....|....*..
gi 489053699 208 VSLAAEGMTMICVTHEM 224
Cdd:cd03236 183 RELAEDDNYVLVVEHDL 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
43-248 |
3.23e-08 |
|
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: 53.00 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMI-----RCINRLEEHQKGKI----VVDGIELTNDLKKIDevRREVGM---- 109
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQPgnhdRIEGLEHIDKVIVID--QSPIGRtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 110 -------VFQHF-NLFphltiLENC--------TLApiwVRKMPKKQAEEIAMHYLERVK----IPEQANKYP------- 162
Cdd:cd03271 87 npatytgVFDEIrELF-----CEVCkgkrynreTLE---VRYKGKSIADVLDMTVEEALEffenIPKIARKLQtlcdvgl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 163 -----GQ----LSGGQQQRVAIARALCM---NPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARqV 230
Cdd:cd03271 159 gyiklGQpattLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK-C 237
|
250 260
....*....|....*....|....
gi 489053699 231 ANRVIFMDQ------GQIVEQNSP 248
Cdd:cd03271 238 ADWIIDLGPeggdggGQVVASGTP 261
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
44-223 |
6.21e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIrciNRLEEHQKGKIVVDGIELTNDLKKIDEVRREVGMVFQHFNLFPHLTIL 123
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLA-----PIWVRKMPKKQAEEIAMHYLERVKIPEQANKYPG--QLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PLN03140 972 ESLIYSaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180
....*....|....*....|....*..
gi 489053699 197 PEMVKEVLDTMVSLAAEGMTMICVTHE 223
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-198 |
7.30e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 28 VAIEITNMHKWYGEFHVLRDINLKVMRGErIV-VAGPSGSGKSTMIRCINRLEEHQKGKIVVDGielTNDLKKIDEVRRe 106
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGG-IVgIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE---TVKLAYVDQSRD- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 107 vgmvfqhfNLFPHLTILENCT--LAPIWV--RKMPKKQaeeiamhYLER--VKIPEQaNKYPGQLSGGQQQRVAIARALC 180
Cdd:PRK11819 398 --------ALDPNKTVWEEISggLDIIKVgnREIPSRA-------YVGRfnFKGGDQ-QKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|....*...
gi 489053699 181 MNPKVMLFDEPTSALDPE 198
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVE 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
59-222 |
1.12e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 59 VVAGPSGSGKSTMIRCInrleehqkgkivvdgieltndlkkidevrrEVGMVFQHFNLFPHLTILENCTLApiwvrkmpk 138
Cdd:cd03227 25 IITGPNGSGKSTILDAI------------------------------GLALGGAQSATRRRSGVKAGCIVA--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 139 kqAEEIAMHYLeRVkipeqankypgQLSGGQQQRVAIARAL----CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEG 214
Cdd:cd03227 66 --AVSAELIFT-RL-----------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
....*...
gi 489053699 215 MTMICVTH 222
Cdd:cd03227 132 AQVIVITH 139
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-224 |
1.28e-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: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITN---------MHKwYGE--FhvlRDINLKVMRGERIV-VAGPSGSGKSTMIRcinrleehqkgkiVVDGiELTND 96
Cdd:COG1245 65 AISIVNlpeeleedpVHR-YGEngF---RLYGLPVPKKGKVTgILGPNGIGKSTALK-------------ILSG-ELKPN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 97 LKKIDEvrrEVG--MVFQHFN---LFPHLTILENCTL----APIWVRKMPK----------KQAEE--IAMHYLERVKIP 155
Cdd:COG1245 127 LGDYDE---EPSwdEVLKRFRgteLQDYFKKLANGEIkvahKPQYVDLIPKvfkgtvrellEKVDErgKLDELAEKLGLE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 156 EQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDpemVKE---VLDTMVSLAAEGMTMICVTHEM 224
Cdd:COG1245 204 NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-222 |
2.33e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 30 IEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGIELTnDLKKIDEVRREV 107
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLL-ELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 108 GMVFQHFNLFPHLT---ILENCTLApiwVRKMPKKQA------EEIAMHYLERVKIPEQ--ANKYPGQLSGGQQQRVAIA 176
Cdd:PRK09580 81 FMAFQYPVEIPGVSnqfFLQTALNA---VRSYRGQEPldrfdfQDLMEEKIALLKMPEDllTRSVNVGFSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489053699 177 RALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
42-259 |
2.44e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 42 FHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGieltndlkkidevrrEVGMVFQHFNLFPHLT 121
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 122 ILENCTLAPI---WVRKMPKKQAEEIAMHYLERVKIPEQANKYpgqlSGGQQQRVAIARALCMNPKVMLFDEPTSALDPE 198
Cdd:PRK13546 102 GIENIEFKMLcmgFKRKEIKAMTPKIIEFSELGEFIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 199 MVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRVIFMDQGQIVEQNSPDEFFdnPQHER 259
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYEA 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-242 |
3.46e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 39 YGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKI-VVDGIELTNDLKKIDEVRREVGMVFQHFnlf 117
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPLQHL--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 118 phltilenCTLAPiwvrkmpkKQAEEIAMHYLERVKIP-EQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALD 196
Cdd:PRK10636 399 --------ARLAP--------QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489053699 197 PEMVKEVLDTMVSLaaEGmTMICVTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK10636 463 LDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-261 |
4.26e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 155 PEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDpemVKEVLDTMVSLAAEGMTMICVTHEMGFARQVANRV 234
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
90 100
....*....|....*....|....*..
gi 489053699 235 IFMDQGQIVEQNSPDEFFDNPQHERTR 261
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLK 438
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
165-222 |
9.87e-07 |
|
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: 49.75 E-value: 9.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVkevlDTMVSLAAE-GMTMICVTH 222
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
14-250 |
1.75e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 14 IEVDRSKMQVSKTEvaIEITNMHKwygefHVLRDINLKVMRGERIVVAGPSGSGKSTMIRCI------NRLEEHQKGKIV 87
Cdd:TIGR00630 600 IEVPAERRPGNGKF--LTLKGARE-----NNLKNITVSIPLGLFTCITGVSGSGKSTLINDTlypalaNRLNGAKTVPGR 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 88 VDGIELTNDLKKI-----------------------DEVR---------REVGMVFQHFNLFPHLTILENCT-LAPIwvr 134
Cdd:TIGR00630 673 YTSIEGLEHLDKVihidqspigrtprsnpatytgvfDEIRelfaetpeaKVRGYTPGRFSFNVKGGRCEACQgDGVI--- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 135 kmpkkqaeEIAMHYLERVKIP-------------------------------EQA----NKYP----------------- 162
Cdd:TIGR00630 750 --------KIEMHFLPDVYVPcevckgkrynretlevkykgkniadvldmtvEEAyeffEAVPsisrklqtlcdvglgyi 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 163 --GQ----LSGGQQQRVAIARAL---CMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFARQvANR 233
Cdd:TIGR00630 822 rlGQpattLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADY 900
|
330 340
....*....|....*....|...
gi 489053699 234 VIFMDQ------GQIVEQNSPDE 250
Cdd:TIGR00630 901 IIDLGPeggdggGTVVASGTPEE 923
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
164-224 |
1.91e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 164 QLSGGQQQRVAIARALCMNPKVMLFDEPTSALDpemVKEVLdTMVSL---AAEGMTMICVTHEM 224
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQRL-NVARLireLAEGKYVLVVEHDL 271
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
43-235 |
8.16e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTMIR-----CINRL-EEHQKGKIVVDG------IELTNDL------------- 97
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFiEQGFCSNLSIQWgaisrlVHITRDLpgrsqrsipltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 98 KKIDEVR---------REVGMVFQHFNL------------FPHLTILENCTLAP-------------IWVRKMPKKQAEE 143
Cdd:PRK00635 689 KAFDDLRelfaeqprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNRTSIPcpsclgkrflpqvLEVRYKGKNIADI 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 144 IAMHYLERVKI----PEQANKYPG----------------QLSGGQQQRVAIARALCM---NPKVMLFDEPTSALDPEMV 200
Cdd:PRK00635 769 LEMTAYEAEKFfldePSIHEKIHAlcslgldylplgrplsSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDI 848
|
250 260 270
....*....|....*....|....*....|....*
gi 489053699 201 KEVLDTMVSLAAEGMTMICVTHEMGFARqVANRVI 235
Cdd:PRK00635 849 KALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
44-222 |
3.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 44 VLRDINLKVMRGERIVVAGPSGSGKSTMIRCINRLEEHQKGKIVVDGIELTNDLKKIdevrreVGMVFQHFNLFPHLTIL 123
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY------CTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 124 ENCTLapiWVRKMPKKQAEEIAMHYLervKIPEQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEV 203
Cdd:PRK13541 89 ENLKF---WSEIYNSAETLYAAIHYF---KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 489053699 204 LDTMVSLAAEGMTMICVTH 222
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
162-222 |
3.88e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.30 E-value: 3.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489053699 162 PGQLSGGQQQ---RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTH 222
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
165-269 |
1.02e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 165 LSGGQQQRVAIARALC--MNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICVTHEMGFArQVANRVIFMDQ--- 239
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgag 555
|
90 100 110
....*....|....*....|....*....|...
gi 489053699 240 ---GQIVEQNSPDEFFDNpQHERTRLFLSQILH 269
Cdd:PRK00635 556 ifgGEVLFNGSPREFLAK-SDSLTAKYLRQELT 587
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
141-242 |
1.23e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 141 AEEIAMHYLERVKIP-EQANKYPGQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTmvsLAAEGMTMIC 219
Cdd:PRK15064 131 AEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
90 100
....*....|....*....|...
gi 489053699 220 VTHEMGFARQVANRVIFMDQGQI 242
Cdd:PRK15064 208 ISHDRHFLNSVCTHMADLDYGEL 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-250 |
1.57e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 29 AIEITNMHKWYGEFHVLRDINLKVMRGERIVVAGPSGSGKSTMI------RCInrleehQKGKIVVdgieLTNDLKKIDE 102
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEV----LGGDMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 103 vRREVG-----MVfQHF--NLFPHLTILEN------------------------CT-LAPiwvrkmpkkqaeeiamhYLE 150
Cdd:NF033858 71 -RRAVCpriayMP-QGLgkNLYPTLSVFENldffgrlfgqdaaerrrridellrATgLAP-----------------FAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 151 RvkipeqankyP-GQLSGGQQQRVAIARALCMNPKVMLFDEPTSALDP-------EMVKevldtmvSLAAE--GMTMICV 220
Cdd:NF033858 132 R----------PaGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELID-------RIRAErpGMSVLVA 194
|
250 260 270
....*....|....*....|....*....|....
gi 489053699 221 THEM----GFARQVAnrvifMDQGQIVEQNSPDE 250
Cdd:NF033858 195 TAYMeeaeRFDWLVA-----MDAGRVLATGTPAE 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
164-220 |
1.71e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 164 QLSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAEGMTMICV 220
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
43-70 |
6.83e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 6.83e-04
10 20
....*....|....*....|....*...
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKST 70
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
165-223 |
7.17e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 7.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489053699 165 LSGGQQQRVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVsLAAEGMTMicVTHE 223
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGGVLM--VSHD 683
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-266 |
1.07e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 138 KKQAEEIAMHYLERVKI----------PEQAnkyPGQLSGGQQQRVAIARALCMN-PKVM-LFDEPTSALDPEMVKEVLD 205
Cdd:TIGR00630 455 KKIAEEVLKEIRERLGFlidvgldylsLSRA---AGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLIN 531
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489053699 206 TMVSLAAEGMTMICVTHEMGFARqVANRVIFMDQ------GQIVEQNSPDEFFDNPqHERTRLFLSQ 266
Cdd:TIGR00630 532 TLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgagehgGEVVASGTPEEILANP-DSLTGQYLSG 596
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
58-109 |
1.67e-03 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 38.67 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 58 IVVAGPSGSGKSTMIRC-INRLEEHQKGKIVV--DGIELTNDLKKIDEVRREVGM 109
Cdd:cd01131 24 VLVTGPTGSGKSTTLAAmIDYINETRSKHIITieDPIEFVHKHKKSLINQREVGR 78
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
166-244 |
1.70e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 166 SGGQQQRVAIARALCMNPKVMLFDEPTSALDpemvkevLDTMVSL-----AAEGmTMICVTHEMGFARQVANRVIFMDQG 240
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLekwlkSYQG-TLILISHDRDFLDPIVDKIIHIEQQ 222
|
....
gi 489053699 241 QIVE 244
Cdd:PRK10636 223 SLFE 226
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
43-75 |
2.41e-03 |
|
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441830 [Multi-domain] Cd Length: 189 Bit Score: 37.88 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|...
gi 489053699 43 HVLRDINLKvmrgerIVVAGPSGSGKSTMIRCI 75
Cdd:COG2229 6 VAAREITVK------IVYAGPFGAGKTTFVRSI 32
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
58-87 |
2.59e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 38.53 E-value: 2.59e-03
10 20 30
....*....|....*....|....*....|....
gi 489053699 58 IVVAGPSGSGKST----MIRCINRleeHQKGKIV 87
Cdd:COG2805 128 VLVTGPTGSGKSTtlaaMIDYINE---TRAKHII 158
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
43-71 |
2.72e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.72e-03
10 20
....*....|....*....|....*....
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKSTM 71
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
164-221 |
4.64e-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: 37.62 E-value: 4.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489053699 164 QLSGGQQQRVAIARALCMN---PKVM-LFDEPTSALDPEMVKEVLDTMVSLaAEGMTMICVT 221
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdPAPFyLFDEIDAALDAQYRTAVANMIKEL-SDGAQFITTT 218
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
58-88 |
6.07e-03 |
|
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are bacterial conjugation proteins involved in type IV secretion (T4S) systems, versatile bacterial secretion systems mediating transport of protein and/or DNA. They are present in gram-negative and gram-positive bacteria, as well as archaea. They form hexameric rings and belong to the RecA-like NTPases superfamily, which also includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases.
Pssm-ID: 410871 [Multi-domain] Cd Length: 144 Bit Score: 36.43 E-value: 6.07e-03
10 20 30
....*....|....*....|....*....|.
gi 489053699 58 IVVAGPSGSGKSTMIRCINRLEEHQKGKIVV 88
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVII 32
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
166-239 |
6.50e-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: 37.19 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489053699 166 SGGQQQRVAIARALCMNPKVMLFDEPTSA-----LDPEM------VKEVLDTMVSLAAE-----GMTMICVTHEMGFARQ 229
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmiRDERMqalvskDKEPITPFVDRVRSlyddlGVSTILVVGGSGDYLD 238
|
90
....*....|
gi 489053699 230 VANRVIFMDQ 239
Cdd:pfam09818 239 VADTVILMDE 248
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
43-70 |
8.23e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.36 E-value: 8.23e-03
10 20
....*....|....*....|....*...
gi 489053699 43 HVLRDINLKVMRGERIVVAGPSGSGKST 70
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
45-102 |
8.37e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 36.53 E-value: 8.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489053699 45 LRDINLKVMRGER--IVVAGPSGSGKSTMIR-CINRLEEHQKGKIVVDGIElTNDLKKIDE 102
Cdd:pfam01637 8 LKELEEWAERGPNliYVIYGPEGCGKTALLReSIENLLDLGYYVIYYDPLR-RYFISKLDR 67
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
163-226 |
8.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 37.72 E-value: 8.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489053699 163 GQLSGGQQQ------RVAIARALCMNPKVMLFDEPTSALDPEMVKEVLDTMVSLAAE-----GMTMICVTHEMGF 226
Cdd:TIGR00606 1198 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqrNFQLLVITHDEDF 1272
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
58-108 |
9.89e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.58 E-value: 9.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489053699 58 IVVAGPSGSGKSTMIRcinrleEHQKGKIVVDgieltndlkkIDEVRREVG 108
Cdd:COG4639 5 VVLIGLPGSGKSTFAR------RLFAPTEVVS----------SDDIRALLG 39
|
|
| |
